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Information on EC 2.3.1.22 - 2-acylglycerol O-acyltransferase
for references in articles please use BRENDA:EC2.3.1.22
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.22 2-acylglycerol O-acyltransferase
IUBMB Comments
Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.3.1.22
- n-glycans
-
mgats
- diacylglycerols
- triacylglycerol
-
n-acetylglucosaminyltransferase
-
bisect
- glcnac
- gnt-iii
-
nipecotic
-
glycome
-
tiagabine
-
acyl-coa:diacylglycerol
- medicine
- st6gal1
- drug development
- pharmacology
- analysis
showSynonyms
mgat1, mgat2, mgat3, mogat1, lpgat1, mogat2, mogat3, acyl-coa:monoacylglycerol acyltransferase, monoacylglycerol o-acyltransferase, monoacylglycerol o-acyltransferase 1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl coenzyme A-monoglyceride acyltransferase
-
-
-
-
acyl coenzyme A:diacylglycerol acyltransferase
acyl-CoA:monoacylglycerol transferase
-
-
-
-
acylglycerol palmitoyltransferase
-
-
-
-
DGAT
MGAT
MGAT1
Mgat2
MGAT3
MGOT1
MGOT2
MGOT3
MOGAT1
MOGAT2
MOGAT3
monoacylglycerol acyltransferase
monoglyceride acyltransferase
-
-
-
-
palmitoyltransferase, acylglycerol
-
-
-
-
wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
WS/DGAT
additional information
MGAT
-
-
-
-
MGAT
enzyme shows bifunctional activities: monoacylglycerol and lysophosphatidylcholine hydrolytic activities
MGAT3
-
small intestine, only in higher mammals and humans, not in rodents, more homology with DGAT2 than with other MGAT isoforms
monoacylglycerol acyltransferase
-
-
-
-
additional information
-
the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase, MGAT, gene family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + 2-acylglycerol = CoA + diacylglycerol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:2-acylglycerol O-acyltransferase
Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
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CAS REGISTRY NUMBER
COMMENTARY
9055-17-8
-
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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
2-acyl-sn-glycerol + acetyl-CoA
diacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
2-acyl-sn-glycerol + palmitoyl-CoA
diacylglycerol + CoA
-
Substrates: in vitro assay in lysate of transfected CHO cells or of microsome preparation of mouse liver, 2-monoacylglycerol is preferred over 1-monoacylglycerol, 25°C, pH 6.4
Products: -
Products: -
?
acetyl-CoA + 2-oleoyl-(Z)-1-(octadec-9-enyl)glycerol
CoA + 2,3-dioleoyl-(Z)-1-(octadec-9-enyl)glycerol
Substrates: -
Products: -
Products: -
?
acetyl-CoA + 3-oleoyl-(Z)-1-(octadec-9-enyl)glycerol
CoA + 2,3-dioleoyl-(Z)-1-(octadec-9-enyl)glycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-oleoylglycerol
CoA + 1-acyl-2-oleoylglycerol
Substrates: deuterated substrate 2-oleoylglycerol-d5
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + sn-1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + sn-2-monolinolenoylglycerol
CoA + 1-acyl-2-linolenoylglycerol
-
Substrates: in preference to sn-2-monooleoylglycerol
Products: -
Products: -
?
acyl-CoA + sn-2-monolinoleoylglycerol
CoA + 1-acyl-2-linoleoylglycerol
-
Substrates: in preference to sn-2-monooleoylglycerol
Products: -
Products: -
?
arachidonoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-arachidonoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
arachidoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-arachidoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + 2-oleoylglycerol
?
Substrates: -
Products: -
Products: -
?
lauroyl-CoA + sn-2-monooleoylglycerol
CoA + 1-lauroyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
N-(7-nitro-2-1,3-benzoxadiazol-4-yl)amino-palmitoyl-CoA + 2-oleoylglycerol
CoA + N-(7-nitro-2-1,3-benzoxadiazol-4-yl)amino-palmitoyl-diacylglycerol
Substrates: fluorescent-labeled substrate
Products: -
Products: -
?
n-octanoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-octanoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + (Z)-1-(octadec-9-enyl)glycerol
CoA + 2-oleoyl-(Z)-1-(octadec-9-enyl)glycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + (Z)-1-(octadec-9-enyl)glycerol
CoA + 3-oleoyl-(Z)-1-(octadec-9-enyl)glycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1-monooleoylglycerol
CoA + dioleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-1-monooleoylglycerol
CoA + sn-1,3-dioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-3-monostearoylglycerol
CoA + 1-oleoyl-3-stearoylglycerol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 1-palmitoyl-sn-glycerol
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-hexadecylglycerol
CoA + 2-hexadecyl-1-palmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + rac-1-monooleoylglycerol
CoA + ?
-
Substrates: intestine, at 78% the rate of sn-2-monooleoylglycerol acylation
Products: -
Products: -
?
palmitoyl-CoA + rac-1-monooleoylglycerol ether
CoA + ?
-
Substrates: intestine, at 45% the rate of sn-2-monooleoylglycerol acylation
Products: -
Products: -
?
palmitoyl-CoA + rac-1-monopalmitoylglycerol
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-1,2-dioleoylglycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-1-monooleylglycerol ether
CoA + ?
-
Substrates: at 5.7% of the activity with sn-2-monooleoylglycerol
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleylglycerol
CoA + 2-oleyl-1-palmitoylglycerol
-
Substrates: at 5.7% of the activity with sn-2-monooleoylglycerol
Products: -
Products: -
?
rac-1-linolenoylglycerol + oleoyl-CoA
1-linolenoyl-3-oleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
rac-1-linoleoylglycerol + oleoyl-CoA
1-linoleoyl-3-oleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
rac-1-monoacylglycerol + palmitoyl-CoA
diacylglycerol + CoA
-
Substrates: in vitro assay in lysate of transfected CHO cells, 25°C, pH 6.4
Products: -
Products: -
?
rac-1-oleoylglycerol + oleoyl-CoA
1,3-dioleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
sn-2-oleoylglycerol + oleoyl-CoA
2,3-dioleoylglycerol + CoA
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 1-palmitoyl-sn-glycerol
CoA + ?
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-stearoyl-2-oleolyglycerol
Substrates: -
Products: -
Products: -
?
[N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)-methyl]amino]palmitoyl-CoA + 2-oleoylglycerol
CoA + 1-[N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)-methyl]amino]palmitoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
-
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: diacylglycerol biosynthetic activity
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: representative enzyme of the neutral lipid pathway
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme plays a major role in the absorption of dietary fat by catalyzing the resynthesis of triacylglycerol in enterocytes
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme plays a predominant role in dietary fat absorption in the small intestine, where it catalyzes the first step of triacylglycerol resynthesis in enterocytes for chylomicron formation and secretion
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
Substrates: in the intestine the enzyme plays a major role in the absorption of dietary fat because resynthesis of triacylglycerol is required for the assembly of lipoproteins that transport absorbed fat to other tissues
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: MGAT2 may play an important role in dietary fat absorption
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: involved in synthesis of triacylglycerols
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme is developmentally expressed, associated with physiological periods characterized by high rates of lipolysis and depends on fatty acids for energy production. During these periods the enzyme may help to retain essential fatty acids selectively
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme may be regulated physiologically by specific intermediates of glycerolipid metabolism. In neonatal liver, signal transduction may be linked to the synthesis of complex lipids via the monoacylglycerol pathway
Products: -
Products: -
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the specificity of the enzyme for sn-2-monoacylglycerol and the probable enhanced affinity for sn-2-monoacylglycerols of specific acyl chains may allow selected omega6 and omega3 fatty acids to be retained within the adipocyte, while nonessential fatty acids are released for beta-oxidation in flight muscles
Products: -
Products: -
?
fatty acyl-CoA + sn-2-monoacylglycerol
CoA + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
fatty acyl-CoA + sn-2-monoacylglycerol
CoA + 1,2-diacylglycerol
Substrates: 2-monoacylglycerol is preferred substrate
Products: -
Products: -
?
fatty acyl-CoA + sn-2-monoacylglycerol
CoA + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
fatty acyl-CoA + sn-2-monoacylglycerol
CoA + 1,2-diacylglycerol
-
Substrates: -
Products: 88% 1,2-diacylglycerol and 12% 1,3-diacylglycerol
Products: 88% 1,2-diacylglycerol and 12% 1,3-diacylglycerol
?
linoleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-linoleoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
linoleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-linoleoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
monoacylglycerol + acyl-CoA
diacylglycerol + CoA
-
Substrates: radioactive monoacylglycerol administration to the lumen of the small intestine
Products: -
Products: -
?
monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
Substrates: -
Products: -
Products: -
?
monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: monoacylglycerol pathway predominates in enterocytes after feeding, when large amounts of 2-monoacylglycerols and fatty acids are released from the digestion of dietary lipids
Products: -
Products: -
?
monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: monoacylglycerol pathway predominates in enterocytes after feeding, when large amounts of 2-monoacylglycerols and fatty acids are released from the digestion of dietary lipids, also active in adipose tissue
Products: -
Products: -
?
monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-sn-glycerol
Substrates: preferred substrate
Products: -
Products: -
?
oleoyl-CoA + 1-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1-palmitoyl-sn-glycerol
CoA + 1-palmitoyl-3-oleoyl-sn-glycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 1-palmitoyl-sn-glycerol
CoA + 1-palmitoyl-3-oleoyl-sn-glycerol
-
Substrates: -
Products: 1-palmitoyl-3-oleoyl-sn-glycerol is the predominant reaction product
Products: 1-palmitoyl-3-oleoyl-sn-glycerol is the predominant reaction product
?
oleoyl-CoA + 2-oleoylglycerol
CoA + 1,2-dioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 2-oleoylglycerol
CoA + 1,2-dioleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + 2-oleoylglycerol
CoA + 1,2-dioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
Substrates: -
Products: preferentially esterified at sn-1-position, 10% esterification at sn-3-position
Products: preferentially esterified at sn-1-position, 10% esterification at sn-3-position
?
palmitoyl-CoA + 1,2-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 1,2-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 1,3-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 1,3-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 2,3-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 2,3-dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
Substrates: i.e. 1,2-dipalmitin
Products: -
Products: -
?
palmitoyl-CoA + 2-palmitoyl-sn-glycerol
CoA + 1,2-dipalmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2-palmitoyl-sn-glycerol
CoA + 1,2-dipalmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-1-monooleoylglycerol
CoA + ?
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-1-monooleoylglycerol
CoA + ?
-
Substrates: at 7.5% of the activity with sn-2-monooleoylglycerol
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: intestine, at 52% the rate of sn-2-monooleoylglycerol acylation
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: liver enzyme highly specific for sn-2-monooleoylglycerol
Products: -
Products: -
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme catalyzes the reaction of EC 2.3.1.22, acyl coenzyme A:diacylglycerol acyltransferase, and of EC 2.3.1.75, wax ester synthase, overview, linear acyl acceptor specificity, C14-C18 acceptor substrates in the wax ester synthase reaction are preferred, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme catalyzes the reaction of EC 2.3.1.22, acyl coenzyme A:diacylglycerol acyltransferase, and of EC 2.3.1.75, wax ester synthase, overview, linear acyl acceptor specificity, C14-C18 acceptor substrates in the wax ester synthase reaction are preferred, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: OLE3 acylates monoacylglycerol
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad acyl-donor pattern with maximal activities for C10:0 to C16:0, the highest activity with C16:0. Preferential esterification for 2-monoacylglycerols as compared with the 1-isomers
Products: -
Products: -
?
additional information
?
-
-
Substrates: the multifunctional enzyme plays an important role in lipid metabolism in human skin
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme DGAT1 also performs the reaction of the retinol O-fatty-acyltransferase, EC 2.3.1.76
Products: -
Products: -
?
additional information
?
-
-
Substrates: the multifunctional O-acetyltransferase is catalyzing the reactions of the monoacylglycerol transferase, 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the acylation of rac-1-monoacylglycerol, sn-2-monoacylglycerol, and sn-3-monoacylglycerols, the enzyme prefers monoacylglycerols containing unsaturated fatty acyls
Products: -
Products: -
?
additional information
?
-
-
Substrates: predominant role of enzyme in dietary fat absorption
Products: -
Products: -
?
additional information
?
-
-
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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no significant production of phosphatidic acid (substrate lysophosphatidic acid), triacylglycerol (diacylglycerol), or cholesterol ester (substrate cholesterol), 25°C, pH 6.4
Products: -
Products: -
?
additional information
?
-
-
Substrates: sn-2-monoacylglycerol is preferred over sn-1(3)-monoacylglycerol
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-acyl-sn-glycerol + acetyl-CoA
diacylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + sn-1,2-dioleoylglycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
Substrates: -
Products: -
Products: -
?
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
Products: -
Products: -
?
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
Substrates: -
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acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
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acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
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acyl-CoA + 2-acylglycerol
CoA + diacylglycerol
Substrates: -
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: diacylglycerol biosynthetic activity
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: representative enzyme of the neutral lipid pathway
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme plays a major role in the absorption of dietary fat by catalyzing the resynthesis of triacylglycerol in enterocytes
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: -
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme plays a predominant role in dietary fat absorption in the small intestine, where it catalyzes the first step of triacylglycerol resynthesis in enterocytes for chylomicron formation and secretion
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
Substrates: in the intestine the enzyme plays a major role in the absorption of dietary fat because resynthesis of triacylglycerol is required for the assembly of lipoproteins that transport absorbed fat to other tissues
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: MGAT2 may play an important role in dietary fat absorption
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: involved in synthesis of triacylglycerols
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme is developmentally expressed, associated with physiological periods characterized by high rates of lipolysis and depends on fatty acids for energy production. During these periods the enzyme may help to retain essential fatty acids selectively
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the enzyme may be regulated physiologically by specific intermediates of glycerolipid metabolism. In neonatal liver, signal transduction may be linked to the synthesis of complex lipids via the monoacylglycerol pathway
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acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
Substrates: the specificity of the enzyme for sn-2-monoacylglycerol and the probable enhanced affinity for sn-2-monoacylglycerols of specific acyl chains may allow selected omega6 and omega3 fatty acids to be retained within the adipocyte, while nonessential fatty acids are released for beta-oxidation in flight muscles
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monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
Substrates: -
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monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: monoacylglycerol pathway predominates in enterocytes after feeding, when large amounts of 2-monoacylglycerols and fatty acids are released from the digestion of dietary lipids
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monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: monoacylglycerol pathway predominates in enterocytes after feeding, when large amounts of 2-monoacylglycerols and fatty acids are released from the digestion of dietary lipids, also active in adipose tissue
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monoacylglycerol + fatty acyl-CoA
diacylglycerol + CoA
-
Substrates: -
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additional information
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-
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Substrates: the multifunctional enzyme plays an important role in lipid metabolism in human skin
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additional information
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Substrates: predominant role of enzyme in dietary fat absorption
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
(1S)-4'-(2-cyclopropyl-3H-pyrrol-4-yl)-5'-(5-oxo-4,5-dihydro-1,2,4-oxadiazol-3-yl)-5-(4,4,4-trifluorobutoxy)-2,3-dihydro-1'H-spiro[indene-1,2'-pyridin]-6'(3'H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
(6S)-4-(4-methylphenyl)-2-oxo-N-[4-(1H-tetrazol-5-yl)phenyl]-6-[4-(4,4,4-trifluorobutoxy)phenyl]-6-(trifluoromethyl)-1,2,5,6-tetrahydropyridine-3-carboxamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
(6S)-4-(5-cyclopropyl-1,3-thiazol-2-yl)-6-[2-fluoro-4-(4,4,4-trifluorobutoxy)phenyl]-3-(5-oxo-4,5-dihydro-1H-tetrazol-1-yl)-6-(trifluoromethyl)-5,6-dihydropyridin-2(1H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
(6S)-4-(5-cyclopropylthiophen-2-yl)-3-(2,5-dihydro-1H-tetrazol-5-yl)-6-[2-fluoro-4-(4,4,4-trifluorobutoxy)phenyl]-6-(trifluoromethyl)-5,6-dihydropyridin-2(1H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
(6S)-4-[4-(difluoromethyl)phenyl]-6-[2-fluoro-4-[(6,6,6-trifluorohexyl)oxy]phenyl]-N-(methanesulfonyl)-2-oxo-6-(trifluoromethyl)-1,2,5,6-tetrahydropyridine-3-carboxamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
1-[5-[(4-methoxyanilino)sulfanyl]-2-methylphenyl]-3-phenoxypropan-2-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-(4-chlorophenoxy)-N-[5-[(4-methoxyphenyl)sulfamoyl]-2-methylphenyl]acetamide
potent inhibitory activity toward human intestinal MGAT and recombinant human MGAT2, with selectivity over MGAT3. IC50 value in intestinal microsomes 0.000021 mM
2-(benzylsulfanyl)-6-[6-[4-(4-fluorophenyl)piperazin-1-yl]pyrimidin-4-yl]-3-phenyl-3,4,5,6,7,8-hexahydropyrido[4,3-d]pyrimidine
blocks MGAT2-mediated activity in vitro and in vivo
2-(cyclobutylsulfanyl)-3-phenyl-6-[([5-[4-(trifluoromethyl)phenoxy]pentyl]amino)acetyl]-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-(cyclobutylsulfanyl)-6-(3-[[(2,3-dihydro-1,4-benzodioxin-2-yl)methyl]amino]propanoyl)-3-phenyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-(cyclobutylsulfanyl)-6-(3-[[(2,3-dihydro-1H-inden-2-yl)methyl]amino]propanoyl)-3-phenyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[(1R)-1-(3,5-difluorophenyl)ethyl]-N-[3-(pyrrolidine-1-carbonyl)-1,2,4-oxadiazol-5-yl]-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
3,3-dimethyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-(2,5-dihydro-1H-tetrazol-5-yl)-4-(5-ethylthiophen-2-yl)-6-[4-[(6,6,6-trifluorohexyl)oxy]-2-(trifluoromethyl)phenyl]pyridin-2(1H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
3-ethyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
3-ethyl-3-methyl-2,5-dioxo-N-[4-(trifluoromethyl)phenyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-ethyl-N,3-dimethyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-ethyl-N-(4-methoxyphenyl)-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-phenyl-2-[[(pyridin-3-yl)methyl]sulfanyl]-6-[5-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-benzimidazol-2-yl]-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-N-[4-(trifluoromethyl)phenyl]-2,3-dihydro-1H-indole-1-carboxamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
7-(4,6-di-tert-butylpyrimidin-2-yl)-3-[4-(trifluoromethoxy)phenyl]-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyrazine
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
9-chloro-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
diethyldicarbonate
-
0.04 mM, 50% inhibition, 0.05 mM palmitate partly protects, completely reversible by 50 mM hydroxylamine, enzyme from intestine is less sensitive than enzyme from liver
ethyl 3-[4-([3-[2-(cyclohexylsulfanyl)-4-oxo-3-phenyl-3,5,7,8-tetrahydropyrido[4,3-d]pyrimidine-6(4H)-carbonyl]azetidin-1-yl]methyl)phenyl]propanoate
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
Mn2+
-
85.5% inhibition at 2.5 mM, inhibition of Mg2+ and bovine serum albumin is antagonistic
N-(2,4-dichlorophenyl)-2-[[(4-methoxyphenyl)methyl]amino]-4-oxo-3-phenyl-3,5,7,8-tetrahydropyrido[4,3-d]pyrimidine-6(4H)-carboxamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-(2,4-difluorophenyl)-3,3-diethyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3,3-diethyl-N-methyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3,3-diethyl-N-methyl-2-oxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3,3-diethyl-N-methyl-5-oxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3-ethyl-N,3,4-trimethyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-3-methyl-2,5-dioxo-3-propyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
N-(2-chlorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(3-chlorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepin-7-yl)benzenesulfonamide
-
N-(4-chloro-2,6-difluorophenyl)-1-[5-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]pyrimidin-2-yl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-(4-chlorophenyl)-2,5-dioxo-1,2,4,5-tetrahydrospiro[1,4-benzodiazepine-3,1'-cyclobutane]-7-sulfonamide
-
N-(4-chlorophenyl)-2,5-dioxo-1,2,4,5-tetrahydrospiro[1,4-benzodiazepine-3,1'-cyclopentane]-7-sulfonamide
-
N-(4-chlorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(4-chlorophenyl)-3-ethyl-N,1,3-trimethyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-(4-chlorophenyl)-N,3,3-trimethyl-5-oxo-2,3,4,5-tetrahydro-1,4-benzoxazepine-7-sulfonamide
-
N-(4-chlorophenyl)-N-methyl-2,5-dioxo-1,2,4,5-tetrahydrospiro[1,4-benzodiazepine-3,1'-cyclobutane]-7-carboxamide
-
N-benzyl-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-cyclohexyl-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-[(1R)-1-(4-[[(2S)-2-(4-fluorophenyl)morpholin-4-yl]methyl]phenyl)ethyl]methanesulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-[(1S)-1-[4-[(4-tert-butylpiperidin-1-yl)methyl]phenyl]-2,2,2-trifluoroethyl]methanesulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-[(1S)-1-[4-[([[(3S)-2,3-dihydro[1,4]dioxino[2,3-b]pyridin-3-yl]methyl]amino)methyl]phenyl]2,2,2-trifluoroethyl]methanesulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-[4-(difluoromethoxy)phenyl]-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
N-[5-[(2,4-difluorophenyl)sulfamoyl]-1-(2-phenylethyl)-2,3-dihydro-1H-indol-7-yl]acetamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
N-[[(6'S)-5-(2-hydroxypropan-2-yl)-2'-oxo-6'-[4-(4,4,4-trifluorobutoxy)phenyl]-6'-(trifluoromethyl)-1',2',5',6'-tetrahydro[2,4'-bipyridin]-3'-yl]methyl]-2-(methanesulfonyl)acetamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
shRNA-adenovirus
-
short hairpin RNA adenovirus construct to knockdown mouse lysophosphatidylglycerol acyltransferase 1, injected via tail vein
-
sphingosine
-
IC50 is 9 mol%, inhibits activity in Triton X-100 mixed micelles and isolated hepatocytes
XP620
-
selective isozyme DGAT1 inhibitor, inhibits the diacylglycerol acyltransferase and the retinol acyltransferase activities at the retinol recognition site
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
compound shows strong selectivity for MGAT2 over DGAT1, DGAT2 and ACAT1
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
compound inhibits elevation of plasma triglyceride in mice challenged with an oil-supplemented liquid meal. Oil challenge stimulates the secretion of hormones peptide tyrosine-tyrosine and glucagon-like peptide-1 into the bloodstream, and these responses are augmented in mice pretreated with the inhibitor. Administration of the compound to high-fat diet-fed ob/ob mice for 5 weeks suppresses food intake and body weight gain and inhibits elevation of glycated hemoglobin
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
ex hibits more than 100fold selectivity over human MGAT3, human DGAT1, and human DGAT2
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
-
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
ex hibits more than 100fold selectivity over human MGAT3, human DGAT1, and human DGAT2
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
2,4,6-Trinitrobenzene sulfonic acid
-
3 mM, 80% inactivation of liver enzyme, 45% inactivation of intestinal enzyme, palmitate partly protects, enzyme from intestine is less sensitive than enzyme from liver
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
ex hibits more than 100fold selectivity over human MGAT3, human DGAT1, and human DGAT2
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
-
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
-
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
ex hibits more than 100fold selectivity over human MGAT3, human DGAT1, and human DGAT2
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
-
bovine serum albumin
-
47% inhibition at 1 mg/ml, inhibition of Mg2+ and bovine serum albumin is antagonistic
-
MnCl2
-
2.5 mM, 86% inhibition of the intestinal enzyme, 40% inhibition of the enzyme from suckling liver
MnCl2
-
10 mM, 18-25%; 2.5-5 mM, 40% inhibition of enzymne from neonatal liver
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
ex hibits more than 100fold selectivity over human MGAT3, human DGAT1, and human DGAT2
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
-
additional information
identification, development, and optimisation of a novel series of MGAT2 inhibitors, pIC50 values, overview
-
additional information
not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620; not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620, i.e (2R,3S,6R)-N-[2,6-di(propan-2-yl)phenyl]-3,6-dipentyl-3,6-dihydro-2H-thiopyran-2-carboxamide
-
additional information
not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620; not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620, i.e (2R,3S,6R)-N-[2,6-di(propan-2-yl)phenyl]-3,6-dipentyl-3,6-dihydro-2H-thiopyran-2-carboxamide
-
additional information
-
not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620; not inhibitory: acyl-CoA:diacylglycerol acyltransferase DGAT1 selective inhibitor XP-620, i.e (2R,3S,6R)-N-[2,6-di(propan-2-yl)phenyl]-3,6-dipentyl-3,6-dihydro-2H-thiopyran-2-carboxamide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phospholipid
-
phosphatidylcholine/phosphatidylserine at 0.025 mg/ml stimulates 80%
bovine serum albumin
-
activation, liver, below 1 mg/ml, inhibitory above, not intestine
-
sn-1,2-dioleoylglycerol
-
cooperative activator, reverses the 50% inhibition caused by 10 mol%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01481
1-oleoyl-sn-glycerol
pH and temperature not specified in the publication
0.00832
oleoyl-CoA
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics depend highly on retinol concentration, overview, recombinant enzyme
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000085 - 0.0000081
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
0.000001
(1S)-4'-(2-cyclopropyl-3H-pyrrol-4-yl)-5'-(5-oxo-4,5-dihydro-1,2,4-oxadiazol-3-yl)-5-(4,4,4-trifluorobutoxy)-2,3-dihydro-1'H-spiro[indene-1,2'-pyridin]-6'(3'H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000063 - 0.00005
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
0.000007
(6S)-4-(4-methylphenyl)-2-oxo-N-[4-(1H-tetrazol-5-yl)phenyl]-6-[4-(4,4,4-trifluorobutoxy)phenyl]-6-(trifluoromethyl)-1,2,5,6-tetrahydropyridine-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000002
(6S)-4-(5-cyclopropyl-1,3-thiazol-2-yl)-6-[2-fluoro-4-(4,4,4-trifluorobutoxy)phenyl]-3-(5-oxo-4,5-dihydro-1H-tetrazol-1-yl)-6-(trifluoromethyl)-5,6-dihydropyridin-2(1H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000002
(6S)-4-(5-cyclopropylthiophen-2-yl)-3-(2,5-dihydro-1H-tetrazol-5-yl)-6-[2-fluoro-4-(4,4,4-trifluorobutoxy)phenyl]-6-(trifluoromethyl)-5,6-dihydropyridin-2(1H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000001
(6S)-4-[4-(difluoromethyl)phenyl]-6-[2-fluoro-4-[(6,6,6-trifluorohexyl)oxy]phenyl]-N-(methanesulfonyl)-2-oxo-6-(trifluoromethyl)-1,2,5,6-tetrahydropyridine-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000038 - 0.0000067
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
0.0000014 - 0.0000016
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
0.00013
1-[5-[(4-methoxyanilino)sulfanyl]-2-methylphenyl]-3-phenoxypropan-2-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000083
2-(4-chlorophenoxy)-N-[5-[(4-methoxyphenyl)sulfamoyl]-2-methylphenyl]acetamide
Homo sapiens
pH 7.5, 23°C
0.000075
2-(benzylsulfanyl)-6-[6-[4-(4-fluorophenyl)piperazin-1-yl]pyrimidin-4-yl]-3-phenyl-3,4,5,6,7,8-hexahydropyrido[4,3-d]pyrimidine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000064
2-(cyclobutylsulfanyl)-3-phenyl-6-[([5-[4-(trifluoromethyl)phenoxy]pentyl]amino)acetyl]-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000011
2-(cyclobutylsulfanyl)-6-(3-[[(2,3-dihydro-1,4-benzodioxin-2-yl)methyl]amino]propanoyl)-3-phenyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000038
2-(cyclobutylsulfanyl)-6-(3-[[(2,3-dihydro-1H-inden-2-yl)methyl]amino]propanoyl)-3-phenyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000016
2-[(1R)-1-(3,5-difluorophenyl)ethyl]-N-[3-(pyrrolidine-1-carbonyl)-1,2,4-oxadiazol-5-yl]-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00117 - 0.001522
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
0.000004 - 0.000028
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
0.0000019 - 0.0000051
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
0.0000003
3-(2,5-dihydro-1H-tetrazol-5-yl)-4-(5-ethylthiophen-2-yl)-6-[4-[(6,6,6-trifluorohexyl)oxy]-2-(trifluoromethyl)phenyl]pyridin-2(1H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000398 - 0.002511
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
0.000056
3-phenyl-2-[[(pyridin-3-yl)methyl]sulfanyl]-6-[5-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-benzimidazol-2-yl]-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-4(3H)-one
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000034
5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-N-[4-(trifluoromethyl)phenyl]-2,3-dihydro-1H-indole-1-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000019
7-(4,6-di-tert-butylpyrimidin-2-yl)-3-[4-(trifluoromethoxy)phenyl]-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyrazine
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000009
9-chloro-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000011 - 0.0000034
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
0.000004
ethyl 3-[4-([3-[2-(cyclohexylsulfanyl)-4-oxo-3-phenyl-3,5,7,8-tetrahydropyrido[4,3-d]pyrimidine-6(4H)-carbonyl]azetidin-1-yl]methyl)phenyl]propanoate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000006 - 0.0000032
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
0.0000078
N-(4-chloro-2,6-difluorophenyl)-1-[5-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]pyrimidin-2-yl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000274
N-[(1R)-1-(4-[[(2S)-2-(4-fluorophenyl)morpholin-4-yl]methyl]phenyl)ethyl]methanesulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000058
N-[(1S)-1-[4-[(4-tert-butylpiperidin-1-yl)methyl]phenyl]-2,2,2-trifluoroethyl]methanesulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000038
N-[(1S)-1-[4-[([[(3S)-2,3-dihydro[1,4]dioxino[2,3-b]pyridin-3-yl]methyl]amino)methyl]phenyl]2,2,2-trifluoroethyl]methanesulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000001
N-[5-[(2,4-difluorophenyl)sulfamoyl]-1-(2-phenylethyl)-2,3-dihydro-1H-indol-7-yl]acetamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000073
N-[[(6'S)-5-(2-hydroxypropan-2-yl)-2'-oxo-6'-[4-(4,4,4-trifluorobutoxy)phenyl]-6'-(trifluoromethyl)-1',2',5',6'-tetrahydro[2,4'-bipyridin]-3'-yl]methyl]-2-(methanesulfonyl)acetamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00000085
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000081
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000063
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00005
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000038
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Mus musculus
pH 7.4, 23°C
0.0000067
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Homo sapiens
pH 7.4, 23°C
0.0000014
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
pH 7.4, 23°C
0.0000016
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Mus musculus
pH 7.4, 23°C
0.00117
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.001522
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000004
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.000028
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000019
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
Mus musculus
pH 7.4, 23°C
0.0000051
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
Homo sapiens
pH 7.4, 23°C
0.000398
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.002511
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000011
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
Mus musculus
pH 7.4, 23°C
0.0000034
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
Homo sapiens
pH 7.4, 23°C
0.0000006
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
Mus musculus
pH 7.4, 23°C
0.0000032
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
pH 7.4, 23°C
additional information
additional information
Homo sapiens
MGAT2 inhibitors, pIC50 values, overview
-
additional information
shRNA-adenovirus
Mus musculus
-
infection with 60000000000 particles per animal (dose limit of no effect of control particles) leads to 83% decreased mRNA levels on day 5, 92% decrease on day 16 post-injection, associated with reduces hepatic MGAT and LPGAT activities (pH 6.4, 25°C), slight body weight reduction despite normal food consumption throughout most of the experimental treatment period (only 15% reduction on day 2), reduced serum triacylglycerols and cholesterol but increased total cholesterol accumulation in the liver
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.118
-
purified recombinant enzyme, substrates palmitoyl-CoA and 1,3-dipalmitoylglycerol
0.211
-
purified recombinant enzyme, substrates palmitoyl-CoA and 1,2-dipalmitoylglycerol
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
7 weeks old male diabetic (db/db) and control (db/m) mice, 7 days adjusted
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
uptake of monoacylglycerol and fatty acids, resynthesized into triacylglycerols, packaged into chylomicrons, and secreted into circulation
brenda
expression of MOGAT2 does not correlate with enzymatic activity
brenda
expression of MOGAT3 is correlated with enzymatic activity
brenda
-
absorption of dietary fat and storage in white adipose tissue
brenda
additional information
-
not: stomach, cecum, colon, rectum, kidney, liver
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MGAT1 localizes to the endoplasmic reticulum under normal conditions, and colocalizes to lipid droplets under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion
brenda
additional information
integral membrane protein, the C-terminus is exposed to the cytosol, while the N-terminus is partially buried in the ER membrane. Domains that are important for catalysis face the cytosol. Both transmembrane domains of MGAT2 are important for its ER localization, and MGAT2 is present in mitochondrial-associated membranes
brenda
MGAT1 localizes to the endoplasmic reticulum under normal conditions, and colocalizes to lipid droplets under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion
brenda
for the enzyme activity, both the N-terminal transmembrane domain and catalytic HPHG motif are required. The transmembrane domain consists of two hydrophobic regions in the N-terminus, the consensus sequence FLXLXXXn, a putative neutral lipid-binding domain, exists in the first transmembrane domain
brenda
additional information
-
determination of subcellular distribution, overview
-
brenda
additional information
-
determination of subcellular distribution, overview
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
the enzyme belongs to the evolutionarily conserved acyltransferase gene family. All DGAT2 family members, including monoacylglycerol acyltransferases (MGAT)1-3 and wax synthases 1 and 2, contain a highly conserved four amino acid sequence - histidine-proline-histidine-glycine
evolution
three subtypes of monoacylglycerol O-acyltransferase, MGAT, enzymes, MGAT1, MGAT2, and MGAT3: in a phylogenetic tree with inferred evolutionary relationships, MGAT3 shares higher sequence homology with the diacylglycerol O-acyltransferase 2 enzyme than with MGAT1 or MGAT2, phylogenetic analysis
malfunction
-
mice with targeted inactivation of the MGAT2 gene exhibit a delay in dietary fat absorption, however, in contrast to knockout mice that absorb normal quantities of fat
malfunction
-
Mogat2 (-/-) mice lack MGAT2 protein and have a greater than 50% decrease in intestinal MGAT activity compared to wild-type mice, they display a normal weight gain and body composition on low-fat diet, with 60% calories from fat knockout mice gain 40% less weight than wild-type mice after 16 weeks, Mogat2 (+/-) mice show an intermediate phenotype, female mice with 60% fat containing diet and males with a 45% fat containing diet also show reduced weight gain, knockout mice show lower fasting insulin concentrations, better glucose tolerance, lower concentrations of total and non-high-density lipoprotein cholesterol in plasma, similar plasma triacylglycerol concentrations as wild-type mice, and less than 5% of wild-type hepatic triacylglycerol content, 7% higher oxygen consumption during active (dark) phase and a higher body temperature (while the mechanism of the increased thermogenisis remains unclear) but similar locomotive activity, similar fat absorption in knockout and wild-type mice, similar fecal fat amounts, fecal mass and energy content, 70% triacylglycerol synthesis in enterocytes compared to wild-type, residual diacylglycerol formation from monoacylglycerol or alternative pathway via breakdown of monoacylglycerol to glycerol and fatty acids and entering into the glycerol-phosphate pathway which is more energy demanding, knockout mice show a reduced rate of fat entering the circulation upon a fat boost, more fat enters the distal intestine, therefore fat entry into the circulation is delayed
malfunction
knockout of MOGAT3 attenuates MGAT activity in a liver-derived cell line
malfunction
-
overexpression of the OLE3 gene in Saccharomyces cerevisiae results in an increased accumulation of diacylglycerols and triacylglycerols and decreased phospholipids
malfunction
mice lacking the gene Mogat2 , which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. The Mogat2-deficient mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. Recombinant expression of the human gene MOGAT2, encoding the enzyme, in the intestine increases intestinal MGAT activity, restores fat absorption rate, partially corrects energy expenditure, and promotes weight gain upon high-fat feeding. The changes in respiratory exchange ratio are not reverted, and the recoveries in metabolic efficiency and weight gain are incomplete
malfunction
the enzyme is involved in hepatic steatosis, characterized by an increase in intrahepatic triacylglycerol, is an important marker of metabolic dysfunction and is associated closely with insulin resistance and dyslipidemia. Inhibition of MGAT1 ameliorates hepatic steatosis in human liver Hep-G2 cell line, inhibition of MGAT1 by siRNA treatment efficiently ameliorates the lipid accumulation
malfunction
-
mice lacking the gene Mogat2 , which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. The Mogat2-deficient mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. Recombinant expression of the human gene MOGAT2, encoding the enzyme, in the intestine increases intestinal MGAT activity, restores fat absorption rate, partially corrects energy expenditure, and promotes weight gain upon high-fat feeding. The changes in respiratory exchange ratio are not reverted, and the recoveries in metabolic efficiency and weight gain are incomplete
-
metabolism
-
diacylglyceride synthesis, involved in triglyceride and phospholipid synthesis
metabolism
diacylglyceride synthesis, involved in triglyceride and phospholipid synthesis
metabolism
-
monoacylglycerol pathway followed by diacylglycerol acyltransferase activity to produce triacylglycerol
metabolism
-
monoacylglycerol pathway is followed by diacylglycerol acyltransferase activity to produce triacylglycerol
metabolism
-
significant role in hepatic triacylglycerol synthesis and secretion in diabetic mice (db/db)
metabolism
overexpression of the MGAT gene in yeast (Saccharomyces cerevisiae) causes an increase in triacylglycerol accumulation
metabolism
the enzyme interacts with the acyl CoA:1,2-diacylglycerol acyltransferase (DGAT)-2, an endoplasmic reticulum integral membrane protein that catalyzes triacylglycerol synthesis using diacylglycerol and fatty acyl CoA as substrates. Deletion mutagenesis shows that the interaction with MGAT2 is dependent on the two transmembrane domains of DGAT2. The interaction of the enzyme and DGAT2 serves to channel lipid substrates efficiently for triacylglycerol biosynthesis
metabolism
the enzyme is involved in triglyceride synthesis by catalyzing the formation of diacylglycerol from monoacylglycerol and fatty acyl CoAs
physiological function
-
besides being the substrates for monoacylglycerol acyltransferase, monoacylglycerols, especially 2-acylglycerol, function as endogenous ligand for endocannaboid receptors, thus stimulating appetite
physiological function
-
involved in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
involved in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
-
involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols
physiological function
-
involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols, 2-acylglycerol functions as endogenous ligand for endocannaboid receptors, stimulating appetite
physiological function
-
involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols, 2-acylglycerol functions as endogenous ligand for endocannaboid receptors, stimulating apppetite
physiological function
involvid in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
-
heterologous expression of a mouse MGAT acyltransferase in Nicotiana benthamiana significantly increases TAG accumulation in vegetative tissues despite the low levels of endogenous MAG substrate available. In addition, diacylglycerol produced by this acyltransferase can serve as a substrate for both native and coexpressed diacylglycerol acyltransferases
physiological function
-
heterologous expression of Arabidopsis thaliana GPAT4 acyltransferase in Saccharomyces cerevisiae GPAT mutant can produce monoacylglycerol using oleoyl-CoA as the acyl-donor
physiological function
acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency, in other tissues it may contribute to the regulation of energy metabolism
physiological function
acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency, in other tissues it may contribute to the regulation of energy metabolism
physiological function
in the intestine, the majority of diacylglycerol is produced by the MGAT pathway via monoacylglycerol acyltransferase-2, MGAT2, which catalyzes the synthesis of diacylglycerol in an acyl CoA-dependent manner using 2-monoacylglycerol as an acyl acceptor. Co-expression of acyl CoA:1,2-diacylglycerol acyltransferase, DGAT2, and monoacylglycerol acyltransferase MGAT2 stimulates triacylglycerol storage
physiological function
monoacylglycerol O-acyltransferase 1 is regulated by peroxisome proliferator-activated receptor gamma in human hepatocytes and increases lipid accumulation
physiological function
the enzyme is involved in diabetes, obesity and other diseases which together constitute the metabolic syndrome
physiological function
hepatic expression of Mogat1 is significantly increased in the liver of fasted mice compared with mice given ad libitum access to food. Basal and fasting-induced expression of Mogat1 is markedly diminished in the liver of mice lacking the transcription factor PPARalpha. Suppressing Mogat1 expression in liver and adipose tissue with antisense oligonucleotides reduces hepatic MGAT activity and triglyceride content compared with fasted controls. The expression of many other PPARalpha target genes and PPARalpha activity is also decreased in mice given Mogat1 antisense oligonucleotides
physiological function
MGAT1 expression is reduced in physiologic contexts where lipolysis is high. Knockdown or knockout of MGAT1 in adipocytes leads to higher rates of basal adipocyte lipolysis
physiological function
MGAT1 interacts with DGAT2, which serves to synergistically increase the TAG biosynthesis and lipid droplet expansion, leading to enhancement of lipid accumulation in the liver and fat
physiological function
-
acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency, in other tissues it may contribute to the regulation of energy metabolism
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LGAT1_MOUSE
370
4
43088
Swiss-Prot
Secretory Pathway (Reliability: 3)
DGAT2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
418
1
47711
Swiss-Prot
other Location (Reliability: 2)
LGAT1_HUMAN
370
4
43089
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOG2A_XENLA
335
1
38254
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOG2B_XENLA
335
1
37886
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOGT1_BOVIN
335
1
39110
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOGT1_HUMAN
335
1
38812
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOGT1_MOUSE
335
1
38791
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOGT1_XENLA
335
1
38625
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOGT1_XENTR
335
1
38751
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOGT2_HUMAN
334
1
38196
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOGT2_MOUSE
334
1
38591
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOGT2_XENTR
335
1
37897
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOGT3_HUMAN
341
1
38730
Swiss-Prot
Secretory Pathway (Reliability: 5)
A0A2P6R1U7_ROSCH
436
0
48777
TrEMBL
other Location (Reliability: 4)
A0A2G9GCZ9_9LAMI
90
0
10045
TrEMBL
other Location (Reliability: 2)
A0A396K0S6_MEDTR
380
0
42711
TrEMBL
other Location (Reliability: 5)
A0A2P6QE93_ROSCH
383
0
43438
TrEMBL
Chloroplast (Reliability: 5)
A0A812CHA9_SEPPH
179
0
20518
TrEMBL
other Location (Reliability: 3)
A0A2G9GHA8_9LAMI
332
0
37482
TrEMBL
other Location (Reliability: 5)
A0A2G8XMZ3_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A2G9G4Z0_9LAMI
235
0
26255
TrEMBL
other Location (Reliability: 2)
A0A2G9GWP9_9LAMI
334
0
36807
TrEMBL
other Location (Reliability: 2)
A0A086KST4_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A396IZC2_MEDTR
376
1
42091
TrEMBL
Chloroplast (Reliability: 2)
A0A086LMV7_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A086PRZ0_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A086Q178_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A072VS52_MEDTR
317
0
35929
TrEMBL
other Location (Reliability: 2)
A0A396HDF8_MEDTR
309
0
34842
TrEMBL
other Location (Reliability: 2)
G7ZY18_MEDTR
346
0
39079
TrEMBL
other Location (Reliability: 3)
G7K1K2_MEDTR
395
0
44728
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6SJZ9_ROSCH
314
0
35742
TrEMBL
other Location (Reliability: 2)
A0A396HHJ9_MEDTR
68
0
7715
TrEMBL
other Location (Reliability: 2)
A0A396HHJ9_MEDTR
68
0
7715
TrEMBL
other Location (Reliability: 2)
A0A5B7A3N3_DAVIN
159
2
17522
TrEMBL
other Location (Reliability: 1)
A0A7R8D3P3_LEPSM
256
2
28933
TrEMBL
other Location (Reliability: 5)
A0A072UCF9_MEDTR
391
1
43689
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6RWG8_ROSCH
312
0
34875
TrEMBL
other Location (Reliability: 2)
A0A125YPA4_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A086JCW1_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A396JY26_MEDTR
82
0
9500
TrEMBL
Secretory Pathway (Reliability: 2)
G7IF52_MEDTR
324
0
36824
TrEMBL
Mitochondrion (Reliability: 4)
G7JTB1_MEDTR
326
0
36870
TrEMBL
other Location (Reliability: 2)
A0A2G9GQP5_9LAMI
381
0
42407
TrEMBL
Chloroplast (Reliability: 3)
I3S4R2_MEDTR
325
0
36954
TrEMBL
other Location (Reliability: 2)
A0A2P6Q3U5_ROSCH
316
0
35816
TrEMBL
other Location (Reliability: 1)
A0A0B2R2L8_GLYSO
294
1
33391
TrEMBL
Secretory Pathway (Reliability: 1)
A0A396HHI2_MEDTR
285
0
32334
TrEMBL
other Location (Reliability: 2)
A0A0F6PMY4_9LAMI
320
0
36009
TrEMBL
other Location (Reliability: 2)
A0A2T6IV43_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
G7KMS8_MEDTR
346
0
39008
TrEMBL
other Location (Reliability: 2)
A0A2P6PWW5_ROSCH
343
0
38834
TrEMBL
other Location (Reliability: 5)
A0A425HM17_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A2G9I1W0_9LAMI
209
0
23127
TrEMBL
other Location (Reliability: 2)
A0A2G9HG21_9LAMI
220
0
24815
TrEMBL
Secretory Pathway (Reliability: 5)
A0A139XJ61_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
B5X6R4_SALSA
218
1
24770
TrEMBL
Secretory Pathway (Reliability: 3)
S7UNF3_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A2G9GKK6_9LAMI
226
0
25425
TrEMBL
other Location (Reliability: 1)
A0A2G9GPN0_9LAMI
344
0
39038
TrEMBL
other Location (Reliability: 5)
A0A8M1P3L0_DANRE
368
1
42114
TrEMBL
other Location (Reliability: 2)
H9LBH7_ARAHY
321
0
36159
TrEMBL
other Location (Reliability: 2)
G7I399_MEDTR
325
0
35987
TrEMBL
other Location (Reliability: 2)
B5XA74_SALSA
169
1
19799
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6RK04_ROSCH
314
0
35790
TrEMBL
other Location (Reliability: 2)
A0A2G9GCZ4_9LAMI
321
0
36345
TrEMBL
other Location (Reliability: 3)
A0A3R7KNI8_9TRYP
288
0
32910
TrEMBL
Mitochondrion (Reliability: 4)
G7KRW6_MEDTR
341
0
39293
TrEMBL
other Location (Reliability: 4)
A0A2P6R1Q3_ROSCH
400
0
45217
TrEMBL
Chloroplast (Reliability: 4)
A0A086JYK6_TOXGO
132
0
15028
TrEMBL
other Location (Reliability: 2)
A0A2P6SJG9_ROSCH
307
0
33383
TrEMBL
Chloroplast (Reliability: 2)
A0A0B2PWP9_GLYSO
77
2
8532
TrEMBL
other Location (Reliability: 4)
A0A8M1N2V8_DANRE
252
0
28549
TrEMBL
other Location (Reliability: 2)
A0A2G9HX16_9LAMI
388
0
43634
TrEMBL
Chloroplast (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
the enzyme exists as both a homodimer and homotetramer, cross-linking
35320
-
predicted from sequence analysis, 4237 bp, 327 amino acids, gene location on chromosome 2
37710
predicted from sequence analysis, 10577 bp, 334 amino acids, gene location on chromosome 23
37800
predicted from sequence analysis, 5395 bp, 336 amino acids, gene location on chromosome 5
38000
38010
predicted from sequence analysis, 23470 bp, 330 amino acids, gene location on chromosome 10
38390
-
predicted from sequence analysis, 30645 bp, 334 amino acids, gene location on chromosome 4
39130
-
predicted from sequence analysis, 32654 bp, 335 amino acids, gene location on chromosome 7
43000
53000
80000
the enzyme exists as both a homodimer and homotetramer, cross-linking
additional information
-
molecular weight for triacylglycerol synthetase complex of EC 2.3.1.20/EC 2.3.1.22 is 350000-370000 Da, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C334A
located at the extreme C-terminus, about 200% of wild-type activity
additional information
additional information
mice lacking the gene Mogat2 , which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. The Mogat2-deficient mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. Recombinant expression of the human gene MOGAT2, encoding the enzyme, in the intestine increases intestinal MGAT activity, restores fat absorption rate, partially corrects energy expenditure, and promotes weight gain upon high-fat feeding. The changes in respiratory exchange ratio are not reverted, and the recoveries in metabolic efficiency and weight gain are incomplete
additional information
-
mice lacking the gene Mogat2 , which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. The Mogat2-deficient mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. Recombinant expression of the human gene MOGAT2, encoding the enzyme, in the intestine increases intestinal MGAT activity, restores fat absorption rate, partially corrects energy expenditure, and promotes weight gain upon high-fat feeding. The changes in respiratory exchange ratio are not reverted, and the recoveries in metabolic efficiency and weight gain are incomplete
additional information
a mutant lacking all five cysteine residues is devoid of monoacylglycerol acyltransferase activity
additional information
-
a mutant lacking all five cysteine residues is devoid of monoacylglycerol acyltransferase activity
additional information
-
MGAT2 knockout mice exhibit a reduction of metabolic efficiency and increased thermogenic energy expenditure when fed a high-fat diet, they are protected from developing obesity, fatty liver, hyperlipidemia, and glucose intolerance despite chronic high-fat feeding
additional information
-
knockdown of hepatic lysophosphatidylglycerol acyltransferase 1 gene expression in transfected CHO cells by an adenovirus construct of short hairpin RNA (shRNA)
additional information
-
Mogat2-targeted 129/SvJae embryonic stem cells are generated with a targeting vector designed to replace exon 1 of Mogat2 including the translation-initiating methionine, Mogat2 (-/-) and wild-type are generated from breeding heterozygotes (first backcrossed with C57BL/6J mice)
additional information
expression of human MGAT2 in the intestine of Mogat2-/- mice promotes the uptake and esterification of monoaclglycerol, and partially restores metabolic efficiency in diet-induced weight gain
additional information
mutant FL-DELTA1-160, with both transmembrane regions deleted, displays relocation in the cytosol. Mutant FL-DELTA161-335, which contains the N-terminus and the two transmembrane domains, exists in the membrane fraction
additional information
-
mutant FL-DELTA1-160, with both transmembrane regions deleted, displays relocation in the cytosol. Mutant FL-DELTA161-335, which contains the N-terminus and the two transmembrane domains, exists in the membrane fraction
additional information
-
expression of human MGAT2 in the intestine of Mogat2-/- mice promotes the uptake and esterification of monoaclglycerol, and partially restores metabolic efficiency in diet-induced weight gain
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51
56
-
after microsomes from adult liver are incubated for 13 min, they retain 7% of the control activity. After 13.5 min of heating, neonatal liver microsomes retain 57% of the control activity
51
-
12 min, microsomes from liver lose 23% of the initial activity, microsomes from intestinal mucosa lose 88.5% of control activity
51
-
after microsomes from adult liver are incubated for 13 min, they retain 44% of the control activity. After 13.5 min of heating, neonatal liver microsomes retain 90% of the control activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified recombinant enzyme, no significant loss after several months
-
20°C, the purified enzyme complex EC 2.3.1.20/2.3.1.22 loses 50% of its activity after 2 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
oleosin-3 exists as part of a 14 S multiprotein complex, functioning as both an MGAT and a phospholipase A2
-
recombinant soluble enzyme from Escherichia coli strain BL21(DE3) by cation exchange, hydrophobic interaction, and anion exchange chromatography, 18.7fold
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana GPAT4 acyltransferase is expressed in Saccharomyces cerevisiae GPAT mutant
-
chromosomal location, expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells and in COS-7 cells
-
gene atfA, expression of the soluble enzyme in Escherichia coli strain BL21(DE3)
-
gene MOGAT, co-expression of enzyme MGAT2 and acyl CoA:1,2-diacylglycerol acyltransferase, DGAT2, in HEK-293T and in COS-7 cells and co-localization in the endoplasmic reticulum and on lipid droplets
gene MOGAT, expression analysis, recombinant expression in enzyme-deficient mice
gene Mogat2, expression analysis, comparison of the relative expression levels of human MGAT2 in the transgenic mice to those of endogenous mouse MGAT2 in the wild-type mice
MGAT1 gene expression analysis by real-time PCR, the MGAT1 promoter is highly regulated by PPARgamma, phylogenetic analysis
PCR-amplification, transfection and expression of CHO cells with FLAG-tagged enzyme cDNA plasmid
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
basal and fasting-induced expression of Mogat1 is markedly diminished in the liver of mice lacking the transcription factor PPARalpha
diabetes, obesity, and lactation induce liver monoacylglycerol acyltransferase activity in rodents that is correlated with increased fat absorption
-
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in fat of genetically-obese mice
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in metabolically abnormal obese human subjects
hepatic expression of Mogat1 is significantly increased in the liver of fasted mice compared with mice given ad libitum access to food
hepatic LPGAT1 expression in diabetic (db/db) mice is 2fold higher than in control (db/m), consistent with 1.5fold higher hepatic monoacylglycerol acyltransferase activity
-
isozyme MGAT1 is highly induced up to 10fold by peroxisome proliferator-activated receptor gamma, PPARgamma, overexpression in human primary hepatocytes
marked weight loss following gastric bypass surgery is associated with a significant reduction in MOGAT2 and MOGAT3 expression
the infection with a short hairpin RNA-adenovirus construct lowers the lysophosphatidylglycerol acyltransferase 1 expression in diabetic (db/db) mice compared to a control virus infection in a dose-dependent manner, causing a marked reduction in serum triacylglycerol and cholesterol levels, and a significant increase in hepatic cholesterol levels
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
[acyl CoA]monoacylglycerol acyltransferase 2 (MGAT2) is of interest as a target for therapeutic treatment of diabetes, obesity and other diseases which together constitute the metabolic syndrome
medicine
pharmacology
[acyl CoA]monoacylglycerol acyltransferase 2 (MGAT2) is of interest as a target for therapeutic treatment of diabetes, obesity and other diseases which together constitute the metabolic syndrome
analysis
development of a MGAT enzymatic assay of human intestinal microsomes using a high-throughput mass spectrometry-based detection system
analysis
development of LC/ESI/MS/MS-based fat absorption assay using 1-oleoyl-glycerol-d5 and U13C-triglyceride to assess the ability of MGAT2 inhibitors to inhibit fat absorption in CD1 mice by a meal tolerance test
medicine
-
enzyme expression is not affected during diabetes, while total intestinal activity is significantly increased. Up-regulation of both enzyme expression and activity in animals fed with high fat diet
medicine
-
enzyme deficiency protects mice from metabolic disorders (obesity, glucose intolerance, hypercholesterolemia, and fatty liver) despite high-fat diet, caloric intake is normal and dietary fat is absorbed fully but entry into the circulation is reduced, enzyme may be useful target to treat obesity and other metabolic diseases associated with excessive fat intake
medicine
-
selective inhibition may provide a novel treatment for obesity and its related metabolic complications, defective triacylglycerol synthesis and storage can lead to severe insulin resistance, excess triacylglycerol accumulation leads to obesity, ectopic storage in nonadipose tissues such as liver and skeletal muscle is associated with insulin resistance
medicine
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in fat of genetically-obese mice
medicine
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in metabolically abnormal obese human subjects
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Manganaro, F.; Kuksis, A.
Rapid isolation of a triacylglycerol synthetase complex from rat intestinal mucosa
Can. J. Biochem. Cell Biol.
63
107-114
1985
Rattus norvegicus
brenda
Loirdighi, N.; Menard, D.; Delvin, E.; Levy, E.
Ontogeny and location of HMG-CoA reductase, ACAT, and MGAT in human small intestine
Am. J. Physiol.
273
G62-G67
1997
Homo sapiens
brenda
Manganaro, F.; Kuksis, A.
Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells
Can. J. Biochem. Cell Biol.
63
341-347
1985
Rattus norvegicus
brenda
Coleman, R.A.; Walsh, J.P.; Millington, D.S.; Maltby, D.A.
Stereospecificity of monoacylglycerol acyltransferase activity from rat intestine and suckling rat liver
J. Lipid Res.
27
158-165
1986
Rattus norvegicus
brenda
Bierbach, H.
Triacylglycerol biosynthesis in human small intestinal mucosa. Acyl-CoA: monoglyceride acyltransferase
Digestion
28
138-147
1983
Homo sapiens
brenda
Cao, J.; Lockwood, J.; Burn, P.; Shi, Y.
Cloning and functional characterization of a mouse intestinal acyl-CoA: monoacylglycerol acyltransferase, MGAT2
J. Biol. Chem.
278
13860-13866
2003
Mus musculus
brenda
Bhat, B.G.; Bardes, E.S.G.; Coleman, R.A.
Solubilization and partial purification of neonatally expressed rat hepatic microsomal monoacylglycerol acyltransferase
Arch. Biochem. Biophys.
300
663-669
1993
Rattus norvegicus
brenda
Waite, M.; Sisson, P.
Utilization of serum lipoprotein lipids by the monoacylglycerol acyltransferase
Biochim. Biophys. Acta
450
301-310
1976
Rattus norvegicus
brenda
Tietz, A.; Weintraub, H.; Peled, Y.
Utilization of 2-acyl-sn-glycerol by locust fat body microsomes. Specificity of the acyltransferase system
Biochim. Biophys. Acta
388
165-170
1975
Locusta migratoria
brenda
Manganaro, F.; Kuksis, A.; Myher, J.J.
Radioassay of the stereospecificity of 2-monoacylglycerol acyltransferase
Anal. Biochem.
119
4-11
1982
Rattus norvegicus
brenda
Short, V.; Brindley, D.N.; Dils, R.
A new assay procedure for monoglyceride acyltransferase
Biochem. J.
141
407-411
1974
Cavia porcellus
brenda
Coleman, R.A.; Haynes, E.B.
Monoacylglycerol acyltransferase. Evidence that the activities from rat intestine and suckling liver are tissue-specific isoenzymes
J. Biol. Chem.
261
224-228
1986
Rattus norvegicus
brenda
Lehner, R.; Kuksis, A.; Itabashi, Y.
Stereospecificity of monoacylglycerol and diacylglycerol acyltransferases from rat intestine as determined by chiral phase high-performance liquid chromatography
Lipids
28
29-34
1993
Rattus norvegicus
brenda
Yen, C.L.E.; Stone, S.J.; Cases, S.; Zhou, P.; Farese, R.V., Jr.
Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase
Proc. Natl. Acad. Sci. USA
99
8512-8517
2002
Mus musculus (Q91ZV4)
brenda
Tumaney, A.W.; Shekar, S.; Rajasekharan, R.
Identification, purification, and characterization of monoacylglycerol acyltransferase from developing peanut cotyledons
J. Biol. Chem.
276
10847-10852
2001
Arachis hypogaea
brenda
Mostafa, N.; Bhat, B.G.; Coleman, R.A.
Increased hepatic monoacylglycerol acyltransferase activity in streptozotocin-induced diabetes: characterization and comparison with activities from adult and neonatal rat liver
Biochim. Biophys. Acta
1169
189-195
1993
Rattus norvegicus
brenda
Bhat, B.G.; Wang, P.; Coleman, R.A.
Sphingosine inhibits rat hepatic monoacylglycerol acyltransferase in Triton X-100 mixed micelles and isolated hepatocytes
Biochemistry
34
11237-11244
1995
Rattus norvegicus
brenda
Mostafa, N.; Bhat, B.G.; Coleman, R.A.
Adipose monoacylglycerol:acyl-conenzyme A acyltransferase activity in the white-throated sparrow (Zonotrichia albicollis): characterization and function in an migratory bird
Lipids
29
785-791
1994
Zonotrichia albicollis
brenda
Coleman, R.A.; Wang, P.; Bhat, B.G.
Diradylglycerols alter fatty acid inhibition of monoacylglycerol acyltransferase activity in Triton X-100 mixed micelles
Biochemistry
37
5916-5922
1998
Rattus norvegicus
brenda
Yen, C.L.; Farese, R.V., Jr.
MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine
J. Biol. Chem.
5
1-24
2003
Homo sapiens, Mus musculus
-
brenda
Lockwood, J.F.; Cao, J.; Burn, P.; Shi, Y.
Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity
Am. J. Physiol.
285
E927-937
2003
Homo sapiens (Q3SYC2), Homo sapiens
brenda
Stoveken, T.; Kalscheuer, R.; Malkus, U.; Reichelt, R.; Steinbuchel, A.
The wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1: characterization of a novel type of acyltransferase
J. Bacteriol.
187
1369-1376
2005
Acinetobacter sp., Acinetobacter sp. ADP1
brenda
Cheng, D.; Nelson, T.C.; Chen, J.; Walker, S.G.; Wardwell-Swanson, J.; Meegalla, R.; Taub, R.; Billheimer, J.T.; Ramaker, M.; Feder, J.N.
Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption
J. Biol. Chem.
278
13611-13614
2003
Homo sapiens (Q86VF5), Homo sapiens
brenda
Cao, J.; Hawkins, E.; Brozinick, J.; Liu, X.; Zhang, H.; Burn, P.; Shi, Y.
A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet
J. Biol. Chem.
279
18878-18886
2004
Mus musculus
brenda
Yen, C.L.; Brown Iv, C.H.; Monetti, M.; Farese, R.V., Jr.
A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters
J. Lipid Res.
46
2388-2397
2005
Homo sapiens
brenda
Orland, M.D.; Anwar, K.; Cromley, D.; Chu, C.; Chen, L.; Billheimer, J.T.; Hussain, M.M.; Cheng, D.
Acyl coenzyme A dependent retinol esterification by acyl coenzyme A:diacylglycerol acyltransferase 1
Biochim. Biophys. Acta
1737
76-82
2005
Homo sapiens
brenda
Oxley, A.; Torstensen, B.E.; Rustan, A.C.; Olsen, R.E.
Enzyme activities of intestinal triacylglycerol and phosphatidylcholine biosynthesis in Atlantic salmon (Salmo salar L.)
Comp. Biochem. Physiol. B
141B
77-87
2005
Salmo salar
-
brenda
Yen, C.L.; Monetti, M.; Burri, B.J.; Farese, R.V.
The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters
J. Lipid Res.
46
1502-1511
2005
Mus musculus
brenda
Shi, Y.; Cheng, D.
Beyond triglyceride synthesis: The dynamic functional roles of MGAT and DGAT enzymes in energy metabolism
Am. J. Physiol. Endocrinol. Metab.
297
E10-8
2009
Mammalia, no activity in Rodentia
brenda
Holmes, R.
Comparative genomics and proteomics of vertebrate diacylglycerol acyltransferase (DGAT), acyl CoA wax alcohol acyltransferase (AWAT) and monoacylglycerol acyltransferase (MGAT)
Comp. Biochem. Physiol. D
5
45-54
2010
Danio rerio (A2BHM7), Danio rerio (B0JZB3), Danio rerio (Q5XJR1), Danio rerio, Monodelphis domestica
brenda
Hiramine, Y.; Emoto, H.; Takasuga, S.; Hiramatsu, R.
Novel acyl-coenzyme A:monoacylglycerol acyltransferase (MGAT) plays an important role in hepatic triacylglycerol secretion
J. Lipid Res.
51
1424-1431
2010
Mus musculus
brenda
Yen, C.L.; Cheong, M.L.; Grueter, C.; Zhou, P.; Moriwaki, J.; Wong, J.S.; Hubbard, B.; Marmor, S.; Farese, R.V.
Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding
Nat. Med.
15
442-446
2009
Mus musculus
brenda
Parthibane, V.; Rajakumari, S.; Venkateshwari, V.; Iyappan, R.; Rajasekharan, R.
Oleosin is bifunctional enzyme that has both monoacylglycerol acyltransferase and phospholipase activities
J. Biol. Chem.
287
1946-1954
2012
Arachis hypogaea
brenda
Hall, A.M.; Kou, K.; Chen, Z.; Pietka, T.A.; Kumar, M.; Korenblat, K.M.; Lee, K.; Ahn, K.; Fabbrini, E.; Klein, S.; Goodwin, B.; Finck, B.N.
Evidence for regulated monoacylglycerol acyltransferase expression and activity in human liver
J. Lipid Res.
53
990-999
2012
Homo sapiens (Q3SYC2), Homo sapiens (Q86VF5), Homo sapiens (Q96PD6), Homo sapiens
brenda
Yue, Y.G.; Chen, Y.Q.; Zhang, Y.; Wang, H.; Qian, Y.W.; Arnold, J.S.; Calley, J.N.; Li, S.D.; Perry, W.L.; Zhang, H.Y.; Konrad, R.J.; Cao, G.
The acyl coenzymeA:monoacylglycerol acyltransferase 3 (MGAT3) gene is a pseudogene in mice but encodes a functional enzyme in rats
Lipids
46
513-520
2011
Mus musculus, Rattus norvegicus
brenda
Vijayaraj, P.; Jashal, C.B.; Vijayakumar, A.; Rani, S.H.; Venkata Rao, D.K.; Rajasekharan, R.
A bifunctional enzyme that has both monoacylglycerol acyltransferase and acyl hydrolase activities
Plant Physiol.
160
667-683
2012
Arachis hypogaea (H9LBH7)
brenda
Petrie, J.R.; Vanhercke, T.; Shrestha, P.; El Tahchy, A.; White, A.; Zhou, X.R.; Liu, Q.; Mansour, M.P.; Nichols, P.D.; Singh, S.P.
Recruiting a new substrate for triacylglycerol synthesis in plants: the monoacylglycerol acyltransferase pathway
PLoS ONE
7
e35214
2012
Arabidopsis thaliana, Mus musculus
brenda
Yu, J.H.; Lee, Y.J.; Kim, H.J.; Choi, H.; Choi, Y.; Seok, J.W.; Kim, J.W.
Monoacylglycerol O-acyltransferase 1 is regulated by peroxisome proliferator-activated receptor gamma in human hepatocytes and increases lipid accumulation
Biochem. Biophys. Res. Commun.
460
715-720
2015
Homo sapiens (Q96PD6), Homo sapiens
brenda
Barlind, J.G.; Buckett, L.K.; Crosby, S.G.; Davidsson, O.e.; Emtenaes, H.; Ertan, A.; Jurva, U.; Lemurell, M.; Gutierrez, P.M.; Nilsson, K.; OMahony, G.; Petersson, A.U.; Redzic, A.; Wagberg, F.; Yuan, Z.Q.
Identification and design of a novel series of MGAT2 inhibitors
Bioorg. Med. Chem. Lett.
23
2721-2726
2013
Homo sapiens (Q3SYC2)
brenda
Jin, Y.; McFie, P.J.; Banman, S.L.; Brandt, C.; Stone, S.J.
Diacylglycerol acyltransferase-2 (DGAT2) and monoacylglycerol acyltransferase-2 (MGAT2) interact to promote triacylglycerol synthesis
J. Biol. Chem.
289
28237-28248
2014
Homo sapiens (Q3SYC2)
brenda
Gao, Y.; Nelson, D.W.; Banh, T.; Yen, M.I.; Yen, C.L.
Intestine-specific expression of MOGAT2 partially restores metabolic efficiency in Mogat2-deficient mice
J. Lipid Res.
54
1644-1652
2013
Homo sapiens (Q3SYC2), Homo sapiens, Mus musculus (Q80W94), Mus musculus C57/BL6J (Q80W94)
brenda
Qi, J.; Lang, W.; Connelly, M.A.; Du, F.; Liang, Y.; Caldwell, G.W.; Martin, T.; Hansen, M.K.; Kuo, G.H.; Gaul, M.D.; Pocai, A.; Lee, S.
Metabolic tracing of monoacylglycerol acyltransferase-2 activity in vitro and in vivo
Anal. Biochem.
524
68-75
2017
Homo sapiens (Q3SYC2), Homo sapiens
brenda
McFie, P.J.; Izzard, S.; Vu, H.; Jin, Y.; Beauchamp, E.; Berthiaume, L.G.; Stone, S.J.
Membrane topology of human monoacylglycerol acyltransferase-2 and identification of regions important for its localization to the endoplasmic reticulum
Biochim. Biophys. Acta
1861
1192-1204
2016
Homo sapiens (Q3SYC2), Homo sapiens
brenda
Lee, Y.J.; Kim, J.W.
Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis
BMB Rep.
50
367-372
2017
Mus musculus (Q91ZV4), Mus musculus
brenda
Adachi, R.; Ishii, T.; Ogawa, K.; Matsumoto, S.; Satou, T.; Sakamoto, J.; Sato, K.; Kawamoto, T.
Pharmacological characterization of a series of aryl-sulfonamide derivatives that potently and selectively inhibit monoacylglycerol acyltransferase 2
Eur. J. Pharmacol.
791
569-577
2016
Homo sapiens (Q3SYC2), Homo sapiens, Mus musculus (Q80W94), Mus musculus
brenda
Mochida, T.; Take, K.; Maki, T.; Nakakariya, M.; Adachi, R.; Sato, K.; Kitazaki, T.; Takekawa, S.
Inhibition of MGAT2 modulates fat-induced gut peptide release and fat intake in normal mice and ameliorates obesity and diabetes in ob/ob mice fed on a high-fat diet
FEBS Open Bio
10
316-326
2020
Homo sapiens (Q3SYC2), Mus musculus (Q80W94)
brenda
Ma, Z.; Onorato, J.M.; Chen, L.; Nelson, D.W.; Yen, C.E.; Cheng, D.
Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases
J. Lipid Res.
58
1091-1099
2017
Homo sapiens (Q3SYC2), Homo sapiens (Q86VF5), Homo sapiens
brenda
Liss, K.H.H.; Lutkewitte, A.J.; Pietka, T.; Finck, B.N.; Franczyk, M.; Yoshino, J.; Klein, S.; Hall, A.M.
Metabolic importance of adipose tissue monoacylglycerol acyltransferase 1 in mice and humans
J. Lipid Res.
59
1630-1639
2018
Homo sapiens (Q96PD6), Homo sapiens, Mus musculus (Q91ZV4)
brenda
Lutkewitte, A.J.; McCommis, K.S.; Schweitzer, G.G.; Chambers, K.T.; Graham, M.J.; Wang, L.; Patti, G.J.; Hall, A.M.; Finck, B.N.
Hepatic monoacylglycerol acyltransferase 1 is induced by prolonged food deprivation to modulate the hepatic fasting response
J. Lipid Res.
60
528-538
2019
Mus musculus (Q91ZV4)
brenda
Devasthale, P.; Cheng, D.
Monoacylglycerol acyltransferase 2 (MGAT2) inhibitors for the treatment of metabolic diseases and nonalcoholic steatohepatitis (NASH)
J. Med. Chem.
61
9879-9888
2018
Homo sapiens (Q3SYC2), Mus musculus (Q80W94)
brenda
Li, K.; Olsen, R.E.
Metabolism of sn-1(3)-monoacylglycerol and sn-2-monoacylglycerol in caecal enterocytes and hepatocytes of brown trout (Salmo trutta)
Lipids
52
61-71
2017
Salmo trutta
brenda
Adachi, R.; Ishii, T.; Matsumoto, S.; Satou, T.; Sakamoto, J.; Kawamoto, T.
Discovery of human intestinal MGAT inhibitors using high-throughput mass spectrometry
SLAS Discov.
22
360-365
2017
Homo sapiens (Q3SYC2), Homo sapiens
brenda
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