Any feedback?
Information on EC 2.7.1.107 - diacylglycerol kinase (ATP) and Organism(s) Caenorhabditis elegans
for references in articles please use BRENDA:EC2.7.1.107Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.107 diacylglycerol kinase (ATP)IUBMB Comments
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
Specify your search results
Word Map
- 2.7.1.107
-
phosphatidic
- phospholipase
- phospholipid
- pkc
- phosphatidylinositol
-
phorbol
- isozymes
- phosphoinositide
- phosphatidylcholine
- inositol
- ceramide
- lipase
-
arachidonic
- deoxyguanosine
- deoxycytidine
-
ef-hands
- phosphatidylserine
- 13-acetate
-
polyphosphoinositide
-
phosphohydrolase
-
prelabeled
- deoxynucleoside
- staurosporine
- sphingosine
- pip2
-
pleckstrin
- 4,5-bisphosphate
-
1,4,5-trisphosphate
- 4-phosphate
- deoxyribonucleoside
- analysis
- marcks
-
kinase-dead
- medicine
- phosphatidylethanol
-
transphosphatidylation
- dioctanoylglycerol
- hypospadias
- ptdoh
- 5-kinase
- agriculture
-
3hglycerol
- monoacylglycerols
-
anergy
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dgk, diacylglycerol kinase, dag kinase, dg kinase, dgkzeta, dagk, dgkalpha, dgk-zeta, diglyceride kinase, dgkepsilon, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-diacylglycerol kinase
-
-
-
-
adenosine 5'-triphosphate:1,2-diacylglycerol 3-phosphotransferase
-
-
-
-
arachidonoyl-specific diacylglycerol kinase
-
-
-
-
ATP:diacylglycerol phosphotransferase
-
-
-
-
DAGK
-
-
-
-
DAGKalpha
-
-
-
-
DG kinase
-
-
-
-
DGK
DGK-alpha
-
-
-
-
DGK-theta
-
-
-
-
DGKbeta
-
-
-
-
DGKdelta
-
-
-
-
DGKgamma
-
-
-
-
DGKiota
-
-
-
-
DGKksi
-
-
-
-
diacylglycerol kinase
-
-
-
-
diacylglycerol kinase (ATP dependent)
-
-
-
-
diacylglycerol:ATP kinase
-
-
-
-
diglyceride kinase
-
-
-
-
kinase (phosphorylating), 1,2-diacylglycerol
-
-
-
-
kinase, 1,2-diacylglycerol (phosphorylating)
-
-
-
-
sn-1,2-diacylglycerol kinase
-
-
-
-
DGK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
CAS REGISTRY NUMBER
COMMENTARY
60382-71-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,3-dioleoyl-sn-glycerol
ADP + 1,3-dioleoyl-sn-glycerol 2-phosphate
-
low activity, about 4% of the activity with 1,2-dioleoyl-sn-glycerol
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
about 110% of the activity with 1,2-dioleoyl-sn-glycerol
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid, isozyme dgk-1 regulates diacylglycerol signalling required for acetylcholine release
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
the enzyme inhibits neurotransmission to control behaviour by terminating diacylglycerol signaling, probably independent of Galpha0 signaling
-
-
?
additional information
?
-
-
1-oleoyl-rac-glycerol is a poor substrate
-
-
?
additional information
?
-
-
DGK-3 affects the resetting of the thermal memory by altering plasticity in the temperature range of AFD synaptic output, without detectably affecting plasticity in the temperature range of AFD temperature sensitivity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid, isozyme dgk-1 regulates diacylglycerol signalling required for acetylcholine release
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
the enzyme inhibits neurotransmission to control behaviour by terminating diacylglycerol signaling, probably independent of Galpha0 signaling
-
-
?
additional information
?
-
-
DGK-3 affects the resetting of the thermal memory by altering plasticity in the temperature range of AFD synaptic output, without detectably affecting plasticity in the temperature range of AFD temperature sensitivity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00001
-
recombinant MBP-fusion enzyme in recombinant insect cell extract, substrate 1-oleoyl-rac-glycerol
0.0008
-
recombinant MBP-fusion enzyme in recombinant insect cell extract, substrate 1,3-dioleoyl-sn-glycerol
0.0019
-
recombinant MBP-fusion enzyme in recombinant insect cell extract, substrate 1,2-dioleoyl-sn-glycerol
0.0021
-
recombinant MBP-fusion enzyme in recombinant insect cell extract, substrate 1-stearoyl-2-arachidonoyl-sn-glycerol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular localization of isozymes, overview, the enzyme must undergo membrane translocation for access of diacylglycerols
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols
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). DGK3_CAEEL
795
0
89315
Swiss-Prot
other Location (Reliability: 3)
DGK5_CAEEL
937
0
105198
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A3B1E3M2_CAEEL
1150
0
127886
TrEMBL
other Location (Reliability: 3)
Q17860_CAEEL
952
0
106816
TrEMBL
other Location (Reliability: 1)
Q7Z299_CAEEL
351
0
39007
TrEMBL
other Location (Reliability: 1)
A0A3B1DVJ7_CAEEL
875
0
98305
TrEMBL
other Location (Reliability: 1)
H2KZC9_CAEEL
1339
0
148528
TrEMBL
other Location (Reliability: 1)
Q58AU6_CAEEL
794
0
88479
TrEMBL
other Location (Reliability: 1)
Q7JNZ1_CAEEL
950
0
106546
TrEMBL
other Location (Reliability: 1)
D5MCN8_CAEEL
1288
0
143107
TrEMBL
other Location (Reliability: 1)
H2KYI9_CAEEL
536
1
60422
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3B1E8R6_CAEEL
941
0
105852
TrEMBL
other Location (Reliability: 5)
Q58AU4_CAEEL
919
0
103171
TrEMBL
other Location (Reliability: 1)
A0A3B1DQ66_CAEEL
986
0
110494
TrEMBL
other Location (Reliability: 3)
Q58AU5_CAEEL
796
0
88750
TrEMBL
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure-function relationships of isozyme domain motifs, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A722V
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
C115Y
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
C184Y
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G606E
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G609E
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G796R
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
N745I
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
P736S
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
Q246stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
Q422stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
R167stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
R180stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
S880L
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W646stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W674stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W767stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
additional information
-
determination of mutational defects/molecular lesions affecting the enzyme activity and splice forms of the enzyme, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged wild-type and mutant enzymes or MBP-fusion protein from insect cells by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dgk-1alpha, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, expression of N-terminally His-tagged wild-type and mutant enzymes and of wild-type enzyme enzyme fused to the maltose binding protein in insect cells via the baculovirus infection system, enzyme is found to 95% in aggregated form
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization of the active enzyme from aggregates after recombinant expression in yeast
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luo, B.; Regier, D.S.; Prescott, S.M.; Topham, M.K.
Diacylglycerol kinases
Cell. Signal.
16
983-989
2004
Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mammalia, no activity in Saccharomyces cerevisiae
Jose, A.M.; Koelle, M.R.
Domains, amino acid residues, and new isoforms of Caenorhabditis elegans diacylglycerol kinase 1 (DGK-1) important for terminating diacylglycerol signaling in vivo
J. Biol. Chem.
280
2730-2736
2005
Caenorhabditis elegans
Biron, D.; Shibuya, M.; Gabel, C.; Wasserman, S.M.; Clark, D.A.; Brown, A.; Senqupta, P.; Samuel, A.D.
A diacylglycerol kinase modulates long-term thermotactic behavioral plasticity in Caenorhabditis elegans
Nat. Neurosci.
9
1499-1505
2006
Caenorhabditis elegans
EXTERNAL LINKS (specific for EC-Number 2.7.1.107)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
