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Information on EC 2.3.1.20 - diacylglycerol O-acyltransferase
for references in articles please use BRENDA:EC2.3.1.20
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.20 diacylglycerol O-acyltransferase
IUBMB Comments
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
The enzyme appears in viruses and cellular organisms
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
- phosphatidate
- glycerolipids
-
lipolysis
-
oleaginous
- glycerol-3-phosphate
- chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
-
insig1
- biofuel production
-
oleosins
-
cholinephosphotransferase
- elovl6
- drug development
-
triacylglyceride
-
holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
-
lipin
- lpaat
-
ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
-
steryl
-
kennedy
showSynonyms
dgat1, dgat2, dgat, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol o-acyltransferase, dgat-1, monoacylglycerol acyltransferase, acyl-coa:diacylglycerol acyltransferase, diacylglycerol acyltransferase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-diacylglycerol acyltransferase
-
-
-
-
2 diacylglycerol acyltransferase
acetyl coenzyme A:diacylglycerol acyltransferase
acyl CoA:diacylglycerol acyltransferase
acyl CoA:diacylglycerol acyltransferase 1
acyl CoA:diacylglycerol acyltransferase-2
acyl coenzyme A:diacylglycerol acyltransferase 1
acyl-CoA:1,2-diacylglycerol O-acyltransferase
acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase
-
-
-
-
acyl-CoA:diacylglycerol acyltransferase
acyl-CoA:diacylglycerol acyltransferase 1
acyl-CoA:diacylglycerol acyltransferase 2
acyltransferase, diacylglycerol
-
-
-
-
AtfA
enzyme possesses both wax ester synthase and diacylglycerol:acyl-coenzyme A acyltransferase (DGAT) activities
bifunctional DGAT/wax ester synthase
BnaDGAT1
DAG acyltransferase
DAGAT
DGA1
Dga1p
DGA2
DGAT
DGAT type 2
DGAT-1
DGAT1
DGAT1.a
DGAT1A
DGAT1B
DGAT2
DGAT2.1
DGAT2.2
DGAT2.3
DGAT2A
DGAT2b
DGAT3
DGTT
diacylglycerol acyltransferase
diacylglycerol acyltransferase 1
diacylglycerol acyltransferase 2
diacylglycerol acyltransferase 3
diacylglycerol acyltransferase-1
diacylglycerol acyltransferase-2
diacylglycerol acyltransferase1
diacylglycerol acyltransferase2
diacylglycerol O-acyltransferase 2
diglyceride acyltransferase
-
-
-
-
diglyceride O-acyltransferase
-
-
-
-
EC 2.3.1.124
-
-
formerly
-
FBPA
GhDGAT3D
HpDGAT2A
HpDGAT2B
HpDGAT2D
HpDGAT2E
MaDGAT
MaDGAT1A/1B/1C
MaDGAT1B
MaDGAT2
MaDGAT2A
MaDGAT2A/2B
MGAT
NeoDGAT2
palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
-
-
-
-
RtDGATa
RtDGATb
Rv3088 (TGS4)
Rv3130c (TGS1)
Rv3234c (TGS3)
Rv3371
Rv3734 (TGS2)
SAV7256
enzyme possesses both wax ester synthase and diacylglycerol:acyl-coenzyme A acyltransferase (DGAT) activities
TAG synthase
tDGAT
TrWSD4
TrWSD5
type 1 acyl-CoA:diacylglycerol acyltransferase
type 1 diacylglycerol acyltransferase
type 2 acyl-CoA:diacylglycerol acyltransferase
type 2 DGAT
type-2 diacylglycerol acyltransferase
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
wax ester synthase
wax ester synthase/acyl-CoA diacylglycerol acyltransferase
wax ester synthase/acyl-CoA:diacylglycerol acyltransferase
wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1
bifunctional enzyme
wax ester synthase/triacylglycerol:acylCoA acyltransferase
WS/DGAT
WS2
WSD4
WSD5
YALI0D07986g
YALI0E32769g
additional information
DGAT
-
-
-
-
DGAT1
-
-
-
-
DGAT1A
-
-
-
-
DGAT2
-
-
-
-
DGAT2A
-
-
-
-
diacylglycerol acyltransferase
-
-
-
-
diacylglycerol acyltransferase
-
-
type 2 acyl-CoA:diacylglycerol acyltransferase
-
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
-
-
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
-
-
-
wax ester synthase/acyl-CoA diacylglycerol acyltransferase
-
wax ester synthase/acyl-CoA:diacylglycerol acyltransferase
-
wax ester synthase/triacylglycerol:acylCoA acyltransferase
-
-
additional information
-
the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase, MGAT, gene family
additional information
cf. EC 2.3.1.75, the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase, DGAT, 2 gene superfamily
additional information
cf. EC 2.3.1.75, the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase, DGAT, 2 gene superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
-
-
-
-
acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
the conserved sequence 161HPHG164 is important for activity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
diacylglycerol and triacylglycerol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
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CAS REGISTRY NUMBER
COMMENTARY
9029-98-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycerol + erucoyl-CoA
1,2-diacyl-3-erucoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacyl-sn-glycerol + oleoyl-CoA
1,2-diacyl-3-oleoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + erucoyl-CoA
1,2-diacyl-3-erucoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + oleoyl-CoA
1,2-diacyl-3-oleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + palmitoyl-CoA
1,2-diacyl-3-palmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + stearoyl-CoA
1,2-diacyl-3-stearoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolein + alpha-linolenoyl-CoA
1,2-dilinoleoyl-3-alpha-linolenoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolein + linoleoyl-CoA
1,2,3-trilinoleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolein + oleoyl-CoA
1,2-dilinoleoyl-3-oleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolein + palmitoyl-CoA
1,2-dilinoleoyl-3-palmitoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolenin + alpha-linolenoyl-CoA
1,2-dilinolenoyl-3-alpha-linolenoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolenin + linoleoyl-CoA
1,2-dilinolenoyl-3-linoleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolenin + oleoyl-CoA
1,2-dilinolenoyl-3-oleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dilinolenin + palmitoyl-CoA
1,2-dilinolenoyl-3-palmitoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diolein + alpha-linolenoyl-CoA
1,2-dioleoyl-3-alpha-linolenoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diolein + linoleoyl-CoA
1,2-dioleoyl-3-linoleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diolein + oleoyl-CoA
1,2,3-trioleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dioleoyl-sn-glycerol + oleoyl-CoA
triolein + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoyl-sn-glycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoylglycerol + arachidonoyl-CoA
1,2-dioleoyl-3-arachidonoylglycerol + CoA
-
Substrates: about 8% of the activity with palmitoyl-CoA
Products: -
Products: -
?
1,2-dioleoylglycerol + linoleoyl-CoA
1,2-dioleoyl-3-linoleoylglycerol + CoA
-
Substrates: about 12% of the activity with palmitoyl-CoA
Products: -
Products: -
?
1,2-dioleoylglycerol + stearoyl-CoA
1,2-dioleoyl-3-stearoylglycerol + CoA
-
Substrates: about 10% of the activity with palmitoyl-CoA
Products: -
Products: -
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
tripalmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycerol + oleoyl-CoA
1,2-dipalmitoyl-3-oleoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycerol + palmitoyl-CoA
tripalmitin + CoA
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-sn-glycerol + stearoyl-CoA
1,2-dipalmitoyl-3-stearoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diricinoleoyl-sn-glycerol + ricinoleoyl-CoA
triricinolein + CoA
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoylglycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 1,2-diacetyl-sn-glycerol
CoA + triacetylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
acyl-CoA + 1,2-didecanoylglycerol
CoA + 3-acyl-1,2-didecanoylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-dihexanoylglycerol
CoA + 3-acyl-1,2-dihexanoylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-dilauroylglycerol
CoA + 3-acyl-1,2-dilauroylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-dimyristoylglycerol
CoA + 3-acyl-1,2-dimyristoylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-dioctanoylglycerol
CoA + 3-acyl-1,2-dioctanoylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-dipalmitin
CoA + 3-acyl-1,2-dipalmitoylglycerol
-
Substrates: no acceptor
Products: -
Products: -
?
acyl-CoA + 1,2-dipalmitoylglycerol
CoA + 3-acyl-1,2-dipalmitoylglycerol
-
Substrates: membrane bound 1,2-dipalmitoylglycerol
Products: -
Products: -
?
acyl-CoA + 1,2-hexadec-9-enoyl-sn-glycerol
CoA + 1,2-dihexadec-9-enoyl-3-acylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1-decanol
? + CoA
Substrates: at 48% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + 1-oleoyl-2-palmitoyl-sn-glycerol
CoA + 1-oleoyl-2-palmitoyl-3-acylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1-palmitoyl-2-oleoyl-sn-glycerol
CoA + 1-palmitoyl-2-oleoyl-3-acylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2,3-dioleoyl-sn-glycerol
CoA + 1-acyl-2,3-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-cyclohexylethanol
? + CoA
Substrates: at 45% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + 2-decanol
? + CoA
Substrates: at 39% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + 2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-oleoylglycerol
CoA + 3-acyl-2-oleoylglyerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 4-decanol
? + CoA
Substrates: at 15.6% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + cyclododecanol
? + CoA
Substrates: at 80% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + cyclohexandiol
? + CoA
Substrates: at 4.1% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + cyclohexanol
? + CoA
Substrates: at 32% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + cyclohexanone oxime
? + CoA
Substrates: at 5.2% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + lysophosphatidylcholine
CoA + acyllysophosphatidylcholine
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + phenol
? + CoA
Substrates: at 4.1% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + phenylethanol
? + CoA
Substrates: at 99% of the activity with hexanol
Products: -
Products: -
?
acyl-CoA + rac-1,2-diacetylglycerol
CoA + 3-acyl-rac-1,2-diacetylglycerol
-
Substrates: no acceptor
Products: -
Products: -
?
acyl-CoA + rac-1,2-dibutyrylglycerol
CoA + 3-acyl-rac-1,2-dibutyrylglycerol
-
Substrates: no acceptor
Products: -
Products: -
?
alpha-linolenoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linolenoyl-sn-glycerol
Substrates: 100% activity
Products: -
Products: -
?
caproyl-CoA + 1,2-dicaproyl-sn-glycerol
CoA + tricaproylglycerol
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-decanoylglycerol
-
Substrates: saturated fatty acyl-CoAs from C-8 to C-18 with decanoyl-CoA as the best
Products: -
Products: -
?
dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
docosahexaenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-docosahexaenoylglycerol
Substrates: -
Products: -
Products: -
?
eicosapentaenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-eicosapentaenoylglycerol
Substrates: -
Products: -
Products: -
?
erucoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 3-erucoyl-1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + 1,2-dipalmitoyl glycerol
coenzyme A + 1,2-dipalmitoyl-3-hexanoyl glycerol
-
Substrates: -
Products: -
Products: -
r
lauryl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-lauryl-glycerol
-
Substrates: -
Products: -
Products: -
?
lignoceryl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-lignocerylglycerol
Substrates: -
Products: -
Products: -
?
linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linolenoyl-glycerol
Substrates: -
Products: -
Products: -
?
linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoyl-glycerol
Substrates: -
Products: -
Products: -
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-linoleoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 3-linoleoyl-1,2-dioleoylglycerol
-
Substrates: i.e. diolein
Products: -
Products: -
?
N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)]aminopalmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 3-[N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)]-16-aminopalmitoyl]-1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + 1,2-di-(cis-9-octadecenoyl)-sn-glycerol
CoA + 1,2-di-(cis-9-octadecenoyl)-3-octanoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
octodecyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-octodecylglycerol + CoA
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-sn-glycerol
Substrates: BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA. The lipidated BnaDGAT1 exhibited a sigmoidal response to increasing concentrations of oleoyl-CoA
Products: -
Products: -
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
triolein + CoA
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-dioleoylglycerol
CoA + 1,2,3-trioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-dipalmitoylglycerol
CoA + 3-oleoyl-1,2-dipalmitoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diricinoloylglycerol
CoA + 3-oleoyl-1,2-diricinoloylglycerol
Substrates: best substrate
Products: -
Products: -
?
oleoyl-CoA + 1,2-divernoloyl-sn-glycerol
CoA + 1,2-divernoloyl-3-oleoyl-sn-glycerol
Substrates: oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
Products: -
Products: -
?
palmitoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-palmitoleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
palmitoleoyl-CoA + 1,2-dipalmitoleoyl-sn-glycerol
CoA + tripalmitoleoylglycerol
-
Substrates: preferred substrate for isoform DGAT2
Products: -
Products: -
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-palmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2,3-tripalmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1,2-dipalmitoylglycerol
CoA + tripalmitin
Substrates: approximately 10fold lower level of diacylglycerol acyltransferase activity
Products: -
Products: -
?
palmitoyl-CoA + 1,2-distearin
CoA + 3-palmitoyl-1,2-distearoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: usage of fluorescent NBD-tagged palmitoyl-CoA as substrate
Products: -
Products: -
?
palmitoyl-CoA + 1,3-diolein
CoA + 1,3-dioleoyl-2-palmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1,3-dipalmitin
CoA + tripalmitin
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1-monoolein
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1-monopalmitin
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1-monostearin
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + didecanoylglycerol
CoA + 1,2-didecanoyl-3-palmitoylglycerol
-
Substrates: i.e. dicaprin
Products: -
Products: -
?
palmitoyl-CoA + dihexanoylglycerol
CoA + dihexanoyl-palmitoylglycerol
-
Substrates: i.e. dicaproin
Products: -
Products: -
?
palmitoyl-CoA + dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: membrane-bound dipalmitoylglycerol
Products: -
Products: -
?
palmitoyl-CoA + hexadecanol
hexadecyl palmitate + CoA
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
ricinoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-ricinoleoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
ricinoleoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
1,2-dipalmitoyl-3-ricinoleoyl-sn-glycerol + CoA
-
Substrates: prefers acyl acceptor 1,2-dioleoyl-sn-glycerol over 1,2-dipalmitoyl-sn-glycerol
Products: -
Products: -
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sn-1,2-diacylglycerol + erucoyl-CoA
triacylglycerol + CoA
-
Substrates: i.e. a 22:1cisDELTA13-CoA
Products: -
Products: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-stearoylglycerol + CoA
Substrates: -
Products: -
Products: -
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vernoloyl-CoA + 1,2-divernoloyl-sn-glycerol
CoA + trivernoloyl-sn-glycerol
Substrates: oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: role in leaf metabolism, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT catalyzes the transfer of an acyl moiety between two DAG molecules to form triacylglycerol and monoacylglycerol
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Cuphea sp.
-
Substrates: microsomal DGAT from Cuphea exhibits high activity toward diacylglycerols containing unusual fatty acids, e.g. lauric acids, at both sn-1 and sn-2 positions, acyl-CoA specificity, overview
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: acyl-CoA specificity, overview
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: acyl-CoA specificity, overview
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: acyl-CoA specificity, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: microsomal DGAT from castor bean exhibited high activity toward diacylglycerols containing unusual fatty acids, e.g. ricinoleic acids, at both sn-1 and sn-2 positions, acyl-CoA specificity, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: acyl-CoA specificity, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: acyl-CoA specificity, no acylation activity with phosphoatidylcholine or oleic acid, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT1 and DGAT2 are two unrelated enzymes that catalyze the committed step in triacylglycerol biosynthesis
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT1 catalyzes the committed step in triacylglycerol biosynthesis
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT2 catalyzes the committed step in triacylglycerol biosynthesis
Products: -
Products: -
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1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: acyl-CoA specificity, overview
Products: -
Products: -
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1,2-diolein + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-diolein + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
Substrates: about 90% of the activity with palmitoyl-CoA
Products: -
Products: -
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1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-glycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-glycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
rac-tripalmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
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1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
rac-tripalmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Cuphea sp.
-
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
2,3-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
2,3-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
Substrates: low activity with the DAG substrate
Products: -
Products: -
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acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
E2RDN4
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Haematococcus lacustris UTEX 2505
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Lobosphaera incisa SAG 2468
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
KY859195, A0A2D2CI94
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Nannochloropsis oceanica CCAP 849/10
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: RtDGATa has obvious preference for monounsaturated fatty acids. RtDGATa is active with C16:1 and C18:1 and shows poor activity for C16:0, C18:0, C18:2 and C18:3
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: isozyme RtDGATb prefers unsaturated fatty acids over saturated fatty acids, but not C18:3
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: RtDGATa has obvious preference for monounsaturated fatty acids. RtDGATa is active with C16:1 and C18:1 and shows poor activity for C16:0, C18:0, C18:2 and C18:3
Products: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: isozyme RtDGATb prefers unsaturated fatty acids over saturated fatty acids, but not C18:3
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
M1E7W9, XP_011098009
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Thraustochytrium roseum ATCC28210
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: isoform DGAT2b is catalytically more active than DGAt2a
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: isoform DGAT2b is catalytically more active than DGAt2a
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: functional complementation assay using triacylglycerol-deficient yeast (Saccharomyces cerevisiae) mutant H1246 demonstrates that GmDGAT3-2 fully restores triacylglycerol biosynthesis in the yeast and preferentially incorporates monounsaturated fatty acids, especially oleic acid (C18:1) into triacylglycerols
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: fatty acid profile assays reveal that HpDGAT2A prefers monounsaturated fatty acyl-CoAs for triacylglycerol synthesis in yeast cells, and shows a preference for polyunsaturated fatty acyl-CoAs based on their feeding strategy
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: overexpressing HpDGAT1 in triacylglycerol-deficient Saccharomyces cerevisiae H1246 reveals that HpDGAT1 exhibits a high substrate preference for monounsaturated fatty acyl-CoAs (C16:1 and C18:1) and polyunsaturated fatty acyl-CoAs (C18:2n6 and C18:3n3)
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: fatty acid profile assays reveal that HpDGAT2D prefers monounsaturated fatty acyl-CoAs for triacylglycerol synthesis in yeast cells, and shows a preference for polyunsaturated fatty acyl-CoAs based on their feeding strategy
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: fatty acid profile assays reveal that HpDGAT2E prefers monounsaturated fatty acyl-CoAs for triacylglycerol synthesis in yeast cells, and shows a preference for polyunsaturated fatty acyl-CoAs based on their feeding strategy
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Haematococcus lacustris FACHB-712
Substrates: overexpressing HpDGAT1 in triacylglycerol-deficient Saccharomyces cerevisiae H1246 reveals that HpDGAT1 exhibits a high substrate preference for monounsaturated fatty acyl-CoAs (C16:1 and C18:1) and polyunsaturated fatty acyl-CoAs (C18:2n6 and C18:3n3)
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Lobosphaera incisa SAG 2468
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: in Saccharomyces cerevisiae H1246MaDGAT1A prefers C16:1 among monounsaturated fatty acids, MaDGAT1B prefers C16:0 among saturated fatty acids, and MaDGAT2A/2B prefers C18:0 among saturated fatty acids. Under exogenous addition of polyunsaturated fatty acids, MaDGAT1A and 2A preferentially assembled linoleic acid into TAG, and MaDGAT2B had substrate selectivity for eicosapentaenoic and linoleic acids in omega-6 polyunsaturated fatty acids. In vitro, MaDGAT1A shows no obvious acyl-CoA selectivity and MaDGAT1B prefers C20:5-CoA. MaDGAT1A/1B prefers C18:1/C18:1-DAG compared with C20:4/C20:4-DAG
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: in Saccharomyces cerevisiae H1246MaDGAT1A prefers C16:1 among monounsaturated fatty acids, MaDGAT1B prefers C16:0 among saturated fatty acids, and MaDGAT2A/2B prefers C18:0 among saturated fatty acids. Under exogenous addition of polyunsaturated fatty acids, MaDGAT1A and 2A preferentially assembled linoleic acid into TAG, and MaDGAT2B had substrate selectivity for eicosapentaenoic and linoleic acids in omega-6 polyunsaturated fatty acids. In vitro, MaDGAT1A shows no obvious acyl-CoA selectivity and MaDGAT1B prefers C20:5-CoA. MaDGAT1A/1B prefers C18:1/C18:1-DAG compared with C20:4/C20:4-DAG
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: isoforms DGAT1 and DGAT2 Can compensate for each other to synthesize triacylglycerol
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: PrDGAT3 has a high diacylglycerol acyltransferase activity and substrate selection for unsaturated fatty acids, particularly linoleic acid and alpha-linolenic acid
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: PtDGAT2b exhibits a broad acyl-CoA preference with both di-16:0-diacylglycerol and di-18:1-diacylglycerol, whereas di-18:1-diacylglycerol is favored. The highest preference for acyl donors is observed for 16:1-CoA, 10:0-CoA and 12:0-CoA. PtDGAT2b very efficiently utilizes CoA-conjugated omega-3 long-chain-polyunsaturated fatty acids (stearidonic acid, eicosatetraenoic acid and EPA)
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: SbDGAT1: high substrate preference towards 16:0, 16:1 and 18:1 fatty acids
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: saturated fatty acyl-CoAs from C-4 to C-18
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: broad range of donors from C-12 to C-22, broad range of acceptors from C12 to C-22
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: enzyme catalyzing the final reaction in the sn-glycerol-3-phosphate pathway leading to TAG
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: acceptors: 1,2-diacylglycerol containing oleic acid and 1,2-diacylglycerol containing capric acid
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: last step of triacylglycerol synthesis
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
Substrates: acceptors: overview
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: DGAT1 is more involved in fat absorption in the intestine and DGAT2 plays important role in assembly of de novo synthesized fatty acids into VLDL particles in liver
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: endogenously and exogenously synthesized diacylglycerol
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: acyl-donors: broad specificity, saturated, mono-, di- and tetraenoic thioesters
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: saturated fatty acyl-CoAs from C-8 to C-12
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: 2,3-diacylglycerol is acylated at 20% the rate of 1,2-isomer
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: last reaction in triacylglycerol synthesis
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: endogenous 1,2-diacylglycerol
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
Products: -
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acyl-CoA + 1,2-dilinoleoyl-sn-glycerol
CoA + 1,2-dilinoleoyl-3-acylglycerol
Substrates: low activity with the DAG substrate
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acyl-CoA + 1,2-dilinoleoyl-sn-glycerol
CoA + 1,2-dilinoleoyl-3-acylglycerol
Substrates: -
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acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
Substrates: low activity with the DAG substrate
Products: -
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acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
Substrates: -
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acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-acylglycerol
Substrates: low activity with the DAG substrate
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acyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-acylglycerol
Substrates: -
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acyl-CoA + 1,3-dioleoyl-sn-glycerol
CoA + 1,3-dioleoyl-2-acylglycerol
Substrates: low activity with the DAG substrate
Products: -
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acyl-CoA + 1,3-dioleoyl-sn-glycerol
CoA + 1,3-dioleoyl-2-acylglycerol
Substrates: -
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acyl-CoA + 1,3-dioleoylglycerol
CoA + 2-acyl-1,3-dioleoylglycerol
-
Substrates: no acceptor
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acyl-CoA + 1,3-dioleoylglycerol
CoA + 2-acyl-1,3-dioleoylglycerol
-
Substrates: -
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acyl-CoA + rac-1,2-dioleoylglycerol
CoA + 3-acyl-rac-1,2-dioleoylglycerol
-
Substrates: -
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acyl-CoA + rac-1,2-dioleoylglycerol
CoA + 3-acyl-rac-1,2-dioleoylglycerol
-
Substrates: -
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acyl-CoA + sn-1,2-diolein
CoA + acyl-sn-1,2-diolein
-
Substrates: -
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acyl-CoA + sn-1,2-diolein
CoA + acyl-sn-1,2-diolein
-
Substrates: -
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alpha-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-alpha-linolenoylglycerol
Substrates: best acyl-CoA substrate
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alpha-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-alpha-linolenoylglycerol
Substrates: -
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arachidonoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-arachidnoylglycerol
KY859195, A0A2D2CI94
Substrates: -
Products: -
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arachidonoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-arachidnoylglycerol
Substrates: -
Products: -
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arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
Substrates: -
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arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
-
Substrates: -
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butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
Substrates: -
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butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
Substrates: -
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butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
Substrates: -
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butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
Substrates: -
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dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
KY859195, A0A2D2CI94
Substrates: -
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dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
Substrates: -
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erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Substrates: -
Products: -
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erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Substrates: Jet Neuf enzyme displays an enhanced specificity for erucoyl-CoA over oleoyl-CoA
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erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Substrates: -
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erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Substrates: -
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erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Substrates: -
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gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
Substrates: -
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gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
KY859195, A0A2D2CI94
Substrates: -
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gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
Substrates: -
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hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
Substrates: preferred acyl-CoA substrate
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hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
Substrates: -
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hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
Substrates: best acyl-CoA subbstrate
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lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
Substrates: -
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lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
Substrates: -
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lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
Substrates: -
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lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
Substrates: -
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lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
Substrates: -
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lauroyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-lauroyl-sn-glycerol
Substrates: -
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lauroyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-lauroyl-sn-glycerol
Substrates: -
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lauroyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-lauroyl-sn-glycerol
Substrates: -
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linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
KY859195, A0A2D2CI94
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
Substrates: -
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linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
Substrates: -
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linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
Substrates: poor donor
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
Substrates: -
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
Substrates: -
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
Substrates: -
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
Substrates: -
Products: -
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linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
Substrates: -
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myristoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-myristoylglycerol
-
Substrates: -
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myristoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-myristoylglycerol
-
Substrates: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
Substrates: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: assay with radioactive oleoyl-CoA and DAG from microsome preparation of the recombinant yeast cells
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: assay with radioactive oleoyl-CoA and DAG from microsome preparation of the recombinant yeast cells
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: low activity
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oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: -
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oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
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oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
Substrates: -
Products: -
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Substrates: about 85% activity compared to alpha-linolenoyl-CoA
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Haematococcus lacustris UTEX 2505
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
Substrates: -
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
Substrates: oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
Substrates: -
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: i.e. diolein, at 34% the rate of the acylation with stearoyl-CoA
Products: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
Substrates: -
Products: -
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?
oleoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
Substrates: -
Products: -
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?
oleoyl-CoA + diolein
CoA + triolein
Substrates: -
Products: -
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?
oleoyl-CoA + diolein
CoA + triolein
Substrates: -
Products: -
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?
oleoyl-CoA + sn-1,2-dioleoylglycerol
triolein + CoA
-
Substrates: -
Products: -
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?
oleoyl-CoA + sn-1,2-dioleoylglycerol
triolein + CoA
-
Substrates: -
Products: -
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?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
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?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
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?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Substrates: best substrate
Products: -
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palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Substrates: low activity
Products: -
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palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: best substrate
Products: -
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palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: low activity
Products: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
Substrates: -
Products: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
Substrates: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Substrates: good acyl-CoA substrate
Products: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Substrates: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Substrates: high activity
Products: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: high activity
Products: -
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?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Substrates: -
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palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Thraustochytrium roseum ATCC28210
-
Substrates: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
Substrates: diacylglycerol diluted in ethanol
Products: -
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palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: about 85% activity compared to alpha-linolenoyl-CoA
Products: -
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palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
Substrates: -
Products: -
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?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
Substrates: -
Products: -
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palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
Substrates: -
Products: -
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palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
Substrates: -
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palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
Substrates: i.e. diolein
Products: -
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palmitoyl-CoA + 1,2-dipalmitin
CoA + tripalmitin
-
Substrates: -
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palmitoyl-CoA + 1,2-dipalmitin
CoA + tripalmitin
-
Substrates: -
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palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + tripalmitoylglycerol
-
Substrates: preferred substrate for isoform DGAT1
Products: -
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palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + tripalmitoylglycerol
-
Substrates: -
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: the final step in triacylglycerol synthesis is catalyzed by the acyl-CoA:diacylglycerol acyltransferase enzymes, DGAT1 and DGAT2
Products: -
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: the enzyme contains a neutral lipid binding sequence 80FLVLGVAC87 residing in the first transmembrane domain
Products: -
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stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
Substrates: -
Products: -
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?
stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
Substrates: high activity
Products: -
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stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: high activity
Products: -
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?
stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
-
Substrates: weak donor
Products: -
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stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
-
Substrates: weak donor
Products: -
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?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
Substrates: -
Products: -
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?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
Substrates: fluorescent assay method using NBD-tagged diglycerol substrate
Products: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
Substrates: fluorescent assay method using NBD-tagged diglycerol substrate
Products: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
Substrates: fluorescent assay method using NBD-tagged diglycerol substrate
Products: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
Substrates: -
Products: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
Substrates: -
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
Substrates: i.e. diolein
Products: -
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additional information
?
-
Substrates: ATfA exhibits a clear preference for the acylation of the sn-2 position of sn-1,2-dipalmitoylglycerol rather than the sn-2 position of sn-1,3-dipalmitoylglycerol
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additional information
?
-
Substrates: enzyme also has acyl-CoA-monoacylglycerol acyltransferase activity, sn-1 and sn-3 positions are accepted with higher specificity than sn-2 position
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additional information
?
-
-
Substrates: the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
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additional information
?
-
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Substrates: the bifunctional enzyme catalyzes the reactions of the diacylglycerol transferase, EC 2.3.1.20, and of the wax synthase, EC 2.3.1.75
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additional information
?
-
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Substrates: the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
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additional information
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Substrates: rate of activity is highly dependent on acyl composition with highest activities for acyl groups containing several double bonds, epoxy, or hydroxy groups. Enzyme uses both sn-positions of phosphatidylcholine with 3fold preference for sn-2 position
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additional information
?
-
-
Substrates: acyl-CoA specificity, overview
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additional information
?
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Substrates: acyl-CoA specificity, overview
Products: -
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additional information
?
-
-
Substrates: bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
Products: -
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additional information
?
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Substrates: bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
Products: -
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additional information
?
-
Substrates: bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
Products: -
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additional information
?
-
Substrates: bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
Products: -
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additional information
?
-
-
Substrates: substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
Products: -
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additional information
?
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Substrates: substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
Products: -
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additional information
?
-
Substrates: substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
Products: -
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additional information
?
-
-
Substrates: acyl-CoA specificity, overview
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additional information
?
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Substrates: acyl-CoA specificity, overview
Products: -
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additional information
?
-
Substrates: acyl-CoA specificity, overview
Products: -
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additional information
?
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Substrates: interaction of CoA and oleoyl-CoA with the cytoplasmic N-terminal region (BnaDGAT11-113) of isoform BnaC.DGAT1.a. Truncated forms BnaDGAT11-113 and BnaDGAT11-80 interact with oleoyl-CoA or CoA with micromolar affinity, docking study and kinetics. The N-terminal domain of BnaDGAT1 has a higher affinity for thioester than free CoA. Interestingly, BnaDGAT11-80 also interacts with both ligands but with lower affinity. Ligand binding results in gain of secondary structure in mutants BnaDGAT11-113 and BnaDGAT11-80
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additional information
?
-
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Substrates: interaction of CoA and oleoyl-CoA with the cytoplasmic N-terminal region (BnaDGAT11-113) of isoform BnaC.DGAT1.a. Truncated forms BnaDGAT11-113 and BnaDGAT11-80 interact with oleoyl-CoA or CoA with micromolar affinity, docking study and kinetics. The N-terminal domain of BnaDGAT1 has a higher affinity for thioester than free CoA. Interestingly, BnaDGAT11-80 also interacts with both ligands but with lower affinity. Ligand binding results in gain of secondary structure in mutants BnaDGAT11-113 and BnaDGAT11-80
Products: -
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additional information
?
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Substrates: although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
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additional information
?
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Substrates: although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
Products: -
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additional information
?
-
-
Substrates: although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
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additional information
?
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Substrates: relative increase in activity of microsomal BnaDGAT1, BnaDGAT181-501, and BnaDGAT2 at different concentrations of oleoyl-CoA upon addition of 18:1/18:1-phosphatidate in the reaction mixture. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA, kinetics, overview
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additional information
?
-
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Substrates: relative increase in activity of microsomal BnaDGAT1, BnaDGAT181-501, and BnaDGAT2 at different concentrations of oleoyl-CoA upon addition of 18:1/18:1-phosphatidate in the reaction mixture. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA, kinetics, overview
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additional information
?
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Substrates: the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
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additional information
?
-
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Substrates: the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
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additional information
?
-
-
Substrates: no activity with sn-1,3-diacylglycerols, water-soluble diacylglycerols, including rac-1,2-diacetylglycerol and rac-1,2-dibutyrylglycerol, are poor substrates of DGAT from safflower seeds, acyl-CoA specificity, overview
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additional information
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
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Substrates: distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
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Substrates: isozyme CzDGAT2C displays typical DGAT activity
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Substrates: isozyme CzDGAT2C displays typical DGAT activity
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Substrates: isozyme CzDGAT2C displays typical DGAT activity
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Substrates: isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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Substrates: isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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Substrates: isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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Substrates: the enzyme exhibits substrate preference for two unsaturated fatty acids (UFAs), palmitoleic acid (C16:1) and oleic acid (C18:1)
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Substrates: isozyme CeDGAT2b from Cyperus esculentus might have a preference for unsaturated fatty acids such as oleic acid as substrates for the production of triacylglycerol (TAG) in tubers
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Substrates: increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
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Substrates: substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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Substrates: substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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Substrates: substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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Substrates: substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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Substrates: substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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Substrates: substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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Substrates: the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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Substrates: the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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Haematococcus lacustris UTEX 2505
Substrates: the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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Substrates: the multifunctional enzyme plays an important role in lipid metabolism in human skin
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Substrates: the enzyme also performs the reaction of the retinol O-fatty-acyltransferase, EC 2.3.1.76
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Substrates: DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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Substrates: enzyme displays striking preference to palmitoyl-CoA and oleoyl-CoA as acyl donors and utilizes 1,2-diacylglycerol as acceptor
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Substrates: the enzyme interacts with monoacylglycerol acyltransferase-2
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Substrates: acyl-CoA specificity, overview
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Substrates: co-expressing flax diacylglycerol acyltransferase1-1 (DGAT1-1) and acyl-CoA:lysophosphatidylcholine acyltransferase1 (LPCAT1) in a yeast quintuple mutant significantly increases 18-carbon polyunsaturated fatty acids in triacylglycerol with a concomitant decrease of 18-carbon polyunsaturated fatty acids in phospholipid. The specific activity of overall LPCAT1 and DGAT1-1 coupling process exhibited a preference for transferring 14C-labeled linoleoyl or linolenoyl than oleoyl moieties from the sn-2 position of phosphatidylcholine to triacylglycerol
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Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Lobosphaera incisa SAG 2468
Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Lobosphaera incisa SAG 2468
Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Lobosphaera incisa SAG 2468
Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Lobosphaera incisa SAG 2468
Substrates: recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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Substrates: the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
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Substrates: the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
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Substrates: the enzyme shows very low activity with ethanol, methanol, butanol, and glycerol
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KY859195
Substrates: substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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Substrates: substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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Substrates: substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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KY859195
Substrates: substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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Substrates: substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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Substrates: substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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Substrates: DGAT is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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Substrates: DGAT is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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Substrates: DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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Substrates: DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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Substrates: DGAT1 is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
?
-
Substrates: DGAT1 is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
Products: -
Products: -
?
additional information
?
-
Substrates: calnexin is a DGAT2-interacting protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: calnexin is a DGAT2-interacting protein
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
Products: -
Products: -
?
additional information
?
-
-
Substrates: increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: DGAT3 protein has two catalytic domains: a wax ester synthase-like acyl-CoA acyltransferase domain and a bacteria-specific acyltransferase domain and shows a significant preference to endogenous benzeneacetic acid and octadecenoic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
Products: -
Products: -
?
additional information
?
-
Substrates: in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
Products: -
Products: -
?
additional information
?
-
Substrates: in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with sn-1,3-diacylglycerols, acyl-CoA specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers unsaturated fatty acids over saturated ones
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers unsaturated fatty acids over saturated ones
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme substrate specificities, overview
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme substrate specificities, overview
Products: -
Products: -
?
additional information
?
-
Rhodotorula toruloides CGMCC 2.1389
Substrates: isozyme substrate specificities, overview
Products: -
Products: -
?
additional information
?
-
Rhodotorula toruloides CGMCC 2.1389
Substrates: isozyme substrate specificities, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanism for the degradation of the DGAT protein, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: in castor bean DGAT2 is more likely to play a major role in seed triacylglycerol biosynthesis than DGAT1
Products: -
Products: -
?
additional information
?
-
-
Substrates: the purified enzyme AtfG25 shows acyltransferase activity with C12- or C16-acyl-CoA, C12 to C18 alcohols (ethanol, butanol, hexanol, octanol, decanol, dodecanol, tetradecanol, hexadecanol, palmitoleyl alcohol, and octadecanol, cf. EC 2.3.1.75), and dipalmitoyl glycerol. Substrate specificity, overview. The DGAT activity of AtfG25 corresponds to about 70% of its wax synthase activity
Products: -
Products: -
?
additional information
?
-
Substrates: docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
Products: -
Products: -
?
additional information
?
-
-
Substrates: docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
Products: -
Products: -
?
additional information
?
-
Substrates: docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
Products: -
Products: -
?
additional information
?
-
Thraustochytrium roseum ATCC28210
-
Substrates: the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant TmDGAT1 protein is capable of utilizing a range of (14)C-labelled fatty acyl-CoA donors and diacylglycerol acceptors, and can synthesize (14)C-trierucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant TmDGAT1 protein is capable of utilizing a range of (14)C-labelled fatty acyl-CoA donors and diacylglycerol acceptors, and can synthesize (14)C-trierucin
Products: -
Products: -
?
additional information
?
-
-
Substrates: DGAT is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22
Products: -
Products: -
?
additional information
?
-
Substrates: acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diricinoleoyl-sn-glycerol + ricinoleoyl-CoA
triricinolein + CoA
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + 1,2-di-(cis-9-octadecenoyl)-sn-glycerol
CoA + 1,2-di-(cis-9-octadecenoyl)-3-octanoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: role in leaf metabolism, overview
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT catalyzes the transfer of an acyl moiety between two DAG molecules to form triacylglycerol and monoacylglycerol
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT1 and DGAT2 are two unrelated enzymes that catalyze the committed step in triacylglycerol biosynthesis
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT1 catalyzes the committed step in triacylglycerol biosynthesis
Products: -
Products: -
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Substrates: DGAT2 catalyzes the committed step in triacylglycerol biosynthesis
Products: -
Products: -
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
E2RDN4
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Haematococcus lacustris UTEX 2505
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Lobosphaera incisa SAG 2468
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
KY859195, A0A2D2CI94
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Nannochloropsis oceanica CCAP 849/10
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
M1E7W9, XP_011098009
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Thraustochytrium roseum ATCC28210
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: isoform DGAT2b is catalytically more active than DGAt2a
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: isoform DGAT2b is catalytically more active than DGAt2a
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Lobosphaera incisa SAG 2468
Substrates: -
Products: -
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acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: isoforms DGAT1 and DGAT2 Can compensate for each other to synthesize triacylglycerol
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
Substrates: -
Products: -
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?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
Substrates: -
Products: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: enzyme catalyzing the final reaction in the sn-glycerol-3-phosphate pathway leading to TAG
Products: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: last step of triacylglycerol synthesis
Products: -
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acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: DGAT1 is more involved in fat absorption in the intestine and DGAT2 plays important role in assembly of de novo synthesized fatty acids into VLDL particles in liver
Products: -
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?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: last reaction in triacylglycerol synthesis
Products: -
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?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
Substrates: -
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acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
Substrates: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
Substrates: -
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oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
Substrates: -
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: -
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
Substrates: the final step in triacylglycerol synthesis is catalyzed by the acyl-CoA:diacylglycerol acyltransferase enzymes, DGAT1 and DGAT2
Products: -
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additional information
?
-
-
Substrates: the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
Products: -
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?
additional information
?
-
-
Substrates: the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
Products: -
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?
additional information
?
-
-
Substrates: increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
Products: -
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additional information
?
-
-
Substrates: the multifunctional enzyme plays an important role in lipid metabolism in human skin
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additional information
?
-
Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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additional information
?
-
Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
Products: -
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additional information
?
-
-
Substrates: increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
Products: -
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additional information
?
-
Substrates: calnexin is a DGAT2-interacting protein
Products: -
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additional information
?
-
-
Substrates: calnexin is a DGAT2-interacting protein
Products: -
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additional information
?
-
-
Substrates: increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanism for the degradation of the DGAT protein, overview
Products: -
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?
additional information
?
-
-
Substrates: in castor bean DGAT2 is more likely to play a major role in seed triacylglycerol biosynthesis than DGAT1
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-2-[4'-[(phenylcarbamoyl)amino][1,1'-biphenyl]-4-carbonyl]cyclopentane-1-carboxylic acid
-
(2E)-1-[2,4-dihydroxy-6-methoxy-3-[(2R)-5-methyl-2-(1-methylethenyl)hex-4-en-1-yl]phenyl]-3-(2,4-dihydroxyphenyl)prop-2-en-1-one
-
IC50: 0.0098 mM
(2E,4Z,8E)-N-[9-(3,4-methylenedioxyphenyl)-2,4,8-nonatrienoyl]piperidine
-
IC50: 0.0298 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
(2R,3R)-2-(2,4-Dihydroxy-phenyl)-3,7-dihydroxy-8-((R)-5-hydroxy-2-isopropenyl-5-methyl-hexyl)-5-methoxy-chroman-4-one
-
i.e. kushenol H, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.142 mM
(2R,3S)-2-(2,4-Dihydroxy-phenyl)-3,7-dihydroxy-8-((R)-5-hydroxy-2-isopropenyl-5-methyl-hexyl)-5-methoxy-chroman-4-one
-
i.e. kushenol K, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.250 mM
(2S)-1-(3-[[(2S)-1-ethoxy-4-phenylbutan-2-yl]sulfamoyl]anilino)-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
-
-
(2S)-1-[(1-[[(1S)-1-(3-cyclopropyl-1,2,4-oxadiazol-5-yl)-3-phenylpropyl]carbamoyl]cyclopentyl)amino]-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
-
-
(4-[4-[4-(2-amino-5-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-(5-chloro-2-nitrobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-([[2-fluoro-5-(trifluoromethyl)phenyl]carbamoyl]amino)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4S,7R)-4-(5,5-dimethyl-4-oxo-4,5-dihydrofuran-2-yl)-2,2-dimethyl-4,7-bis[(4E)-4-methyl-5-[(2R)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-1-yl]-4,5,6,7-tetrahydro-1-benzofuran-3(2H)-one
89.23% inhibition
(trans-4-(4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-cyclopentylethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
-
(trans-4-(4-[(5-cyclopentylmethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
-
(trans-4-(4-[(5-[1-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-[2-chlorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-[2-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
(trans-4-[4-[(5-benzyl-1,2,4-oxadiazol-3-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
(trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
1,2-diacyl-sn-glycerol
-
dicaprin, dimyristin, dipalmitin, high concentration
1-acyl-sn-glycero-3-phosphocholine
-
activation, at low concentrations, inhibition above 0.2 mM
1-O-Hexadecylpropanediol-3-phosphocholine
-
activation, low concentration, inhibitory at high concentration
1-[2,4-dihydroxy-3-(2-isopropenyl-5-methyl-hex-4-enyl)-6-methoxy-phenyl]-3-(2,4-dihydroxy-phenyl)-propenone
-
i.e. kuraridin, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.099 mM
2-(2,4-dihydroxy-phenyl)-7-hydroxy-8-(2-isopropenyl-5-methyl-hex-4-enyl)-5-methoxy-chroman-4-one
-
i.e. kurarinone, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.0109 mM
2-(2,4-dihydroxy-phenyl)-7-hydroxy-8-[2-(3-hydroxy-3-methyl-butyl)-3-methyl-but-3-enyl]-5-methoxy-chroman-4-one
-
i.e. kurarinol, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.0086 mM
3,5-dimethyl-6-([(6E)-6-methyl-7-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]hept-6-en-1-yl]oxy)pyrazine-2-carboxamide
-
3-(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)propanoic acid
-
3-oxoolean-12-en-27-oic acid
-
the compound exhibits strong inhibition efficacy towards diacylglycerol acyltransferases 1 and 2, and acts competitively against oleoyl-CoA in vitro
4-amino-6-[(4E)-4-methyl-5-[(2R)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-2-yn-1-yl]-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-5(6H)-one
-
4-amino-6-[(4E)-4-methyl-5-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-2-yn-1-yl]-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-5(6H)-one
-
4-[(4-chloro-3-fluorophenyl)methyl]-N-[2-(3,4-diethoxyphenyl)ethyl]-4H-thieno[3,2-b]pyrrole-5-carboxamide
-
EC value is 0.000009 mM
4-[4-(4-[[2-phenyl-5-(trifluoromethyl)-1,3-oxazole-4-carbonyl]amino]phenyl)piperidine-1-carbonyl]cyclohexane-1-carboxylic acid
-
4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexane-1-carboxylic acid
-
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
aceriphyllic acid A
-
the compound exhibits strong inhibition efficacy towards diacylglycerol acyltransferases 1 and 2, and acts competitively against oleoyl-CoA in vitro
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetic acid
-
cis-4-(4-[[5-(cyclopentylamino)-1,3,4-thiadiazol-2-yl]carbamoyl]phenoxy)cyclohexane-1-carboxylic acid
-
-
cis-4-([5-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]pyridin-2-yl]oxy)cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([3-[(3,5-difluorophenyl)methyl]-1,2,4-oxadiazol-5-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(5-anilino-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[[5-([5-[(3-chlorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)pyridin-2-yl]oxy]cyclohexane-1-carboxylic acid
-
-
dehydropipernonaline
-
noncompetitive inhibition, IC50: 0.0212 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
ethyl 1-(1-[[(2-chlorophenyl)carbamoyl]amino]cyclohexane-1-carbonyl)piperidine-4-carboxylate
-
EC value is 0.0015 mM
ethyl 1-[N-[(2,4-dichlorophenyl)carbamoyl]-2-methylalanyl]piperidine-4-carboxylate
-
EC value is 0.00025 mM
lysophosphatidylcholine
-
activation at low concentrations, optimum at 0.075 mM, inhibitory above 0.2 mM
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[[(thiophen-3-yl)methyl]amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 2-(4-(4-(4-((tert-butoxycarbonyl)amino)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohex-3-en-1-yl)acetate
-
methyl 2-(4-(4-(4-((tert-butoxycarbonyl)amino)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl) acetate
-
methyl 2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl 2-(4-(4-(4-aminophenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl 3-benzamido-1-[(furan-2-yl)methyl]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 3-[(furan-2-carbonyl)amino]-1-(3-methylbutyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[(2,3-dihydro-1H-inden-2-yl)amino]-3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[[(4-acetamidophenyl)methyl]amino]-1-benzyl-3-[(furan-3-carbonyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[[(furan-3-yl)methyl]amino]-1-(2-methylpropyl)-3-(2-phenylacetamido)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
N-(1-[[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]amino]-2-methyl-1-oxopropan-2-yl)-4-fluorobenzamide
-
-
N-(4,5-dihydronaphtho[1,2-d]thiazol-2-yl)-2-(3,4-dimethoxy phenyl)acetamide
selective inhibitor of isoform DGAT2 when used at low concentrations; selective inhibitor of isoform DGAT2 when used at low concentrations
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(dimethylamino)ethyl]carbamoyl]cyclohexyl)benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(morpholin-4-yl)ethyl]carbamoyl]cyclohexyl)benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2,3-dihydroxypropyl)carbamoyl]cyclohexyl]benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-hydroxy-2-methylpropyl)carbamoyl]cyclohexyl]benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-methoxyethyl)carbamoyl]cyclohexyl]benzamide
-
-
N-[(2S)-1-ethoxy-4-phenylbutan-2-yl]-1-[2-(tricyclo[3.3.1.1~3,7~]decan-2-yl)acetamido]cyclopentane-1-carboxamide
-
-
N-[1,5-bis(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(3,5-dimethylphenyl)-4,5,6,7-tetrahydro-1H-indazol-4-yl]-1,2,3-thiadiazole-4-carboxamide
-
EC value is 0.10 mM
N-[1-(4-fluoro-2-methylphenyl)-5-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(4-fluorophenyl)-5-[2-(4-fluorophenyl)propan-2-yl]-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(4-hydroxyphenyl)-4,5,6,7-tetrahydro-1H-indazol-4-yl]pyridine-2-carboxamide
-
EC value is 0.00000034 mM
N-[2-(3,4-diethoxyphenyl)ethyl]-4-methyl-4H-thieno[3,2-b]pyrrole-5-carboxamide
-
EC value is 0.011 mM
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-(1-methylcyclopropane-1-carbonyl)alaninamide
-
-
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
p-chloromercuribenzene sulfonate
-
complete inhibition, DTT protects
pipernonaline
-
IC50: 0.0372 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
piperrolein B
-
IC50: 0.0201 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
retrofractamide C
-
IC50: 0.9 mM, above, isolated from the extracts of fruits of Piper longum and Piper nigrum
tert-butyl (2S)-2-[[1-([(2S)-2-[(2,2-dimethylpropanoyl)oxy]-4-methylpentanoyl]amino)cyclopentane-1-carbonyl]amino]-4-phenylbutanoate
-
-
trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetic acid
-
trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
Trifluoperazine
-
0.5 mM, in the presence of suboptimal phosphatidic acid concentration
[(1r,4r)-4-(4-[[5-(3,4-difluoroanilino)-1,3,4-oxadiazole-2-carbonyl]amino]phenyl)cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
[(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid
89.32% inhibition
[4-(4-[4-[(naphthalene-2-carbonyl)amino]phenyl]thieno[3,2-d]pyrimidin-7-yl)cyclohexyl]acetic acid
-
[4-[4-(4-[[(3-chlorophenyl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[(4-chloropyridin-2-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[(5-bromopyridin-3-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[2-phenyl-5-(trifluoromethyl)-1,3-oxazole-4-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[6-(trifluoromethyl)pyridine-3-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[trans-4-(4-[[5-(2-cyclopentylethyl)-1,3,4-thiadiazol-2-yl]carbamoyl]phenyl)cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-oxadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[2-(oxolan-2-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[2-(oxolan-3-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
i.e. DTNB, complete inhibition, DTT protects
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
-
-
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
-
-
acyl-CoA
substrate inhibition is observed at higher concentrations of acyl-CoA
acyl-CoA
substrate inhibition of DGAT1, acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana slightly enhances the substrate inhibition of DGAT1 at the acyl-CoA concentrations above 0.01 mM
betulinic acid
-
a lupane-type triterpenoid, isolated from methanolic extracts of Alnus hirsuta, inhibition of Hep-G2 cell triacyglycerol biosynthesis
betulinic acid
-
a lupane-type triterpenoid, isolated from methanolic extracts of Alnus hirsuta, noncompetitive inhibition, IC50: 0.0096 mM
bovine serum albumin
-
binds palmitoyl-CoA and decreases activity towards palmitoyl-CoA, but not butyryl-CoA
-
CaCl2
-
2 mM, inhibits purified enzyme but not activity in lipid body fraction
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
E2RDN4
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
CoA
noncompetitively inhibits isozyme BnaC.DGAT1.a. The N-terminal domain of isoform BnaA.DGAT1.b can interact with acyl-CoA at a possible allosteric site, and CoA can displace the thioester
CoA
an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview
MgCl2
-
5 mM, inhibits purified enzyme but not activity in lipid body fraction
N-ethylmaleimide
-
inhibits solubilized enzyme, but not membrane-bound enzyme
niacin
a specific noncompetitive DGAT2 inhibitor. Dga1p enzyme mutant versions exhibit DGAT2 specific activity, which is inhibited by niacin. The decrease is 70% for Dga1pDELTA19 and up to 99.5% for Dga1pDELTA85
oleoyl-CoA
BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition. BnaDGAT1 is less susceptible to substrate inhibition at 0.005-0.020 mM oleoyl-CoA in the presence of 1 mg/ml BSA
oleoyl-CoA
an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview
oleoyl-CoA
substrate inhibition; substrate inhibition
Tween 20
-
99% inhibition at 5 mg/ml, 89% inhibition at 1 mg/ml, 49% inhibition at 0.5 mg/ml
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
E2RDN4
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
phosphorylation downregulates the activity of the enzyme
-
additional information
-
phosphorylation downregulates the activity of the enzyme
-
additional information
the highly disordered segment at the enzyme's N-terminus is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif
-
additional information
-
the highly disordered segment at the enzyme's N-terminus is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif
-
additional information
the cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites, conformational heterogeneity in the N-terminal domain of DGAT1
-
additional information
-
the cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites, conformational heterogeneity in the N-terminal domain of DGAT1
-
additional information
E2RDN4
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
-
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
design and synthesis of diacylglycerol acyltransferase 1 inhibitors based on aphadilactone C. The lactone group of aphadilactone C is introduced into the [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid (which have entered into clinical research) to verify whether the lactone in aphadilactone C plays the same role as carboxylic group in [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid. The final in vitro assay shows that the synthesized compounds have not the inhibition activity to DGAT1. This might suggest that the inhibition mechanism of aphadilactone C is not the same as of [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid. No inhibition by 3,5-dimethyl-6-[(1E)-1-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]prop-1-en-2-yl]pyrazine-2-carboxamide
-
additional information
-
high-throughput screening for enzyme inhibitors, quantitative-high throughput image-based assay, overview. The activity of the identified lipid storage inhibitors is evolutionary conserved. Three scaffolds: structures are characterized by a tetrahydroindazole (CT1), thienopyrrole (CT2) or arylureido (CT3) core, phenotypic analysis of thienopyrrole (CT2) treated cells
-
additional information
a series of thieno[3,2-d]pyrimidine derivatives are synthesized and their inhibitory effects against diacylglycerol acyltransferase 1 (DGAT-1) are assessed
-
additional information
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
-
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
no inhibition by selective DGAT1 inhibitor PF-04620110
-
additional information
-
no inhibition by selective DGAT1 inhibitor PF-04620110
-
additional information
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
-
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
-
diethyl-p-nitrophenylphosphate, diisopropyl fluorophosphate
-
additional information
-
not inhibitory: hesperetin, naringenin, quercetin, kaempferol up to 0.8 mM
-
additional information
-
an ethylacetic extract of Youngia koidzumiana, a plant endemic to the Mount Chiri region of Korea, significantly inhibits the liver microsome enzyme
-
additional information
-
inhibition mechanism, the inhibitory activity of Piper fruits is influenced by the presence of the piperidine group rather than by isobutyl group, overview
-
additional information
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-acyl-sn-glycero-3-phosphocholine
-
activation, at low concentrations, inhibition above 0.2 mM
1-O-Hexadecylpropanediol-3-phosphocholine
-
activation, low concentration, inhibitory at high concentration
calnexin
calnexin is a diacylglycerol acyltransferase-2 interacting protein
-
lysophosphatidylcholine
-
activation at low concentrations, optimum at 0.075 mM, inhibitory above 0.2 mM
PtdOH
a feedforward activator of plant DGAT1. PtdOH is suggested to aid in relieving possible autoinhibition by interacting with the N-terminal regulatory domain spanning the autoinhibitory motif and converts DGAT1 to a more active state that is also less sensitive to substrate inhibition
sucrose
-
treatment of cells with elevated sucrose levels increases DGAT activity
phosphatidic acid
PA, Feed-forward activation of BnaDGAT1 by phosphatidate, PA facilitates the transition of the enzyme into the more active state. PA may also relieve possible autoinhibition of BnaDGAT1 brought about by the N-terminal regulatory domain, which is shown to interact with PA. The soluble domain of BnaDGAT1 is likely to interact with the small highly charged head group of PA. 18:1/18:1-PA and 16:0/18:1-PA activated BnaDGAT1 by about 4.7fold and 2.4fold, respectively. 16:0/16:0-PA only activates the enzyme by about 1.24fold, while 18:0/18:0-PA has a minimal effect on enzyme activity. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
additional information
Cuphea sp.
-
effectivity of detergents used in in vitro assays, overview
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
additional information
-
tgs transcript levels are upregulated under various stress culture conditions
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00055
oleoyl-CoA
pH 7.4, 30°C, recombinant truncated enzyme mutant BnaDGAT181-501
0.00061
oleoyl-CoA
pH 7.4, 30°C, recombinant full-length wild-type enzyme
0.00307
oleoyl-CoA
isozyme CzDGAT2C, pH 7.4, 30°C
0.00067
palmitoyl-CoA
pH 7.4, 30°C, recombinant truncated enzyme mutant BnaDGAT181-501
0.00069
palmitoyl-CoA
pH 7.4, 30°C, recombinant full-length wild-type enzyme
additional information
additional information
-
the flux control coefficient is 0.12 in oil palm
-
additional information
additional information
-
acyl-CoA substrate binding kinetics of the recombinant N-terminal fragment, overview
-
additional information
additional information
-
the flux control coefficient is 0.74 in olive
-
additional information
additional information
Michaelis-Menten or allosteric sigmoidal kinetics
-
additional information
additional information
-
Michaelis-Menten or allosteric sigmoidal kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA
-
additional information
additional information
-
kinetic analysis of lipidated BnaDGAT1. BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA
-
additional information
additional information
isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model
-
additional information
additional information
-
isozyme BnaC.DGAT1.a exhibits positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. Kinetics of wild-type and enzyme mutants, Michaelis-Menten kinetic model
-
additional information
additional information
kinetics of wax synthase activity, overview
-
additional information
additional information
kinetics of wax synthase activity, overview
-
additional information
additional information
-
kinetics of wax synthase activity, overview
-
additional information
additional information
the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding
-
additional information
additional information
the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding
-
additional information
additional information
the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0098
(2E)-1-[2,4-dihydroxy-6-methoxy-3-[(2R)-5-methyl-2-(1-methylethenyl)hex-4-en-1-yl]phenyl]-3-(2,4-dihydroxyphenyl)prop-2-en-1-one
Rattus norvegicus
-
IC50: 0.0098 mM
0.0298
(2E,4Z,8E)-N-[9-(3,4-methylenedioxyphenyl)-2,4,8-nonatrienoyl]piperidine
Rattus norvegicus
-
IC50: 0.0298 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
0.01
(2S)-1-(3-[[(2S)-1-ethoxy-4-phenylbutan-2-yl]sulfamoyl]anilino)-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
Homo sapiens
-
IC50 less than 0.01 mM, at pH 7.5 and 25°C
0.000011
(2S)-1-[(1-[[(1S)-1-(3-cyclopropyl-1,2,4-oxadiazol-5-yl)-3-phenylpropyl]carbamoyl]cyclopentyl)amino]-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
Homo sapiens
-
at pH 7.5 and 25°C
0.000326
(4-[4-[4-(2-amino-5-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.000276
(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.001
(4-[4-[4-(5-chloro-2-nitrobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
Homo sapiens
above, pH 7.4, 25°C
0.000351
(4-[4-[4-([[2-fluoro-5-(trifluoromethyl)phenyl]carbamoyl]amino)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.00046
(4S,7R)-4-(5,5-dimethyl-4-oxo-4,5-dihydrofuran-2-yl)-2,2-dimethyl-4,7-bis[(4E)-4-methyl-5-[(2R)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-1-yl]-4,5,6,7-tetrahydro-1-benzofuran-3(2H)-one
Homo sapiens
pH 7.4, temperature not specified in the publication
0.00036
(trans-4-(4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.000019
(trans-4-(4-[(5-cyclopentylethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.000024
(trans-4-(4-[(5-cyclopentylmethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.000045
(trans-4-(4-[(5-[1-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.00003
(trans-4-(4-[(5-[2-chlorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.00003
(trans-4-(4-[(5-[2-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
Homo sapiens
-
pH not specified in the publication, 25°C
0.000253
(trans-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000286
(trans-4-[4-[(5-benzyl-1,2,4-oxadiazol-3-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000036
(trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000409
3-(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)propanoic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.001
4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexane-1-carboxylic acid
Homo sapiens
above, pH 7.4, 25°C
0.047 - 0.1607
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
0.0096
betulinic acid
Rattus norvegicus
-
a lupane-type triterpenoid, isolated from methanolic extracts of Alnus hirsuta, noncompetitive inhibition, IC50: 0.0096 mM
0.000022
cis-4-(4-[[5-(cyclopentylamino)-1,3,4-thiadiazol-2-yl]carbamoyl]phenoxy)cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000045
cis-4-([5-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]pyridin-2-yl]oxy)cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.00012
cis-4-[4-([3-[(3,5-difluorophenyl)methyl]-1,2,4-oxadiazol-5-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000011
cis-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000012
cis-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000057
cis-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000004
cis-4-[4-[(5-anilino-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000016
cis-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000055
cis-4-[[5-([5-[(3-chlorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)pyridin-2-yl]oxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.0212
dehydropipernonaline
Rattus norvegicus
-
noncompetitive inhibition, IC50: 0.0212 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
0.0059
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0082
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[[(thiophen-3-yl)methyl]amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0074
methyl 3-benzamido-1-[(furan-2-yl)methyl]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0091
methyl 3-[(furan-2-carbonyl)amino]-1-(3-methylbutyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0088
methyl 3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0072
methyl 5-[(2,3-dihydro-1H-inden-2-yl)amino]-3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0295
methyl 5-[[(4-acetamidophenyl)methyl]amino]-1-benzyl-3-[(furan-3-carbonyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0192
methyl 5-[[(furan-3-yl)methyl]amino]-1-(2-methylpropyl)-3-(2-phenylacetamido)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
Homo sapiens
-
at pH 7.4 and 37°C
0.0035
N-(1-[[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]amino]-2-methyl-1-oxopropan-2-yl)-4-fluorobenzamide
Homo sapiens
-
at pH 7.5 and 25°C
0.0085 - 0.0708
N-(4,5-dihydronaphtho[1,2-d]thiazol-2-yl)-2-(3,4-dimethoxy phenyl)acetamide
0.000048
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-carbamoylcyclohexyl)benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000279
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(dimethylamino)ethyl]carbamoyl]cyclohexyl)benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000122
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(morpholin-4-yl)ethyl]carbamoyl]cyclohexyl)benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000081
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2,3-dihydroxypropyl)carbamoyl]cyclohexyl]benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000092
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-hydroxy-2-methylpropyl)carbamoyl]cyclohexyl]benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000088
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-methoxyethyl)carbamoyl]cyclohexyl]benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.000027
N-[(2S)-1-ethoxy-4-phenylbutan-2-yl]-1-[2-(tricyclo[3.3.1.1~3,7~]decan-2-yl)acetamido]cyclopentane-1-carboxamide
Homo sapiens
-
at pH 7.5 and 25°C
0.00076
N-[1,5-bis(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
Homo sapiens
-
at pH 7.5 and 25°C
0.000062
N-[1-(4-fluoro-2-methylphenyl)-5-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
Homo sapiens
-
at pH 7.5 and 25°C
0.0014
N-[1-(4-fluorophenyl)-5-[2-(4-fluorophenyl)propan-2-yl]-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
Homo sapiens
-
at pH 7.5 and 25°C
0.01
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-(1-methylcyclopropane-1-carbonyl)alaninamide
Homo sapiens
-
IC50 less than 0.01 mM, at pH 7.5 and 25°C
0.0048
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
Homo sapiens
-
at pH 7.5 and 25°C
0.0372
pipernonaline
Rattus norvegicus
-
IC50: 0.0372 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
0.0201
piperrolein B
Rattus norvegicus
-
IC50: 0.0201 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
0.9
retrofractamide C
Rattus norvegicus
-
IC50: 0.9 mM, above, isolated from the extracts of fruits of Piper longum and Piper nigrum
0.000007
tert-butyl (2S)-2-[[1-([(2S)-2-[(2,2-dimethylpropanoyl)oxy]-4-methylpentanoyl]amino)cyclopentane-1-carbonyl]amino]-4-phenylbutanoate
Homo sapiens
-
at pH 7.5 and 25°C
0.00016
trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.00028
trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000019
[(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid
Homo sapiens
pH 7.4, temperature not specified in the publication
0.000157
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
Homo sapiens
pH 7.4, 25°C
0.00008
[(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid
Homo sapiens
pH 7.4, temperature not specified in the publication
0.000398
[4-(4-[4-[(naphthalene-2-carbonyl)amino]phenyl]thieno[3,2-d]pyrimidin-7-yl)cyclohexyl]acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.000121
[4-[4-(4-[[(3-chlorophenyl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
1
[4-[4-(4-[[(4-chloropyridin-2-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
Homo sapiens
above, pH 7.4, 25°C
1
[4-[4-(4-[[(5-bromopyridin-3-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
Homo sapiens
above, pH 7.4, 25°C
0.000152
[4-[4-(4-[[2-phenyl-5-(trifluoromethyl)-1,3-oxazole-4-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
Homo sapiens
pH 7.4, 25°C, recombinant enzyme in microsomes of Spodoptera frugiperda cells
0.001
[4-[4-(4-[[6-(trifluoromethyl)pyridine-3-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
Homo sapiens
above, pH 7.4, 25°C
0.000019
[trans-4-(4-[[5-(2-cyclopentylethyl)-1,3,4-thiadiazol-2-yl]carbamoyl]phenyl)cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000009
[trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.00139
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-oxadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.0006
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000038
[trans-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000144
[trans-4-[4-([5-[2-(oxolan-2-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.000233
[trans-4-[4-([5-[2-(oxolan-3-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
Homo sapiens
-
at pH 7.4 and 37°C
0.047
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
Rattus norvegicus
-
-
0.1607
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
Homo sapiens
-
-
0.0085
N-(4,5-dihydronaphtho[1,2-d]thiazol-2-yl)-2-(3,4-dimethoxy phenyl)acetamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0708
N-(4,5-dihydronaphtho[1,2-d]thiazol-2-yl)-2-(3,4-dimethoxy phenyl)acetamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
Rattus norvegicus
-
kurarione IC50: 0.0048 mg/ml, 8-prenylleutone IC50: 0.015 mg/ml, auriculatin IC50: 0.0072 mg/ml, erysenegalensein O IC50: 0.0011 mg/ml, erysenegalensein D IC50: 0.0015 mg/ml, erysenegalensein N: 28% inhibition at 0.0125 mg/ml, derrone IC50: 0.0151 mg/ml, alpinumisoflavone: 23% inhibition at 0.0125 mg/ml, 6,8-diprenylgenistein IC50: 0.0067 mg/ml
-
additional information
additional information
Homo sapiens
-
IC50 value for tussilagonone above 0.5 mM
-
additional information
XP620
Homo sapiens
-
IC50 above 0.03 mM with 1,2-dioleoyl-sn-glycerol or sn-2-monooleoylglycerol as substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
additional information
additional information
-
substrate specificity of native and recombinant enzyme
additional information
substrate specificity of native and recombinant enzyme
additional information
-
total enzyme activity derived from dehydrated muscle tissue is similar to, or better than, the total activity of enzyme from fresh tissue
additional information
-
specific activity in homogenates in the picomolar range
additional information
-
lipid content and fatty acid composition of triacylglycerols during seed development, overview
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
-
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
recombinant enzyme in Sf9 cell membrane and in COS-7 cell membranes, multifunctional enzyme
additional information
recombinant enzyme in Sf9 cell membrane and in COS-7 cell membranes, multifunctional enzyme
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
additional information
-
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
additional information
-
values of enzyme activity for several isoforms
additional information
high DGAT activity when expressed in recombinant Escherichia coli
additional information
high DGAT activity when expressed in recombinant Escherichia coli
additional information
high DGAT activity when expressed in recombinant Escherichia coli
additional information
high DGAT activity when expressed in recombinant Escherichia coli
additional information
-
shows DGAT activity when expressed in recombinant Escherichia coli
additional information
-
specific activity in the nanomolar range in microsomal preparations, varies considerably between different tissues
additional information
-
quantitative expression analysis of DGAT1 and DGAT2
additional information
shows DGAT activity when expressed in recombinant Escherichia coli
additional information
does not show any DGAT activity when expressed in recombinant Escherichia coli
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
7.2
7.4
7.5
7.6
additional information
-
value of pH-optimum for several enzyme isoforms
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
27
30
37
additional information
additional information
-
assay at various temperatures from 24°C to 40°C
additional information
-
assay at various temperatures from 24°C to 40°C
additional information
-
assay at various temperatures from 24°C to 40°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
about 70% of maximal activity at 20°C, about half-maximal activity at 50°C
40 - 45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the oleaginous microalgae has been first isolated from a glacier in Japan and named Myrmecia incisa to be renamed later to Parietochloris incisa in 2005
UniProt
brenda
Lobosphaera incisa SAG 2468
the oleaginous microalgae has been first isolated from a glacier in Japan and named Myrmecia incisa to be renamed later to Parietochloris incisa in 2005
UniProt
brenda
bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, EC 2.3.1.75 and EC2.3.1.20 resp
Swissprot
brenda
wild-type strain CC-1690 (mt+), cell wall-deficient strain CC-503 (mt+ cw92), and sta6 mutant (CC-4348)
UniProt
brenda
-
UniProt
brenda
synthetic gene, codon-optimized, following the sequence (UniProt A0A2D2CI94) of the wild-type gene of MaDGAT2
KY859195
GenBank
brenda
induction of several enzymic isoform genes upon entry of cells into nonreplicative drug-resistant state
-
-
brenda
-
486338, 486481, 486484, 486486, 486487, 486491, 486492, 486501, 660330, 671657, 675754, 701960, 704119, 704440, 705084
-
-
brenda
DGAT1, genomic sequence; tung tree, DGAT1 and DGAT2, both enzymes are encoded by single genes
SwissProt
brenda
DGAT1, genomic sequence; tung tree, DGAT1, single gene
SwissProt
brenda
DGAT2, genomic sequence; tung tree, DGAT2, single gene
SwissProt
brenda
member of the type 1 acyl-CoA:diacylglycerol acyltransferase family
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SbDGAT1-2 is more abundantly expressed in embryo and bran during the early stage of the grain development in comparison to SbDGAT1-1
brenda
microspore-derived cell suspension cultures
brenda
additional information
-
storage seed oil is mobilized into the cotyledons from endosperm
brenda
-
CoDGAT2 is highly expressed in coconut pulp approximately 7 months after pollination. CoDGAT2 is highly expressed in endosperm developmental stage 1, decreases significantly at stage 2, and is then restored to the same level as in stage 1
brenda
GmDGAT3-2 expression is much higher than expression of GmDGAT3-1
brenda
greater abundance of isozyme DGAT2 mRNA in the heart compared to isozyme DGAT1
brenda
-
small intestinal epithelium, decrease of specific activity from proximal to distal small intestine
brenda
GmDGAT3-2 expression is much higher than expression of GmDGAT3-1
brenda
-
DGAT2 is 18fold more highly expressed in seeds than in leaves and shows temporal specific expression during seed development, while DGAT1 shows little dfference in expression in seeds versus leaves, overview
brenda
-
-
486338, 486484, 486485, 486486, 486487, 486489, 486490, 486491, 486501, 660330, 674136, 676737, 675754, 671657, 705084, 701960, 704119
brenda
-
dehydration is an effective method of storage of samples destined for estimation of the microsomal enzyme activity
brenda
developing seeds, high DGAT1 expression
brenda
GmDGAT1A is highly expressed in seeds, the expression pattern is consistent with oil accumulation
brenda
high expression level, the expression pattern is consistent with oil accumulation
brenda
GmDGAT3-2 expression is much higher than expression of GmDGAT3-1
brenda
-
developmenting, maximal activity at 8-14 days after flowering during rapid lipid accumulation, overview
brenda
-
germinating, enzyme expression throughout seed germination at levels considerably enhanced from that in the dormant seed, no expression in immature seed, expression profile, overview
brenda
-
DGAT2 is 18fold more highly expressed in seeds than in leaves and shows temporal specific expression during seed development, while DGAT1 shows little dfference in expression in seeds versus leaves, overview
brenda
additional information
temporal expression pattern of DGAT1, overview. DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
brenda
additional information
-
in Arabidopsis thaliana, DGAT1 is expressed in different plant organs such as leaves, roots, flowers, siliques, seeds, and seedlings, the last two of which exhibit the highest expression levels. The high expression of AtDGAT1 in developing seeds and pollen correlates with the ability of these organs to accumulate high amounts of TAG. In addition, DGAT1 is expressed at lower levels in shoots and roots of seedling, which are sites exhibiting active cell division and growth
brenda
additional information
in Arabidopsis thaliana, DGAT1 is expressed in different plant organs such as leaves, roots, flowers, siliques, seeds, and seedlings, the last two of which exhibit the highest expression levels. The high expression of AtDGAT1 in developing seeds and pollen correlates with the ability of these organs to accumulate high amounts of TAG. In addition, DGAT1 is expressed at lower levels in shoots and roots of seedling, which are sites exhibiting active cell division and growth
brenda
additional information
in Arabidopsis thaliana, DGAT1 is expressed in different plant organs such as leaves, roots, flowers, siliques, seeds, and seedlings, the last two of which exhibit the highest expression levels. The high expression of AtDGAT1 in developing seeds and pollen correlates with the ability of these organs to accumulate high amounts of TAG. In addition, DGAT1 is expressed at lower levels in shoots and roots of seedling, which are sites exhibiting active cell division and growth
brenda
additional information
in Arabidopsis thaliana, DGAT1 is expressed in different plant organs such as leaves, roots, flowers, siliques, seeds, and seedlings, the last two of which exhibit the highest expression levels. The high expression of AtDGAT1 in developing seeds and pollen correlates with the ability of these organs to accumulate high amounts of TAG. In addition, DGAT1 is expressed at lower levels in shoots and roots of seedling, which are sites exhibiting active cell division and growth
brenda
additional information
-
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
brenda
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
brenda
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
brenda
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
brenda
additional information
-
temporal expression pattern of DGAT1, overview. DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
-
brenda
additional information
no expression of seed-specific DGAT1 in root, stem, leaf, and flower
brenda
additional information
-
spatiotemporal expression analysis of the isozymes in different tissues of Cyperus esculentus, distinct expression patterns of the CeDGAT isozyme genes are observed in the different tissues, maybe also reflecting their potential role in triacylglycerol (TAG) biosynthesis
brenda
additional information
GmDGAT1A is mainly expressed in seeds, but also in tissues like roots, leaves, flowers, at relatively lower levels
brenda
additional information
GmDGAT1A is mainly expressed in seeds, but also in tissues like roots, leaves, flowers, at relatively lower levels
brenda
additional information
-
GmDGAT1A is mainly expressed in seeds, but also in tissues like roots, leaves, flowers, at relatively lower levels
brenda
additional information
GmDGAT2D transcripts are high in flowers and seeds, but also present in other tissues at lower levels, such as roots, leaves and pods
brenda
additional information
GmDGAT2D transcripts are high in flowers and seeds, but also present in other tissues at lower levels, such as roots, leaves and pods
brenda
additional information
-
GmDGAT2D transcripts are high in flowers and seeds, but also present in other tissues at lower levels, such as roots, leaves and pods
brenda
additional information
the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development
brenda
additional information
the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development
brenda
additional information
tissue expression analysis by semiquantitative RT-PCR, ubiquitous expression is observed among different vegetative organs of the plant, although it seems to be higher in developing seeds and particularly in germinating seed cotyledons
brenda
additional information
-
tissue expression analysis by semiquantitative RT-PCR, ubiquitous expression is observed among different vegetative organs of the plant, although it seems to be higher in developing seeds and particularly in germinating seed cotyledons
brenda
additional information
tissue distribution analysis by quantitative real-time PCR
brenda
additional information
XP_011098009
tissue distribution analysis by quantitative real-time PCR
brenda
additional information
-
Streptomyces strain G25 can accumulate extraordinarily large amounts of triacylglycerol (TAG) and consists of 64% fatty acids (dry weight) when cultivated with glucose and 50% fatty acids (dry weight) when cultivated with cellobiose
brenda
additional information
strain DSM 43183 shows an optimal growing temperature of 50°C
brenda
additional information
-
strain DSM 43183 shows an optimal growing temperature of 50°C
brenda
additional information
-
strain DSM 43183 shows an optimal growing temperature of 50°C
-
brenda
additional information
-
DGAT1 is expressed at similar levels in various organs, whereas DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
additional information
DGAT1 is expressed at similar levels in various organs, whereas DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
additional information
DGAT1 is expressed at similar levels in various organs, whereas DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
additional information
-
DGAT1 is expressed at similar levels in various organs, overview
brenda
additional information
DGAT1 is expressed at similar levels in various organs, overview
brenda
additional information
DGAT1 is expressed at similar levels in various organs, overview
brenda
additional information
-
DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
additional information
DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
additional information
DGAT2 is strongly induced in developing seeds at the onset of oil biosynthesis, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
thylakoid and envelope membranes, not in the stroma
brenda
membrane-bound DGAT1 enzyme localized in the chloroplast
brenda
Haematococcus lacustris FACHB-712
-
membrane-bound DGAT1 enzyme localized in the chloroplast
-
brenda
the DGAT2 isozymes all localize to distinct ER domains
brenda
the DGAT2 isozymes all localize to distinct endoplasmic reticulum domains
brenda
Lobosphaera incisa SAG 2468
-
the DGAT2 isozymes all localize to distinct endoplasmic reticulum domains
-
brenda
the endoplasmic reticulum targeting signal is present in the first transmembrane domain, TMD1, of isoform DGAT2
brenda
both the N and C termini are oriented toward the cytosol and have different catalytic roles. A highly conserved motif, 129YFP131, and a hydrophilic segment exclusive to yeast DGAT2 reside in a long endoplasmic reticulum luminal loop following the first transmembrane domain and play an essential role in enzyme catalysis. The strongly conserved residue His195 within the motif HPHG, which may play a role in the active site of DGAT2, is likely embedded in the membrane
brenda
gene MaDGAT encodes one transmembrane region in its 5'-end. MaDGAT without the transmembrane region is still functional. Perhaps the N-terminal transmembrane region in MaDGAT functions only to anchor the enzyme to the endoplasmic reticulum
brenda
-
gene MaDGAT encodes one transmembrane region in its 5'-end. MaDGAT without the transmembrane region is still functional. Perhaps the N-terminal transmembrane region in MaDGAT functions only to anchor the enzyme to the endoplasmic reticulum
-
brenda
DGAT-2 is an integral membrane, it has two transmembrane domains separated by a short loop (about 5-8 amino acids) that extends into the endoplasmic reticulum (ER) lumen. The first transmembrane domain contains an ER targeting signal while the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol
brenda
DGAT1 and DGAT2 are located in different subdomains, but contain similar C-terminal ER retrieval motifs
brenda
an endoplasmic reticulum (ER) retrieval motif responsible for the steady state localization of DGAT2 protein in the ER is identified near the C-terminus of tung tree DGAT2
brenda
the interaction of isoform DGAT2 with lipid droplets is dependent on the C-terminus. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, failed to co-localize with lipid droplets when cells are oleate loaded to stimulate triacylglycerol synthesis
brenda
protein is mainly localised on the cytoplasmic site of the plasma membrane and on the surface of intracellular wax ester inclusions
brenda
embedded in the membrane lipid bilayer
brenda
embedded in the membrane lipid bilayer
brenda
embedded in the membrane lipid bilayer
brenda
embedded in the membrane lipid bilayer
brenda
isozymes HpDGAT2B and HpDGAT2D contain two transmembrane domains each, while isozymes HpDGAT2A and HpDGAT2E do not
brenda
Haematococcus lacustris UTEX 2505
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isozymes HpDGAT2B and HpDGAT2D contain two transmembrane domains each, while isozymes HpDGAT2A and HpDGAT2E do not
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brenda
membrane-bound. The structure of human DGAT1 defines a conserved membrane-bound O-acyltransferase structural fold, which forms a reaction chamber in the ER membrane to shield the acyl transfer reaction from the hydrophobic core of the membrane. The reaction chamber has a tunnel to the cytosolic side and its entrance recognizes the hydrophilic coenzyme A motif of an acyl-CoA molecule. The tunnel has a slit between TM7 and TM8 that could allow the entry of the acyl chain of an acyl-CoA molecule into the chamber, reaching the hydrophobic pocket inside the chamber. The reaction chamber also has a large opening to the hydrophobic core of the membrane, which could allow entry of a diacylglycerol molecule
brenda
embedded in the membrane lipid bilayer
brenda
integral transmembrane enzyme
brenda
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DGAT2 is an integral membrane protein with both the N and C terminus oriented toward the cytosol, the loop between the two transmembrane domains of DGAT2is not exposed to the cytosol
brenda
embedded in the membrane lipid bilayer
brenda
tung tree DGAT1 appears to have two termini localized in the cytosol, suggesting the presence of even-numbered transmembrane domains
brenda
the enzyme contains three putative transmembrane domains
brenda
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the enzyme contains three putative transmembrane domains
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brenda
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the enzyme contains three putative transmembrane domains
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brenda
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brenda
additional information
DGAT1 (BnaDGAT1) is a polytopic membrane protein in the endoplasmic reticulum (ER) with its N-terminal domain (residues 1-113) localized to the cytoplasm. Structure model of isozyme DGAT1-a transmembrane and cytosolic domains, overview
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brenda
additional information
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DGAT1 (BnaDGAT1) is a polytopic membrane protein in the endoplasmic reticulum (ER) with its N-terminal domain (residues 1-113) localized to the cytoplasm. Structure model of isozyme DGAT1-a transmembrane and cytosolic domains, overview
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brenda
additional information
determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
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brenda
additional information
determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
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brenda
additional information
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determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration. Comparison of tissue expression patterns of isozymes GmDGAT1A and GmDGAT2D in nodules, roots, stems, leaves, flowers, pods, and seeds
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brenda
additional information
MaDGAT without the transmembrane region is a cytoplasmic protein
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brenda
additional information
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MaDGAT without the transmembrane region is a cytoplasmic protein
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brenda
additional information
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MaDGAT without the transmembrane region is a cytoplasmic protein
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brenda
additional information
the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets
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brenda
additional information
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the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets
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brenda
additional information
topology prediction, indicating three putative transmembrane domains, hydrophobicity values
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brenda
additional information
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topology prediction, indicating three putative transmembrane domains, hydrophobicity values
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brenda
additional information
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topology prediction, indicating three putative transmembrane domains, hydrophobicity values
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brenda
additional information
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topology prediction, indicating three putative transmembrane domains, hydrophobicity values
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brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
evolution
Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
evolution
the evolutionary and sequence analyses revealed that CzDGAT1 and other green microalgal DGAT1 are closely related to the plant DGAT1 clade. But algal DGAT1 may have different evolutionary and structural features from plant and animal DGAT1 with respect to the hydrophilic N-terminal domain. This domain is predicted to be present in a less disordered state in CzDGAT1 than that of animal/plant DGAT1. The two isoforms of DGAT1 from the green microalga Chromochloris zofingiensis have very distinct features. They share 39.9% amino acid pairwise identity and have very different lengths mainly attributable to the variable N-terminal regions
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
phylogeny of these BnaDGAT1 gene forms. Two clades of DGAT1, which appear to have diverged relatively early in Brassicaceae's history, differ in preference for linoleoyl (18:2DELTA9cis12cis, i.e. 18:2-CoA). Phylogenetic analysis
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOATs). The DGAT1 family is highly conserved. DGAT1 possesses a very hydrophilic N-terminal region corresponding to about the first 100 residues, which is followed by eight to ten predicted transmembrane segments
evolution
the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
evolution
the principal activity of DGATs has been defined as a single-function enzyme catalyzing the esterification of diacylglycerol with acyl-CoA. A dual-function PtWS/DGAT associated with diatom Phaeodactylum tricornutum is discovered in the current study. Distinctive to documented microalgal DGAT types, PtWS/DGAT exhibits activities of both a wax ester synthase (WS) and a DGAT. WS/DGATs are broadly distributed in microalgae, with different topology and phylogeny from those of DGAT1s, DGAT2s, and DGAT3s. In Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure, and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGAT3s
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
-
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
-
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
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the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
-
evolution
-
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
-
evolution
-
Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
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evolution
Lobosphaera incisa SAG 2468
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genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
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evolution
Lobosphaera incisa SAG 2468
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genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
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evolution
Rhodotorula toruloides CGMCC 2.1389
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the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
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evolution
Thraustochytrium roseum ATCC28210
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distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
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malfunction
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enzyme-deficient mice show no effect on retinal anatomy or the ultrastructure of photoreceptor outer-segments. Enzyme loss affects retinyl-ester synthesis and total acyl-coenzyme A:retinol acyl-transferase activityin the eye
malfunction
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Isoform DGAT1 inactivation promotes large lipid droplet formation. Inhibition of isoform DGAT2 augments fatty acid oxidation, whereas inhibition of DGAT1 increases triacylglycerol secretion. Triacylglycerol secretion is significantly reduced on DGAT2 inhibition without altering extracellular apolipoprotein B levels
malfunction
calnexin-deficient mouse embryonic fibroblasts have reduced intracellular triacylglycerol levels and fewer large lipid droplets
malfunction
although the N-terminal domain of algal DGAT1 is not necessary for acyltransferase activity of CzDGAT1, its removal leads to huge decreases in CzDGAT1 enzyme activity, which cannot be restored by fusion with an acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana. Replacement of the N-terminal region by ACBP in CzDGAT1 (ACBP-fused CzDGAT1107-550) is not able to restore or improve the enzyme activity suggesting that the N-terminus may function as a regulatory domain rather than as an acyl-CoA binding site
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. Triglyceride storage is unaffected in DGAT1 inducible knockout (iKO) mice
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function
malfunction
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the respective gene, atfG25, is inactivated in Streptomyces sp. strain G25, cells of the insertion mutant still exhibit DGAT activity and are able to store TAG, albeit in lower quantities and at lower rates than the wild-type strain
malfunction
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phenotypic analysis of thienopyrrole (CT2) inhibitor treated cells, overview
malfunction
in vivo knockdown of CrDGTT1, CrDGTT2 or CrDGTT3 results in 20-35% decreases in TAG content and a reduction of specific TAG fatty acids, in agreement with the findings of the in vitro assay and fatty acid feeding test
malfunction
BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501, which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site
malfunction
with or without cold acclimation, the dgat1 mutants exhibit higher sensitivity upon freezing exposure compared with the wild-type. Under cold conditions, the dgat1 mutants show reduced expression of C-REPEAT/DRE binding factor 2 and its regulons, which are essential for the acquisition of cold tolerance. Lipid profiling reveals that freezing significantly increases the levels of phosphatidic acid (PA) and diacylglycerol (DAG) while decreasing triacylglycerol (TAG) in the rosettes of dgat1 mutant plants. During freezing stress, the accumulation of PA in dgat1 mutant plants stimulates NADPH oxidase activity and enhances RbohD-dependent hydrogen peroxide production compared with the wild-type. Moreover, the cold-inducible transcripts of DGK2, DGK3, and DGK5, encoding diacylglycerol kinases, are significantly more upregulated in the dgat1 mutants than in the wild-type during cold stress. H2O2 and salicylic acid accumulate in the dgat1 mutants upon exposure to freezing temperatures. The dgat1 mutants show decreased expression of CBF2 and its target genes. Comparisons of lipid compositions and contents in wild-type and mutant leaves and seeds, phenotypes, detailed overview
malfunction
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
malfunction
overexpression of PtWS/DGAT in the diatom results in increased levels of total lipids (TL) and triacylglycerol (TAG) regardless of nitrogen availability
malfunction
enhanced DGAT1 expression leads to increased freezing tolerance in Arabidopsis thaliana, whereas DGAT1 deficient mutant lines are sensitive to freezing. The overexpression of DGAT1 with the mutated SnRK1 site translated to higher seed TAG levels in Arabidopsis thaliana when compared to an unmodified enzyme
malfunction
DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought
malfunction
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
malfunction
overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies (LBs). DGAT overexpression affects LB segregation
malfunction
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point mutations, which are capable of obstructing the catalytic capacity result in limited starvation resistance and, thus, presumably restricting Crangon crangon to a habitat with year-round sufficient food
malfunction
inhibiting the diacylglycerol O-acyltransferases, especially DGAT1, disrupts lipid homeostasis and results in channeling of fatty acids into mitochondria for oxidation, leading to generation of high levels of ROS along with mitochondrial damage. High expression of DGAT1 in hepatocytes from cows experiencing fatty liver seems to play a dominant role in promoting fatty acid storage into triacylglycerol and lipid droplets to protect hepatocytes from oxidative damage
malfunction
the synthesis of polyunsaturated fatty acid via the omega-6 desaturase FAD2 becomes essential in seeds when DGAT1 activity is absent
malfunction
DGAT2 inhibitor treatment attenuates the free fatty acid-induced upregulation of PLIN2 and PLIN5 and rescues the impairment of mitochondrial dynamics. Inhibition of DGAT2 restores mitochondrial membrane potential and reduces hepatocyte reactive oxygen species production
malfunction
inhibiting diacylglycerol O-acyltransferases, disrupts lipid homeostasis and results in channeling of fatty acids into mitochondria for oxidation, leading to generation of high levels of ROS along with mitochondrial damage. High expression of DGAT1 in hepatocytes from cows experiencing fatty liver seems to play a dominant role in promoting fatty acid storage into triacylglycerol and lipid droplets to protect hepatocytes from oxidative damage
malfunction
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a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
malfunction
-
with or without cold acclimation, the dgat1 mutants exhibit higher sensitivity upon freezing exposure compared with the wild-type. Under cold conditions, the dgat1 mutants show reduced expression of C-REPEAT/DRE binding factor 2 and its regulons, which are essential for the acquisition of cold tolerance. Lipid profiling reveals that freezing significantly increases the levels of phosphatidic acid (PA) and diacylglycerol (DAG) while decreasing triacylglycerol (TAG) in the rosettes of dgat1 mutant plants. During freezing stress, the accumulation of PA in dgat1 mutant plants stimulates NADPH oxidase activity and enhances RbohD-dependent hydrogen peroxide production compared with the wild-type. Moreover, the cold-inducible transcripts of DGK2, DGK3, and DGK5, encoding diacylglycerol kinases, are significantly more upregulated in the dgat1 mutants than in the wild-type during cold stress. H2O2 and salicylic acid accumulate in the dgat1 mutants upon exposure to freezing temperatures. The dgat1 mutants show decreased expression of CBF2 and its target genes. Comparisons of lipid compositions and contents in wild-type and mutant leaves and seeds, phenotypes, detailed overview
-
malfunction
-
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
-
malfunction
-
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
-
malfunction
-
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
metabolism
-
the triacylglycerol pool generated by DGAT1 is preferentially used for supplying substrates for oxidation, whereas DGAt2-derived triacylglycerol is more favored for secretion
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
metabolism
DGAT-2 atalyzes the final step of triacylglycerol (TG) biosynthesis
metabolism
DGAT1 enzyme is evidenced to be a major determining factor for oil quantity and fatty acid composition of seed oils in several crops
metabolism
-
the primary metabolic enzyme DGAT1 catalyzes the final step in assembly of triacylglycerol (TAG) by acyl transfer from acyl-CoA to diacylglycerol
metabolism
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the last step in triglyceride (TG) synthesis is catalyzed by diacylglycerol:acyltransferase (DGAT) which esterifies the diacylglycerol with a fatty acid
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the final step in triacylglycerol (TAG) biosynthesis is catalyzed by diacylglycerol acyltransferase (DGAT)
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
metabolism
-
type 2 diacylglycerol acyltransferase (DGAT2) is one of the key enzymes involved in triacylglycerol (TAG) biosynthesis
metabolism
-
the isozyme of DGAT in Cyperus esculentus are involved in the triacylglycerol (TAG) biosynthesis
metabolism
diacylglycerol acyltransferase 1 (DGAT1) catalyzes the final and committed step in the Kennedy pathway for triacylglycerol (TAG) biosynthesis
metabolism
seed-specific CpuDGAT1 is associated with medium-chain fatty acid metabolism
metabolism
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGATX gene may contribute more to TAG synthesis in the later stage than during the earlier stages
metabolism
M1E7W9, XP_011098009
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1,2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGAT2B gene may contribute more to TAG synthesis in the early stage than during the later stages
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. The activation of DGAT1 in the maize is responsible for the increased embryo oil content in a high-oil maize line
metabolism
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. Involvement of DGAT3 in TAG biosynthesis in microalgae and diatoms confirmed by heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246
metabolism
-
diacylglycerol acyltransferases catalyze the last and most critical step of triacylglycerol biosynthesis in the Kennedy pathway. Homologous overexpression of MaDGAT1B and MaDGAT2A strengthens triacylglycerol biosynthesis and significantly increases the triacylglycerol content compared to the wild-type by 12.24% and 14.63%, respectively
metabolism
-
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
-
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
diacylglycerol acyltransferases catalyze the last and most critical step of triacylglycerol biosynthesis in the Kennedy pathway. Homologous overexpression of MaDGAT1B and MaDGAT2A strengthens triacylglycerol biosynthesis and significantly increases the triacylglycerol content compared to the wild-type by 12.24% and 14.63%, respectively
-
metabolism
Haematococcus lacustris UTEX 2505
-
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
-
metabolism
Lobosphaera incisa SAG 2468
-
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
-
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
-
physiological function
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
physiological function
enzyme makes a major contribution to triacylglycerol synthesis via an acyl-CoA-dependent mechanism and is not involved in steryl ester synthesis
physiological function
overexpression of the enzyme gene in Saccharomyces cerevisiae leads to accumulation of full-length prtein in wild-type and accumulation of full-length protein and a N-terminally truncated protein in a snf2 disruption mutant, lacking a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, a major cleavage site lies between residues Lys29 and Ser30
physiological function
isoform DGAT2 activity accounts for a modest fraction of less than 20% of overall cellular DGAT activity. Inhibition of DGAT2 activity specifically inhibits and is rate-limiting for the incorporation of de novo synthesized fatty acids and of glycerol into cellular and secreted triglyceride to a much greater extent than it affects the incorporation of exogenously added oleate. Isoform DGAT2 acts upstream of isoform DGAT1, largely determines the rate of de novo synthesis of triglyceride, and uses nascent diacylglycerol and de novo synthesized fatty acids as substrates
physiological function
inhibition of isoform DGAT1 affects equally the incorporation of glycerol and exogenous preformed oleate into cellular and secreted triacylglycerol. Data indicate that isoform DGAT2 acts upstream of isoform DGAT1, and DGAT1 functions in the re-esterification of partial glycerides generated by intracellular lipolysis, using preformed fatty acids
physiological function
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
physiological function
-
the enzyme interacts with lipid droplets presumably to catalyze localized triacylglycerol synthesis for lipid droplet expansion
physiological function
DGAT2 catalyzes the formation of triacylglycerol (TG) using fatty acyl coenzyme A (CoA) and 1,2-diacylglycerol (DG) as substrates. TG is the major form of stored metabolic energy in eukaryotic organisms that is sequestered in the hydrophobic core of cytosolic lipid droplets until it is needed. DGAT-2 catalyzes TG synthesis for lipid droplet growth
physiological function
-
DGAT1 confers freezing tolerance in plants by supporting SFR2 (sensitive-to-freezing2)-mediated remodeling of chloroplast membranes, recombinant overexpression of AtDGAT1 leads to increased freezing tolerance in seedlings
physiological function
isozyme GmDGAT1A may play a role in usual seed triacylglycerol (TAG) production. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses
physiological function
isozyme GmDGAT2D plays a role in usual seed triacylglycerol (TAG) production and is also involved in other tissues in responses to environmental and hormonal cues. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses. Ectopic expression of GmDGATs in soybean hairy roots promotes TAG accumulation
physiological function
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
physiological function
intrinsic disorder in plant proteins has been reported to be essential for the stress response. An intrinsically disordered region (IDR) spanning the N-terminal cytosolic domain of the intramembrane enzyme diacylglycerol acyltransferase1 (DGAT1) from canola-type Brassica napus, has been identified. The IDR spans amino acid residues 1-80, while residues 81-113 have a folded structure. DGAT1 (EC 2.3.1.20) catalyzes the acyl-coenzyme A (CoA)-dependent acylation of sn-1, 2-diacylglycerol (DAG) to produce triacylglycerol (TAG) and CoA. TAG serves as an energy source for germination in plants, a component of edible oil. This enzyme has a substantial effect on carbon flux into seed oil
physiological function
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function. The two DGAT isoforms in the heart have partially redundant function
physiological function
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function
physiological function
-
enzyme AtfG25 has an important, but not exclusive, role in triacylglycerol (TAG) biosynthesis in the Streptomyces sp. G25 isolate, suggesting the presence of alternative metabolic pathways for lipid accumulation
physiological function
-
diacylglycerol acyltransferase 1 (DGAT1) is a key enzyme in the production of triacylglycerols
physiological function
KY859195, A0A2D2CI94
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
physiological function
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii. rDGTT1 is shown to prefer prokaryotic lipid substrates and probably resides in both the endoplasmic reticulum and chloroplast envelope, indicating its role in prokaryotic and eukaryotic TAG biosynthesis. Role of isozyme CrDGTT1 in TAG biosynthesis, overview
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii
physiological function
the specialized diacylglycerol acyltransferase DGAT1 contributes to the extreme medium-chain fatty acid content of Cuphea seed oil
physiological function
diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acylcoenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). Proposed model for BnaDGAT1 regulation involving the hydrophilic N-terminal domain (NTD), overview
physiological function
the conversion of diacylglycerol (DAG) to triacylglycerol (TAG) by DGAT1 is critical for plant freezing tolerance, acting by balancing TAG and phosphatidic acid (PA) production in Arabidopsis thaliana
physiological function
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
physiological function
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
physiological function
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
physiological function
regardless of N availability, PtWS/DGAT exhibits a DGAT activity with a preference on saturated fatty acids. PtWS/DGAT exhibits activities of both a wax ester synthase (WS, EC 2.3.1.75) and a diacylglycerol acyltransferase (DGAT, EC 2.3.1.20)
physiological function
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
physiological function
type I diacylglycerol acyltransferase (MtDGAT1) is involved in triacylglycerol (TAG) biosynthesis and may contribute to biochemical mechanisms determining the particular fatty acid composition of Macadamia oil. Major contribution of DGAT enzymes to TAG biosynthesis in seed plants
physiological function
M1E7W9, XP_011098009
diacylglycerol acyltransferase (DGAT) is an acyl-CoA-dependent enzyme which converts diacylglycerol (DAG) to triacylglycerol (TAG)
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
physiological function
DGAT1 appears to play a role in freezing and/or drought stress responses in Arabidopsis thaliana. DGAT1 is suggested to be involved in maintaining a balance of DAG and acyl-CoA for the biosynthesis of membrane lipids and recycling of fatty acids to TAG under conditions where catabolic reactions are halted. Regulation of the enzyme, overview
physiological function
DGAT1 appears to play a role in freezing and/or drought stress responses in Brassica napus. Regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview. Arabidopsis thaliana DGAT3 appears to be involved in recycling of linoleic acid (18:2DELTA9cis,12cis) and alpha-linolenic acid (18:3DELTA9cis, 12cis,15cis) into for triacylglycerol (TAG) when TAG breakdown is blocked
physiological function
the enzyme is responsible for triacylglycerol biosynthesis via acyl-CoA-dependent pathway
physiological function
HpDGAT2A, HpDGAT2D, and HpDGAT2E genes are together involved in astaxanthin and triacylglycerol biosynthesis under stress
physiological function
the enzyme (IpDGAT2) catalyzes the synthesis of lipids in plants and especially catalyzes the accumulation of mainly fatty acids such as C18:2, C18:3 and C20:1
physiological function
potentially functional role of HpDGAT1 in astaxanthin esterification
physiological function
-
GhDGAT3D is involved in regulating oil biosynthesis and fatty acid composition of cotton seeds. Roles of GhDGAT3D in oil biosynthesis and fatty acid composition. Increase in C18:1 content and a decrease in C18:2 and C18:3 contents in seeds of Arabidopsis transgenic plants overexpressing GhDGAT3D compared with that of control plants. GhDGAT genes function widely in cotton development and stress responses
physiological function
-
the enzyme is responsible for the biosynthesis of unsaturated fatty acids in vegetative organs of Paeonia rockii. PrDGAT3 may potentially interact with other genes in lipid synthesis and metabolism during plant development
physiological function
both diacylglycerol O-acyltransferase isoforms (DGAT1 and DGAT2) play a role in promoting fatty acid storage into triacylglycerol and lipid droplets to protect hepatocytes from oxidative damage. The enzyme catalyze the last step in the fatty acid esterification pathway
physiological function
acyl-CoA:diacylglycerol acyltransferase catalyzes the final committed step in triacylglycerol biosynthesis in eukaryotes. HpDGAT1 is the major triacylglycerol synthetase in Haematococcus lacustris. It can complement triacylglycerol biosynthesis in Saccharomyces cerevisiae H1246
physiological function
-
diacylglycerol acyltransferases catalyze the last and most critical step of triacylglycerol biosynthesis in the Kennedy pathway
physiological function
diacylglycerol O-acyltransferase 1 synthesizes triacylglycerides and is required for dietary fat absorption and fat storage in humans
physiological function
diacylglycerol acyltransferase 1 is the major enzyme that synthesizes triacylglycerols during Arabidopsis seed development
physiological function
acyltransferases (DGAT) 1 and 2 catalyse the final step in triacylglycerol synthesis, the esterification of fatty acyl-CoA to diacylglycerol. The two enzymes play distinct roles in triacylglycerol metabolism in skeletal muscle. DGAT1 is dominant in human skeletal muscle cells utilizing fatty acids derived from various sources, both exogenously supplied fatty acids, de novo synthesised fatty acids, or fatty acids derived from lipolysis, to generate triacylglycerol, as well as being involved in de novo synthesis of triacylglycerol. DGAT2 seems to be specialised for de novo synthesis of triacylglycerol from glycerol-3-posphate only. Diacylglycerol acyltransferase activities are also important for regulating fatty acid oxidation, indicating a key role in balancing fatty acids between storage in triacylglycerol and efficient utilization through oxidation
physiological function
activity of DGAT2 may play a key role in maintaining liver mitochondrial function and lipid homeostasis in dairy cows during the transition period
physiological function
GmDGAT3-2 displays a strong enzymatic activity to catalyze triacylglycerol assembly with high substrate specificity for monounsaturated fatty acids, particularly C18:1, playing an important role in the cytosolic pathway of triacylglycerol synthesis in soybean
physiological function
-
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
-
the conversion of diacylglycerol (DAG) to triacylglycerol (TAG) by DGAT1 is critical for plant freezing tolerance, acting by balancing TAG and phosphatidic acid (PA) production in Arabidopsis thaliana
-
physiological function
-
GhDGAT3D is involved in regulating oil biosynthesis and fatty acid composition of cotton seeds. Roles of GhDGAT3D in oil biosynthesis and fatty acid composition. Increase in C18:1 content and a decrease in C18:2 and C18:3 contents in seeds of Arabidopsis transgenic plants overexpressing GhDGAT3D compared with that of control plants. GhDGAT genes function widely in cotton development and stress responses
-
physiological function
-
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
-
physiological function
-
key enzyme involved in triacylglycerol synthesis
-
physiological function
-
diacylglycerol acyltransferases catalyze the last and most critical step of triacylglycerol biosynthesis in the Kennedy pathway
-
physiological function
-
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
Lobosphaera incisa SAG 2468
-
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
-
physiological function
Nannochloropsis oceanica CCAP 849/10
-
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
-
physiological function
Rhodotorula toruloides CGMCC 2.1389
-
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
-
physiological function
Rhodotorula toruloides CGMCC 2.1389
-
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
-
physiological function
Thraustochytrium roseum ATCC28210
-
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
-
physiological function
Haematococcus lacustris FACHB-712
-
potentially functional role of HpDGAT1 in astaxanthin esterification
-
additional information
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
three-dimensional model of the tDGAT protein, structure homology modeling
additional information
-
three-dimensional model of the tDGAT protein, structure homology modeling
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
-
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
-
quantification of triacylglycerol and analysis of fatty acid composition
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
-
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
-
determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
-
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
-
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
-
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
-
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
-
purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
-
DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
-
relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
-
the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Boechera stricta lines
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
-
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
-
additional information
-
three-dimensional model of the tDGAT protein, structure homology modeling
-
additional information
Lobosphaera incisa SAG 2468
-
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
-
Show AA Sequence and Transmembrane Helices (14252 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
13278
-
x * 13278, recombinant poly-His-tagged N-terminal enzyme fragment comprising residues 1-116, sequence calculation
13900
recombinant His-tagged cytosolic domain BnaDGAT11-113, gel filtration
24500
-
1 * 40800 + 2 * 28700 + 2 * 24500, complete structure of the native enzyme from soybean contains ten molecules of the pentameric enzyme, SDS-PAGE, amino acid analysis
28700
-
1 * 40800 + 2 * 28700 + 2 * 24500, complete structure of the native enzyme from soybean contains ten molecules of the pentameric enzyme, SDS-PAGE, amino acid analysis
40800
-
1 * 40800 + 2 * 28700 + 2 * 24500, complete structure of the native enzyme from soybean contains ten molecules of the pentameric enzyme, SDS-PAGE, amino acid analysis
45000
47000
47400
50000
56800
x * 56800, isoform DGAT1b, calculated from amino acid sequence
57100
x * 57100, isoform DGAT1a, calculated from amino acid sequence
60000
63000
x * 63000, calculated from amino acid sequence
64500
8600
recombinant His-tagged cytosolic domain BnaDGAT11-80, gel filtration
additional information
additional information
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MW 350000-370000, triacylglycerol synthetase complex, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
?
-
x * 13278, recombinant poly-His-tagged N-terminal enzyme fragment comprising residues 1-116, sequence calculation
?
1 * 21000, about, recombinant His-tagged cytosolic domain BnaDGAT11-113, sequence calculation, 1 * 10500, about, recombinant His-tagged autoinhibitory domain BnaDGAT11-80, sequence calculation
?
-
1 * 40800 + 2 * 28700 + 2 * 24500, complete structure of the native enzyme from soybean contains ten molecules of the pentameric enzyme, SDS-PAGE, amino acid analysis
?
x * 99000, mutant Dga1pDELTA19, sequence calculation, x * 90000, mutant Dga1pDELTA85, sequence calculation
?
-
x * 99000, mutant Dga1pDELTA19, sequence calculation, x * 90000, mutant Dga1pDELTA85, sequence calculation
-
?
-
x * 99000, mutant Dga1pDELTA19, sequence calculation, x * 90000, mutant Dga1pDELTA85, sequence calculation
-
dimer
the BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction
homodimer
DGAT1 can exist as either a homodimer or a homotetramer and the two forms have similar enzymatic activity
tetramer
DGAT1 can exist as either a homodimer or a homotetramer and the two forms have similar enzymatic activity
additional information
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analysis of self-associating properties of BnDGAT1(1116)His6 in an gel filtration approach, the recombinant N-terminal fragment associates to form tetramers
additional information
the full-length polypeptide is predominantly well folded (about 68% alpha-helices/beta-sheets), while the N-terminal domain only has about 29% alpha-helices/beta-sheets
additional information
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the full-length polypeptide is predominantly well folded (about 68% alpha-helices/beta-sheets), while the N-terminal domain only has about 29% alpha-helices/beta-sheets
additional information
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
additional information
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
additional information
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
additional information
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isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
additional information
isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
additional information
isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
additional information
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the native enzyme is presumably composed of 10 identical monomers each consisting of 3 different subunits with a ratio of 1:2:2
additional information
the enzyme protein structure is composed of a strongly hydrophilic N-terminal region of about 120 amino acids in MtDGAT1 followed by a long hydrophobic stretch (ca. 400 residues) with a predicted arrangement of 9-10 transmembrane helices that are likely to anchor the protein to the endoplasmic reticulum (ER) membrane
additional information
-
the enzyme protein structure is composed of a strongly hydrophilic N-terminal region of about 120 amino acids in MtDGAT1 followed by a long hydrophobic stretch (ca. 400 residues) with a predicted arrangement of 9-10 transmembrane helices that are likely to anchor the protein to the endoplasmic reticulum (ER) membrane
additional information
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
additional information
-
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex
additional information
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DGAT2 is part of a high molecular weight (about 650 kD) complex
additional information
three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet
additional information
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three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet
additional information
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three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, which lacks a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Major cleavage site lies between residues Lys29 and Ser30
additional information
phosphoprotein
BnaDGAT1 has a predicted SnRK1 phosphorylation site that appears to be conserved among plant DGAT1s. This site is localized in the cytosolic loop connecting the second and third predicted transmembrane segments in the TMHMM topology, indicating that it is accessible to cytoplasmic kinases. In vitro SnRK1-catalyzed phosphorylation of BnaDGAT1 results in a decrease in BnaDGAT1 activity
phosphoprotein
purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1. SnRK1 has also been found to act on the WRI transcription factor, which subsequently regulates DGAT expression
additional information
DGAT2 is degraded via the proteasome in a ubiquitin-dependent manner
additional information
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DGAT2 is degraded via the proteasome in a ubiquitin-dependent manner
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinnat truncated enzyme forms, BnaDGAT11-113 and BnaDGAT11-80, X-ray diffraction structure determination and analysis. Synchrotron small-angle X-ray scattering (SAXS) experiments are performed to obtain detailed 3D structural information on this disordered region of DGAT1, multi-state modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D137A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
G138A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
H132L
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highly conserved residue in acyltransferases, mutation results in strongly decreased activity
H133L
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highly conserved residue in acyltransferases, residue essential for catalytic activity
S205A
site-directed mutagenesis, mutant DGAT1m is less effective compared to wild-type in increasing seed mass, seed size and seed yield in the transgenic Camelina sativa plants when coexpressed with yeast GPD1
K232A
naturally occuring mutation, association with milk fatty acid composition
P178I
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mutation produces a drastic reduction of the neutral lipids content (yeast complementation experiment)
P178S
-
in this position S is invariantly found for acyl-CoA:diacylglycerol acyltransferase 1 proteins in plants and animals, mutation P178S does not have an appreciable effect on the synthesis on triacylglycerol (yeast complementation experiment)
A344T
substitution at position A344 substantially increases the selectivity of the enzyme toward ethanol and other shorter alcohols. An A344T substitution might affect the alcohol selectivity due to change of both steric effects and polarity changes near the active site
D145A
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the mutant is 5fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
D271A
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the mutant shows reduced activity compared to the wild type enzyme
H140A
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the mutant is 10fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
H141A
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the mutant is 5fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
L119A
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the mutant shows reduced activity compared to the wild type enzyme
N270A
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the mutant shows reduced activity compared to the wild type enzyme
R305A
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the mutant shows reduced activity compared to the wild type enzyme
A344T
Marinobacter nauticus DSM 8798
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substitution at position A344 substantially increases the selectivity of the enzyme toward ethanol and other shorter alcohols. An A344T substitution might affect the alcohol selectivity due to change of both steric effects and polarity changes near the active site
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C87S
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H161A
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site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
H161A/P162G/H163A
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site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
H163A
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site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
P162G
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site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme
S126A
H193E/G196S
mutation to corresponding motif found in plant, abolishes enzymic activity
additional information
additional information
expression of atfA in a quadruple mutant of Saccharomyces cerevisiae, lacking own DGAT and steryl ester synthase activites by disrupted DGA1, LRO1, ARE1 and ARE2, restores triacylglycerol but not steryl ester biosynthesis and results in the formation and accumulation of fatty acid ethyl and isoamyl esters, indicating that also eukaryotic systems are suitable hosts for atfA expression
additional information
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a recombinant acyl-CoA binding protein increased the activity of Arabidopsis thaliana DGAT1 expressed in insect cell culture by up to 70%, overexpression of AtDGAT1 cDNA from Arabidopsis does not complement the knocked-out acyl-CoA:cholesterol acyltransferases, ACAT, EC 2.3.1.26, in a yeast double-mutant
additional information
a recombinant acyl-CoA binding protein increased the activity of Arabidopsis thaliana DGAT1 expressed in insect cell culture by up to 70%, overexpression of AtDGAT1 cDNA from Arabidopsis does not complement the knocked-out acyl-CoA:cholesterol acyltransferases, ACAT, EC 2.3.1.26, in a yeast double-mutant
additional information
engineering transgenic Camelina sativa plants for enhanced oil and seed yields by combining heterologous expression of Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and Saccharomyces cerevisiae cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes under the control of seed-specific promoters. Plants co-expressing DGAT1 and GPD1 exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. Further, DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-co-expressing lines is almost twofold higher as compared to wild-type and the lines expressing DGAT1 and GPD1 alone. Evaluation of the effect of stacking the two genes on achieving a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increasing the oil yield. GDP1 and DGAT1 overexpression has no effect on seed germination and early seedling growth
additional information
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engineering transgenic Camelina sativa plants for enhanced oil and seed yields by combining heterologous expression of Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and Saccharomyces cerevisiae cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes under the control of seed-specific promoters. Plants co-expressing DGAT1 and GPD1 exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. Further, DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-co-expressing lines is almost twofold higher as compared to wild-type and the lines expressing DGAT1 and GPD1 alone. Evaluation of the effect of stacking the two genes on achieving a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increasing the oil yield. GDP1 and DGAT1 overexpression has no effect on seed germination and early seedling growth
additional information
generation of plant mutant dgat1-1 (CS3861) by methanesulfonate, and of T-DNA insertional mutant dgat1-2 (SALK_039456), phenotypes, comparison of lipid compositions and contents in wild-type and mutant leaves and seeds, detailed overview
additional information
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generation of plant mutant dgat1-1 (CS3861) by methanesulfonate, and of T-DNA insertional mutant dgat1-2 (SALK_039456), phenotypes, comparison of lipid compositions and contents in wild-type and mutant leaves and seeds, detailed overview
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additional information
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recombinant overexpression of AtDGAT1 leads to increased freezing tolerance in Boechera stricta seedlings, phenotypes. BstDGAT1 sequence polymorphisms in the upstream regulatory regions, the LTM allele contains several potential cis-regulatory elements involved in abiotic stress responses that are missing from SAD12 due to SNPs. Quantitative lipidomics analysis of control, cold-acclimated, and cold-acclimated freezing-treated plants, overview
additional information
construction of truncated enzyme mutants, BnaDGAT11-113 comprises the full-length cytoplasmic domain, and BnaDGAT11-80 comprises the autoinhibitory domain, the truncated proteins are non-globular and monomeric in vitro
additional information
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construction of truncated enzyme mutants, BnaDGAT11-113 comprises the full-length cytoplasmic domain, and BnaDGAT11-80 comprises the autoinhibitory domain, the truncated proteins are non-globular and monomeric in vitro
additional information
directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of several BnaDGAT1 variants with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
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directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of several BnaDGAT1 variants with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
construction of truncated enzyme versions, BnaDGAT11-113 and BnaDGAT181-501. Yeast transformed with BnaDGAT181-501 with N-terminal Nub tag and SnRK1 with N-terminal Cub tag grew on selective media. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation
additional information
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construction of truncated enzyme versions, BnaDGAT11-113 and BnaDGAT181-501. Yeast transformed with BnaDGAT181-501 with N-terminal Nub tag and SnRK1 with N-terminal Cub tag grew on selective media. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation
additional information
construction of several truncated enzyme versions of isozyme BnaC.DGAT1.a, BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501,which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site
additional information
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construction of several truncated enzyme versions of isozyme BnaC.DGAT1.a, BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501,which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site
additional information
directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of analogous mutant variants of Camelina sativa with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
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directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of analogous mutant variants of Camelina sativa with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein AtACBP6 from Arabidosis thaliana (UniProt ID P57752), generation of N-terminally truncated DGAT1 versions as fusion proteins: ACBP-CzDGAT11-550, ACBP-CzDGAT181-550, and ACBP-CzDGAT1107-550. The coding sequences of AtACBP6 and variant CzDGAT1s are individually amplified and the resulting amplicons are fused using overlap extension PCR. Fusion of ACBP to the N-terminus of the full-length CzDGAT1 not only augments the protein accumulation levels in yeast and tobacco leaves but also kinetically improves the enzyme. ACBP-fused DGAT1 is more effective in improving the oil contents of yeast cells and vegetative tissues than the native DGAT1
additional information
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kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein AtACBP6 from Arabidosis thaliana (UniProt ID P57752), generation of N-terminally truncated DGAT1 versions as fusion proteins: ACBP-CzDGAT11-550, ACBP-CzDGAT181-550, and ACBP-CzDGAT1107-550. The coding sequences of AtACBP6 and variant CzDGAT1s are individually amplified and the resulting amplicons are fused using overlap extension PCR. Fusion of ACBP to the N-terminus of the full-length CzDGAT1 not only augments the protein accumulation levels in yeast and tobacco leaves but also kinetically improves the enzyme. ACBP-fused DGAT1 is more effective in improving the oil contents of yeast cells and vegetative tissues than the native DGAT1
additional information
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when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
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when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
the type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants are created, library screening, and effect on Corylus americana seed composition, detailed overview. The corresponding amino acid substitutions are repeated in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, analysis of effect on soybean seed composition
additional information
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the type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants are created, library screening, and effect on Corylus americana seed composition, detailed overview. The corresponding amino acid substitutions are repeated in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, analysis of effect on soybean seed composition
additional information
among the three DGAT2-like genes, only CpuDGAT2C functionally complements TAG biosynthesis in Saccharomyces cerevisiae mutant H1246 cells. Expression of CpuDGAT1 in the TAG-deficient Saccharomyces cerevisiae mutant strain H1246. CpuDGAT1 is able to rescue lipotoxicity of Saccharomyces cerevisiae H1246 cells grown in exogenous 0.25 mM C8:0 or C10:0, but not C18:1. Seed-specific recombinant CpuDGAT1 overexpression in Camelina sativa enhances C10:0 content in Camelina seeds. Coexpression of CpuDGAT1 and CvLPAT2 promotes accumulation of 10:0 at the TAG sn-2 position. Fatty acid composition of TAG and sn-2 position of TAG in mature seeds of wild-type camelina and camelina lines engineered for expression of CvFatB1 alone or with combinations of CpuDGAT1 and CvLPAT2, overview. CpuDGAT1 and CvLPAT2 coexpression increases 10:0 accumulation in DAG, but little 10:0 accumulation is detected in phosphatidylcholine (PC). Seed phenotype analysis
additional information
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functional overexpression of CeDGAT2b in yeast mutant and Arabidopsis TAG1 mutant and wild-type lines not only enhances TAG contents but also modifies the fatty acid compositions of TAG. The expression of CeDGAT2b rescues the seed phenotype of Arabidopsis thaliana TAG1 mutant ABX45
additional information
construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
additional information
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construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
additional information
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construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
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additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
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TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
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TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
a type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants from a screened library are created, then the corresponding amino acid substitutions are made in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, effect on soybean seed composition, detailed overview
additional information
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a type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants from a screened library are created, then the corresponding amino acid substitutions are made in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, effect on soybean seed composition, detailed overview
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
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the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
Lobosphaera incisa SAG 2468
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the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
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additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
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short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
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short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
an isoform DGAT2 mutant lacking both its transmembrane domains still associates with membranes, but is absent from the endoplasmic reticulum and instead localizes to mitochondria. The mutant is still active and capable of interacting with lipid droplets to promote triacylglycerol storage. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, fail to co-localize with lipid droplets when cells are loaded with oleate to stimulate triacylglycerol synthesis
additional information
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an isoform DGAT2 mutant lacking both its transmembrane domains still associates with membranes, but is absent from the endoplasmic reticulum and instead localizes to mitochondria. The mutant is still active and capable of interacting with lipid droplets to promote triacylglycerol storage. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, fail to co-localize with lipid droplets when cells are loaded with oleate to stimulate triacylglycerol synthesis
additional information
construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview
additional information
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construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview
additional information
generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
additional information
generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
additional information
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generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
additional information
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disruption of gene tgs1, i.e. Rv3130c, leads to drastically reduced triacylglycerol accumulation
additional information
generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
additional information
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generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
additional information
Nannochloropsis oceanica CCAP 849/10
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generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
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additional information
construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
additional information
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construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
additional information
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deletion in the N-terminal region (SbDGAT1-1(39-515) and SbDGAT1-1(89-515)) results in decreased accumulation of triacylglycerol and fatty acids (16:0 and 18:0) when compared to the SbDGAT1-1 variant expressed in yeast H1246 strain
additional information
construction of a SCO0958 deletion mutant shows that the protein is responsible for biosynthesis of a significant amount of triacylglycerol
additional information
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generation of an atfG25OMEGAApr insertion mutant of Streptomyces sp. G25
additional information
expression of recombinant TmDGAT1 in the yeast H1246MATalpha quadruple mutant (DGA1, LRO1, ARE1, ARE2) restores the capability of the mutant host to produce triacylglycerols
additional information
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expression of recombinant TmDGAT1 in the yeast H1246MATalpha quadruple mutant (DGA1, LRO1, ARE1, ARE2) restores the capability of the mutant host to produce triacylglycerols
additional information
in plant transformation studies, seed-specific expression of TmDGAT1 is able to complement the low TAG/unusual fatty acid phenotype of the Arabidopsis AS11 (DGAT1) mutant
additional information
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in plant transformation studies, seed-specific expression of TmDGAT1 is able to complement the low TAG/unusual fatty acid phenotype of the Arabidopsis AS11 (DGAT1) mutant
additional information
overexpression of TmDGAT1 in wild-type Arabidopsis and high-erucic-acid rapeseed (HEAR) and canola Brassica napus results in an increase in oil content (3.5%-10% on a dry weight basis, or a net increase of 11%-30%)
additional information
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overexpression of TmDGAT1 in wild-type Arabidopsis and high-erucic-acid rapeseed (HEAR) and canola Brassica napus results in an increase in oil content (3.5%-10% on a dry weight basis, or a net increase of 11%-30%)
additional information
site-directed mutagenesis is conducted on six putative functional regions/motifs of the TmDGAT1 enzyme. Mutagenesis of a serine residue in a putative SnRK1 target site results in a 38%-80% increase in DGAT1 activity, and over-expression of the mutated TmDGAT1 in Arabidopsis results in a 20%-50% increase in oil content on a per seed basis
additional information
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site-directed mutagenesis is conducted on six putative functional regions/motifs of the TmDGAT1 enzyme. Mutagenesis of a serine residue in a putative SnRK1 target site results in a 38%-80% increase in DGAT1 activity, and over-expression of the mutated TmDGAT1 in Arabidopsis results in a 20%-50% increase in oil content on a per seed basis
additional information
construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
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additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
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additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
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additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
65
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes, decrease in activity with buffers such as bis-Tris, HEPES, morpholinoethanesulfonic acid
MgCl2 accelerates loss of activity during storage at 4°C, dilution increases stability, cholate-solubilized activity is more stable than deoxycholate-solubilized activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, more than 50% of activity retained after 4 days in 0.25 M phosphate buffer
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4°C, 20-30% loss of activity after 24 h, cholate solubilized enzyme, dilution restores activity
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4°C, about 65-85% loss of activity after 24 h, deoxycholate solubilized enzyme, partially restorable by dialysis against buffer lacking detergent
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4°C, inactivation after 24 h in the presence of 8 mM MgCl2, deoxycholate solubilized enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cation-exchange chromatography, hydrophobic interaction chromatography, anion-exchange chromatography
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native enzyme 1724fold from developing cotyldons by hydrophobic interaction and adsorption chromatography, followed by gel filtration and heparin affinity chromatography to homogeneity
native enzyme from tissue culture partially by microsome preparation
native enzyme partially by microsome preparation
partial
preparation of TAG-deficient Saccharomyces cerevisiae mutant strain H1246 in microsomes with recombinant CzDGAT2 isozymes
purified enzyme is obtained by cation exchange chromatography, hydrophobic interaction chromatography and subsequent ion exchange chromatography
recombinant biotinylated FLAG- or myc-tagged DGAT-2 fused to biotin ligase from HEK-293T cells, biotinylated proteins are captured with magnetic streptavidin beads
recombinant BnaDGAT1 from Saccharomyces cerevisiae strain H1246 microsomes, purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme cytoplasmic and autoinhibitory domains BnaDGAT11-113 and BnaDGAT11-80 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography. TEV protease tag cleavage as well as enzyme protein concentration after affinity chromatography lead to protein aggregation and are omitted
recombinant His-tagged enzyme from Escherichia coli strain C41(DE3) by ultracentrifugation and nickel affinity chromatography
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recombinant MBP-tagged wild-type enzyme and mutants from Escherichia coli strain BL21(DE3) pLysS by amylose affinity chromatography and gel filtration
recombinant poly-His-tagged N-terminal fragment of the enzyme, i.e. BnDGAT1(1116)His6, from Escherichia coli strain BL21(DE3)
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recombinant soluble N-terminally His-tagged enzyme 19.2fold from Escherichia coli strain BL21(DE3) by cation exchange and nickel affinity chromatography
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solubilization in n-dodecyl-beta-D-maltopyranoside, cobalt affinity chromatography, and Superdex 200 gel filtration
wild-type enzyme DGAT in microsomes
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a single locus is identified that contains the gene encoding BstDGAT1, whose expression is highly cold-responsive, identification of the SKI (QTL seedling koude intolerance) locus in Boechera stricta, quantitative enzyme expression analysis
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chromosomal location, expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells and in COS-7 cells
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DGAT1, a single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional overexpression in tobacco plants
DGAT1, DNA and amino acid sequence determination and analysis
DGAT1, DNA and amino acid sequence determination and analysis, phylogenetic tree
DGAT1, functional expression of the FLAG-tagged enzyme in membranes of Spodoptera frugiperda Sf9 cells and in COS-7 cells, expression analysis
DGAT2, DNA and amino acid sequence determination and analysis, DGAT2 is a truncated enzyme version, phylogenetic tree
DGAT2, functional expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells, expression analysis
DGATsv, splice variant, deletion of 101 residues from the C-terminus, enzymatically inactive
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DNA and amino acid sequence determination and analysis, phylogenetic tree
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DNA and amino acid sequence determination and analysis, phylogenetic tree, expression in insect cells
expressed in a baculovirus expression system
expressed in a Saccharomyces cerevisiae H1246MATa quadruple mutant that is defective in triacylglycerol synthesis
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expressed in Arabidopsis thaliana and Saccharomyces cerevisiae H1246 triacylglycerol-deficient mutant
expressed in Escherichia coli
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae mutant H1246
expressed in Saccharomyces cerevisiae mutant H1246 and in soybean hairy roots
expressed in Saccharomyces cerevisiae strain H1246
expression as His-tagged enzyme in Escherichia coli strain BL21 (DE3), phylogenetic analysis
expression as soluble N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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expression in Saccharomyces cerevisiae H1246 and Nicotiana benthamiana. Functional complementation assay using triacylglycerol-deficient yeast (Saccharomyces cerevisiae) mutant H1246 demonstrates that GmDGAT3-2 fully restores triacylglycerol biosynthesis in the yeast and preferentially incorporates monounsaturated fatty acids, especially oleic acid (C18:1) into triacylglycerols. Heterogeneous expression of GmDGAT3-2 results in a significant increase in seed oil and C18:1 levels but little change in contents of protein and starch compared to the EV-transformed tobacco plants
expression in Saccharomyces cerevisiae, Chlamydomonas reinhardtii and Arabidopsis thaliana
expression in Sacharomyces cerevisiae H1246
expression in Sacharomyces cerevisiae H1246. HpDGAT2A has the capacity to restore triacylglycerol synthesis in triacylglycerol-deficient Saccharomyces cerevisiae (H1246)
expression in Sacharomyces cerevisiae H1246. HpDGAT2B has the capacity to restore triacylglycerol synthesis in triacylglycerol-deficient Saccharomyces cerevisiae (H1246)
expression in Sacharomyces cerevisiae H1246. HpDGAT2D has the capacity to restore triacylglycerol synthesis in triacylglycerol-deficient Saccharomyces cerevisiae (H1246). Heterologous expression of HpDGAT2D in Arabidopsis thaliana and Chlamydomonas reinhardtii significantly increases the triacylglycerol content and promotes the monounsaturated fatty acyl-CoA and polyunsaturated fatty acyl-CoA contents
expression in Sacharomyces cerevisiae H1246. HpDGAT2E has the capacity to restore triacylglycerol synthesis in triacylglycerol-deficient Saccharomyces cerevisiae (H1246). Heterologous expression of HpDGAT2D in Arabidopsis thaliana and Chlamydomonas reinhardtii significantly increases the triacylglycerol content and promotes the monounsaturated fatty acyl-CoA and polyunsaturated fatty acyl-CoA contents
expression in Sacharomyces cerevisiae H1246. Transient expression in Nicotiana benthamiana leaves
expression of Myc-tagged DGAT1 and DGAT2 in Saccharomyces cerevisiae, co-expression with N- and C-terminally myc-tagged DGAT1 or DGAT2, and GFP-tagged DGAT2 in Nicotiana tabacum BY-2 cells in endoplasmic reticulum membranes oriented toward the cytosolic side
expression of Myc-tagged DGAT1 in Saccharomyces cerevisiae, co-expression with N- and C-terminally myc-tagged DGAT1
expression of Myc-tagged DGAT2 in Saccharomyces cerevisiae, co-expression with N- and C-terminally myc-tagged DGAT2, and GFP-tagged DGAT2 in Nicotiana tabacum BY-2 cells in endoplasmic reticulum membranes oriented toward the cytosolic side
expression of the poly-His-tagged N-terminal fragment of the enzyme, i.e. BnDGAT1(1116)His6, in Escherichia coli strain BL21(DE3), BnDGAT1(1116)His6 fails to react with protein in microsomal vesicles following treatment with proteinase K, and thus might be localized to the cytosolic side of the ER
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gene atfG25, DNA and amino acid sequence determination and analysis, geneomic structure, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain C41(DE3)
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gene BnaDGAT1.a, sequence comparisons and phylogenetic analysis, recombinant expression of tagged enzyme BnaDGAT1.a in Saccharomyces cerevisiae strain H1246, deficient in TAG synthesis
gene BnaDGAT1.b, sequence comparisons and phylogenetic analysis, recombinant expression of tagged enzyme BnaDGAT1.a in Saccharomyces cerevisiae strain H1246, deficient in TAG synthesis
gene CoDGAT2, sequence comparisons, recombinant expression in and complementation of Saccharomyces cerevisiae strain H1246 that is deficient in trinacylglycerol (TAG) production. Seed-specific overexpression of CoDGAT2 in Arabidopsis thaliana leads to a significant increase in the linoleic acid (C18:2) content (approximately 6%) compared to wild-type. In contrast, the proportions of eicosadienoic acid (C20:1) and arachidic acid (C20:0) are decreased, quantitative RT-PCR expression analysis
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gene DC3, location of DC3 on the X chromosome at Xq13.1, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae
gene DGAT, genetic organization, DNA and amino acid sequence dteermination and analysis
gene DGAT1, BnaDGAT1 is recombinantly expressed using a codon-optimized cDNA in Saccharomyces cerevisiae strain H1246 microsomes, recombinant expression of truncated enzyme mutants in Saccharomyces cerevisiae strain H1246 microsomes
gene DGAT1, DNA and amino acid sequence determination and analysis, expression analysis of DGAT1 and DGAT2, expression in Saccharomyces cerevisiae microsomes, phylogenetic analysis
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gene DGAT1, DNA and amino acid sequence determination and analysis, sequence comparison, RT-PCR expression analysis, recombinant expression in seeds of Camelina sativa. Microsomes of Camelina sativa seeds engineered for CpuDGAT1 expression display DGAT activity with 10:0-CoA and the diacylglycerol didecanoyl, that is approximately 4fold higher than that in camelina seed microsomes without CpuDGAT1, coexpression with a Cuphea viscosissima FatB thioesterase (CvFatB1) that generates 10:0 results in TAGs with nearly 15 mol% of 10:0. Recombinant expression of CpuDGAT1 and CvFatB1 with CvLPAT2, a 10:0-CoA-specific Cuphea LPAT, increases 10:0 amounts to 25 mol% in camelina seed TAG. These TAGs contain up to 40 mol% 10:0 in the sn-2 position, nearly double the amounts obtained from coexpression of CvFatB1 and CvLPAT2 alone. Although enriched in diacylglycerol, 10:0 is not detected in phosphatidylcholine in these seeds. Recombinant functional expression of CpuDGAT1 in the TAG-deficient Saccharomyces cerevisiae mutant strain H1246. CpuDGAT1 is able to rescue lipotoxicity of Saccharomyces cerevisiae H1246 cells grown in exogenous 0.25 mM C8:0 or C10:0, but not C18:1
gene DGAT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, semiquantitative RT-PCR enzym expression analysis, functional recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 and complementation, lipid analysis, overview
gene DGAT1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli and Saccharomyces cerevisiae double null strain DELZTADGA1/DELTALRO1, recombinant expression of mutant CaDGAT1 in Glycine max
gene DGAT1, recombinant expression of N-terminally His-tagged enzyme cytoplasmic and autoinhibitory domains, BnaDGAT11-113 and BnaDGAT11-80, in Escherichia coli strain BL21(DE3), method optimization and evaluation, overview. The tag is located at the disordered N-terminal region, which is distal to the folded C-terminal region and the primary ligand binding site. Hence tag-induced secondary structure elements, if any, might not influence the ligand binding properties
gene DGAT1, recombinant expression of the isozyme in Spodoptera frugiperda Sf9 cells via baculovirus transfection method
gene DGAT1, seed-specific co-overexpression of AtDGAT1 and ScGPD1 codon-optimized genes in Camelina sativa cv. Suneson, increasing seed mass, seed size and seed yield in the transgenic plants, recombinant co-expression also with mutant DGATm, the glycinin promoter from Glycine max is selected to drive the expression of DGAT1, transfection using the Agrobacterium tumefaciens strain GV3101 method. Quantitative real-time PCR enzyme expression analysis and phenotypes, overview
gene DGAT1, sequence comparisons, recombinant expression of wild-type and mutant enzymes, recombinant expression in Escherichia coli and Saccharomyces cerevisiae double null strain DELZTADGA1/DELTALRO1
gene DGAT1, single copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of DGAT isozymes, recombinant expression in the TAG-deficient Saccharomyces cerevisiae strain H1246, LiDGATs of type 1 and 2 do not co-localize with each other at least in yeast
gene DGAT1, transient expression of N-terminally truncated CzDGAT1 variants and of the ACBP-fused versions in Nicotiana benthamiana leaves for lipid production using the transformation method via Agrobacterium tumefaciens GV3101 cells
gene DGAT1A, functional recombinant expression in Saccharomyces cerevisiae mutant strain H1246 and in Saccharomyces cerevisiae wild-type strain YPH499a, isozyme GmDGAT1A complements the TAG deficiency of mutant strain H1246. Recombinant expression in Arabidopsis thaliana using the Agrobacterium tumefaciens GV3101 transfection method. Quantitative RT-PCR enzyme expression analysis. Determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration
gene DGAT1A, recombinant expression of isozyme AtDGAT1A in Saccharomyces cerevisiae strain INVSc1 microsomes, very low expression level, lipid analyses, overview
gene DGAT1A, recombinant expression of isozyme ElDGAT1A in Spodoptera frugiperda Sf9 insect cells via recombinant baculovirus transfection method, lipid analyses, overview
gene DGAT1A, recombinant expression of isozyme GmDGAT1A in Saccharomyces cerevisiae strain INVSc1 microsomes, and in Spodoptera frugiperda Sf9 insect cells via recombinant baculovirus transfection method, low expression level, lipid analyses, overview
gene DGAT1A, recombinant expression of isozyme VgDGAT1A in Saccharomyces cerevisiae strain INVSc1 microsomes, and in Spodoptera frugiperda Sf9 insect cells via recombinant baculovirus transfection method, lipid analyses, overview
gene DGAT1B, recombinant expression of isozyme GmDGAT1B in Spodoptera frugiperda Sf9 insect cells via recombinant baculovirus transfection method, lipid analyses, overview
gene DGAT1B, recombinant expression of isozyme VgDGAT1B in Saccharomyces cerevisiae strain INVSc1 microsomes, and in Spodoptera frugiperda Sf9 insect cells via recombinant baculovirus transfection method, lipid analyses, overview
gene DGAT2, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons, and phylogenetic analysis, recombinant overexpression of FLAG-tagged enzyme DGAT2 in Nannochloropsis oceanica cells, real-time quantitative PCR expression analysis
gene DGAT2, DNA and amino acid sequence determination and analysis, recombinant expression of NeoDGAT2 cDNA under the control of HSP70-RBCS2 (AR) promoter or beta2-tubulin (beta2-Tub) promoter, both of Chlamydomonas reinhardtii from plasmids pAR-DGAT2 and pB2-DGAT2 in Neochloris oleoabundans cells
gene DGAT2, expression of FLAG-tagged wild-type and mutant enzyme in COS-7 cells
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gene DGAT2, identified from a transcriptome database, DNA and amino acid sequence determination and analysis of DGAT2 isozymes, DGAT2A, DGAT2B, DGAT2D, and DGAT2E, sequence comparisons and phylogenetic analysis, recombinant expression in TAG-deficient Saccharomyces cerevisiae strain H1246. Triacylglycerol (TAG) is synthesized with expression of HpDGAT2A and HPDGAT2D, but no TAG is detected in cells expressing HpDGAT2B and HpDGAT2E
gene DGAT2, localization of DGAT2 at 11q13.5, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae
gene DGAT2.1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of DGAT isozymes, recombinant expression in the TAG-deficient Saccharomyces cerevisiae strain H1246, LiDGATs of type 1 and 2 do not co-localize with each other at least in yeast
gene DGAT2B, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, subcloning in Escherichia coli strain DH5alpha, recombinant expression of wild-type (MaDGAT2) Mortierella alpina gene in and complementation of Saccharomyces cerevisiae strain H1246 defective in synthesis of neutral lipid, lipid analysis of the lipid content of the recombinant culture harboring MaDGAT2 gene
KY859195, A0A2D2CI94
gene DGAT2D, functional recombinant expression in Saccharomyces cerevisiae mutant strain H1246 and in Saccharomyces cerevisiae wild-type strain YPH499a, isozyme GmDGAT2D complements the TAG deficiency of mutant strain H1246. Recombinant ectopic GmDGAT2D expression in soybean hairy roots, recombinant expression in Arabidopsis thaliana using the Agrobacterium tumefaciens GV3101 transfection method. Quantitative RT-PCR enzyme expression analysis. Determination of the subcellular localization of GmDGAT-GFP performed by using tobacco leaf infiltration
gene DGAT3, Arabidopsis thaliana contains a single DGAT3 gene, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
gene DGAT3, Glycine max contains 2 DGAT3 genes, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
gene DGAT3, heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246
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gene DGTT1, quantitative real-time PCR enzyme expression analysis, recombinant expression of the isozyme in TAG-deficient Saccharomyces cerevisiae strain H1246 microsomes, expression of CrDGTT1 restores TAG biosynthesis
gene DGTT2, quantitative real-time PCR enzyme expression analysis, recombinant expression of the isozyme in TAG-deficient Saccharomyces cerevisiae strain H1246 microsomes, expression of CrDGTT2 restores TAG biosynthesis
gene DGTT3, quantitative real-time PCR enzyme expression analysis, recombinant expression of the isozyme in TAG-deficient Saccharomyces cerevisiae strain H1246 microsomes, expression of CrDGTT3 restores TAG biosynthesis
gene MaDGAT, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression in Saccharomyces cerevisiae strain H1246
gene mMaDGAT2B, subcloning in Escherichia coli strain DH5alpha, synthetic gene after codon-optimization, recombinant expression of codon-optimized (mMaDGAT2) Mortierella alpina gene in and complementation of Saccharomyces cerevisiae strain H1246 defective in synthesis of neutral lipid, lipid analysis of the lipid content of the recombinant culture harboring mMaDGAT2 gene
KY859195, A0A2D2CI94
gene Rv3371, specific to pathogenic mycobacteria, leads to modifications in colony morphotype, bacterial architecture, cell surface properties, and to elevated triacylglycerol (TAG) levels when expressed in Mycolicibacterium smegmatis (Mycobacterium smegmatis)
gene SiDGAT1, DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic analysis, quantitative real-time PCR expression analysis, functional recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 and complementation, higher oil content in SiDGAT gene-transformed mutants, lipid analysis, overview
M1E7W9, XP_011098009
gene SiDGAT2, DNA and amino acid sequence determination and analysis, genetic structure, phylogenetic analysis, quantitative real-time PCR expression analysis, functional recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 and complementation, higher oil content in SiDGAT gene-transformed mutants, lipid analysis, overview
M1E7W9, XP_011098009
gene Tcur_3818, DNA and amino acid sequence determination and analysis, recombinant expression of DGAT in Escherichia coli triggering rapid triglyceride accumulation in Escherichia coli. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells
gene tgs1, expressionin Escherichia coli, the recombinant enzyme prefers C26 : 0-CoA for triglycerol accumulation
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gene WSD, Glycine max contains a single WSD gene, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
gene WSD1, Arabidopsis thaliana contains 11 WS/DGAT genes, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
gene WSD4, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta (DE3), recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 results in the accumulation of wax esters, but not any detectable triacylglycerols (TAGs), indicating a predominant wax synthase (WS) activity in yeast
gene WSD5, phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta (DE3), recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 results in the accumulation of wax esters, but not any detectable triacylglycerols (TAGs), indicating a predominant wax synthase (WS) activity in yeast
gene YALI0_E32769g, sequence comparisons, recombinant expression of MBP-tagged wild-type enzyme and mutants in Escherichia coli strain BL21(DE3) pLysS
gene YlDGA1, overexpression in DGAT-deleted Yarrowia lipolytica strain Q4 (JMY1877), subcloning in Escherichia coli
gene YlDGA2, overexpression in DGAT-deleted Yarrowia lipolytica strain Q4 (JMY1877), subcloning in Escherichia coli
genes CeDGAT1, CeDGAT2a, and CeDGAT2b, functional overexpression of the isozymes in yeast mutant strain H1246, and in Arabidopsis thaliana seeds of TAG1 mutant and wild-type lines via Agrobacterium tumefaciens strain EHA105 transfection method, quantitative RT-PCR enzyme expression analysis
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heterologous expression of the 35S::IpDGAT2 in Arabidopsis thaliana
isoform DGAT2 is expressed in Saccharomyces cerevisiae mutant strain H1246
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isozyme BnaC.DGAT1.a, recombinant expression of wild-type and truncated mutant enzymes in Saccharomyces cerevisiae strain H1246, which is devoid of TAG biosynthesis
phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain delta4
quantitative PCR expression analysis of PtDGATX, comparison of isozyme transcription levels and dynamics
quantitative PCR expression analysis of PtDGATX, comparison of isozyme transcription levels and dynamics, gene expression analysis, functional recombinant expression of His6-tagged DGATX using promoters of fcpA and fcpB genes (and fcpA terminators) in Saccharomyces cerevisiae strain H1246 that is deficient in TAG biosynthesis, a substantial amount of wax ester is detected in H1246-PtDGAT, indicating the dual function of PtDGATX. Endogenous overexpression of PtWS/DGAT. In H1246-PtWS/DGAT, TAG and wax ester account for 10.51 and 5.17%, respectively, of the total lipids. C16:1 and C18:1 are the dominant fatty acid species in total lipids, fatty acid content of total lipid in Saccharomyces cerevisiae, overview
recombinant expression in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 in microsomes
recombinant expression of CzDGAT2 isozymes in TAG-deficient Saccharomyces cerevisiae mutant strain H1246 in microsomes
recombinant expression of FLAG- or myc-tagged DGAT-2 fused to biotin ligase in HEK-293T cells and in COS-7 cells
RtDGATa, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme RtDGATa in Saccharomyces cerevisiae TAG-deficient quadruple mutant strain H1246, subcloning in Escherichia coli Top10 cells. The expression of RtDGATa does not alter the TAG content in Saccharomyces cerevisiae strain H1246
RtDGATb, sequence comparisons and phylogenetic analysis, recombinant expression of isozyme RtDGATb in Saccharomyces cerevisiae TAG-deficient quadruple mutant strain H1246, subcloning in Escherichia coli Top10 cells. The expression of RtDGATb completely resumes TAG biosynthesis in Saccharomyces cerevisiae strain H1246
short-term hepatic overexpression of DGAT1 in mice using adenoviral vectors results in 2.0fold increases in the triglyceride content of liver, the increase in hepatic triglyceride content has no effect on the production rate of VLDL triglyceride or apoB
short-term hepatic overexpression of DGAT2 in mice using adenoviral vectors results in 2.4fold increases in the triglyceride content of liver, the increase in hepatic triglyceride content has no effect on the production rate of VLDL triglyceride or apoB
the enzyme without the N-terminal 29 amino acids is expressed in Saccharomyces cerevisiae mutant DELTAdga1
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transient overexpression in Nicotiana benthamiana leaf tissue and stable overexpression in Arabidopsis thaliana. Overexpression of PrDGAT3 functionally recovers oil biosynthesis in triacylglycerol-deficient Saccharomyces cerevisiae H1246
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DGAT1, DNA and amino acid sequence determination and analysis, phylogenetic tree
DGAT1, DNA and amino acid sequence determination and analysis, phylogenetic tree
DGAT1, DNA and amino acid sequence determination and analysis, phylogenetic tree
expression in Sacharomyces cerevisiae H1246
phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain delta4
phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain delta4
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of DGAT1 by a phenylalanine insertion in the maize (Zea mays) DGAT1
both the genes i.e. SbDGAT1-1 and SbDGAT1-2, show similar fold expression on 10 days after pollination. The expression of SbDGAT1-2 in bran increases with a peak level of 11.5fold whereas SbDGAT1-1 remains feebly expressed. Subsequently, SbDGAT1-2 expression drops gradually to 2.1fold until 30 days after pollination. During the embryo development, SbDGAT1-1 expression moderately increases at the early stages (from 15 to 20 days after pollination) followed by a marked drop in the expression level until 30 days after pollination. The SbDGAT1-2 gene shows moderate to elevated expression level at the initial two stages of the embryo development followed by a gradual reduction in the expression level at the later two stages. The expression profile of SbDGAT1-1 and SbDGAT1-2 in developing endosperm remains low at 15 days after pollination
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DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought. The WRI transcription factor regulates DGAT expression
enzyme expression is significantly increased by 800 mM NaCl, 20% (w/v) polyethylene glycol, and 15% (w/v) sucrose treatments
GmDGAT2D is upregulated by cold and heat stress and abscisic acid signaling
high expression of DGAT1 in hepatocytes from cows experiencing fatty liver
in response to high light stress expression of HpDGAT1 increases significantly at 72 h
induced expression in seedlings at low temperature, BstDGAT1 expression is highly cold-responsive and correlates with freezing tolerance in the two Boechera stricta lines
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isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses
mRNA level is remarkably higher in the old leaves than in young developing leaves
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successful introduction of the triacylglycerol biosynthesis pathway in gamma-proteobacteria, in an industrially appropriate microorganism, method development and optimization, overview. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells. Optimization of fluorescence techniques for the detection of in situ TAG accumulation, Nile Red staining
the expression level of the HpDGAT2A gene markedly increases under high light and nitrogen deficient conditions
the expression level of the HpDGAT2DE gene markedly increases under high light and nitrogen deficient conditions
the expression level of the HpDGAT2E gene markedly increases under high light and nitrogen deficient conditions
the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Brassica stricta lines
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the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter
the Rv3371 promoter is minimally active during exponential growth in vitro, but is upregulated under stationary phase, hypoxia, nutrient starvation, nitrosative stress, low iron, in IFN-gamma activated macrophages and infected mice. The low iron-induced expression of Rv3371 is likely due to the de-repression by Rv1404, which is probably activated by ideR
the three PtDGAT genes are all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs are markedly different. PtDGAT1 shows transient upregulation, with its transcript levels peaking at 1 day following the onset of N depletion and declining slightly thereafter
the three PtDGAT genes are all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs are markedly different. The transcript levels of PtDGATX increases more slowly and continuously, peaking at 4 days. Engineering PtWS/DGAT for increased lipid productivity, overview. Combined with the elevated lipid and TAG content, the genetically modified Phaeodactylum tricornutum cells are quite capable of photoautotrophic growth, absorbing CO2 and producing (especially) biomass, lipids, and TAG
the three PtDGAT genes were all upregulated under nitrogen (N)-depleted conditions, although the expression patterns of the individual DGATs were markedly different. Isozyme PtDGAT2B exhibits the greatest fold change (20.3fold). Upregulation of PtDGAT2B occurs rapidly within the first day upon N-depletion and remains at a relatively constant level thereafter
DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
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successful introduction of the triacylglycerol biosynthesis pathway in gamma-proteobacteria, in an industrially appropriate microorganism, method development and optimization, overview. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells. Optimization of fluorescence techniques for the detection of in situ TAG accumulation, Nile Red staining
successful introduction of the triacylglycerol biosynthesis pathway in gamma-proteobacteria, in an industrially appropriate microorganism, method development and optimization, overview. tDGAT is associated with the lipids accumulated in recombinant Escherichia coli cells. Optimization of fluorescence techniques for the detection of in situ TAG accumulation, Nile Red staining
-
-
the Rv3371 promoter is minimally active during exponential growth in vitro, but is upregulated under stationary phase, hypoxia, nutrient starvation, nitrosative stress, low iron, in IFN-gamma activated macrophages and infected mice. The low iron-induced expression of Rv3371 is likely due to the de-repression by Rv1404, which is probably activated by ideR
the Rv3371 promoter is minimally active during exponential growth in vitro, but is upregulated under stationary phase, hypoxia, nutrient starvation, nitrosative stress, low iron, in IFN-gamma activated macrophages and infected mice. The low iron-induced expression of Rv3371 is likely due to the de-repression by Rv1404, which is probably activated by ideR
-
-
the Rv3371 promoter is minimally active during exponential growth in vitro, but is upregulated under stationary phase, hypoxia, nutrient starvation, nitrosative stress, low iron, in IFN-gamma activated macrophages and infected mice. The low iron-induced expression of Rv3371 is likely due to the de-repression by Rv1404, which is probably activated by ideR
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
-
dehydration is an effective method of storage of samples destined for estimation of the microsomal enzyme activity
biofuel production
biotechnology
drug development
industry
PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use
medicine
agriculture
the enzyme can be used successfully in metabolic engineering of plants designed to obtain a boosted TAG level, enriched not only in omega-3 long-chain polyunsaturated fatty acids but also in medium-chain and omega-7 fatty acids
agriculture
high lipid content fruits can be created by the overexpression of IpDGAT2 in Idesia polycarpa
agriculture
-
PrDGAT3 may have practical applications in improving plant lipid nutrition and increasing oil production in plants
agriculture
GmDGAT3-2 can be an excellent molecular target for genetic improvement of soybean or other oilseeds to increase oil yield and quality
biofuel production
combining the overexpression of TAG biosynthetic genes, DGAT1 and GPD1, appears to be a positive strategy to achieve a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increase the oil yield of Camelina sativa, application of genetic engineering approaches to boost the metabolic flux of carbon into seed oils
biofuel production
DGAT1 is a target for genetic manipulation to increase seed oil production in oleaginous plants. Triacylglycerol produced by the enzyme can be a petrochemical alternative
biofuel production
Vernonia diacylglycerol acyltransferase can increase renewable oil production
biofuel production
PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use
biotechnology
overexpression of mutated DGAT1 in Arabidopsis can be used to enhance oil content
biotechnology
WS/DGAT might have possible additional specificities, making it highly attractive for biotechnological applications such as biodiesel production
biotechnology
combining the overexpression of TAG biosynthetic genes, DGAT1 and GPD1, appears to be a positive strategy to achieve a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increase the oil yield of Camelina sativa, application of genetic engineering approaches to boost the metabolic flux of carbon into seed oils
biotechnology
evaluation of the possibility of using the enzyme in biotechnological approaches where a reduction of polyunsaturated fatty acids in the oil is desired
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzyme can be used successfully in metabolic engineering of plants designed to obtain a boosted TAG level, enriched not only in omega-3 long-chain polyunsaturated fatty acids but also in medium-chain and omega-7 fatty acids
biotechnology
heterologous expression of HpDGAT2D in wild-type Arabidopsis thaliana and Chlamydomonas reinhardtii significantly increases the triacylglycerol content and shows a strong preference for monounsaturated fatty acyl-CoAs and polyunsaturated fatty acyl-CoAs, indicating the engineering potential to increase specific triacylglycerol production in plants and algae
biotechnology
-
WS/DGAT might have possible additional specificities, making it highly attractive for biotechnological applications such as biodiesel production
-
drug development
-
the enzyme is a possible target for antilatency drugs
drug development
-
the enzyme is a target for development of inhibitors of lipid deposition
medicine
-
use of enzyme as target for antilacency drugs that prevent cells from surviving dormancy
medicine
-
increase in triglyceride accumulation in diet-induced hyperlipidemic, insulin-resistant animals corresponds with increase in microsomal enzyme activity. Isoform DGAT1 activity changes most in liver and adipose tissue, DGAT2 responses mainly in muscle and intestine
medicine
diacylglycerol acyltransferase (DGAT), the only limited enzyme in the synthesis of triacylglycerol (TAG), is regarded as an important therapeutic target for human obesity and other metabolic syndromes
EXTERNAL LINKS (specific for EC-Number 2.3.1.20)
Transporter Classification Database (TCDB): 2.A.50.4.1, 2.A.50.4.10
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Release 2026.1 (March 2026)
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