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Information on EC 2.7.1.107 - diacylglycerol kinase (ATP) and Organism(s) Sus scrofa and UniProt Accession P20192
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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).
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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: Sus scrofa
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
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-
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adenosine 5'-triphosphate:1,2-diacylglycerol 3-phosphotransferase
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-
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arachidonoyl-specific diacylglycerol kinase
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ATP:diacylglycerol phosphotransferase
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DAGK
DAGKalpha
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-
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DG kinase
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-
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DGK
DGK-alpha
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-
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DGK-theta
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-
-
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DGKbeta
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-
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DGKdelta
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-
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DGKgamma
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-
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DGKiota
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DGKksi
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diacylglycerol kinase
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-
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diacylglycerol kinase (ATP dependent)
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-
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diacylglycerol:ATP kinase
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-
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diglyceride kinase
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-
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kinase (phosphorylating), 1,2-diacylglycerol
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-
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kinase, 1,2-diacylglycerol (phosphorylating)
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-
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sn-1,2-diacylglycerol kinase
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-
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DAGK
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-
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DGK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
C-terminal active site comprises residues 371-501, the C1 domain is absolutely required for catalytic activity, residues Asp434, Asp650, Asp465, and Asp497 are involved
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -
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
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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
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
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-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
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the enzyme may regulate the intracellular concentration of diacylglycerol
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-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
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DGK-Ialpha is involved in IL-2-mediated lymphocyte proliferation
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-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
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the 80000 Da and the 150000 Da enzyme form do not possess specificity towards diacylglycerol molecular species
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
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-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
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ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
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reaction takes place during stimulated phosphatidylinositol turnover
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-
?
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
-
reaction takes place during stimulated phosphatidylinositol turnover
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme may regulate the intracellular concentration of diacylglycerol
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGK-Ialpha is involved in IL-2-mediated lymphocyte proliferation
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the 80000 Da and the 150000 Da enzyme form do not possess specificity towards diacylglycerol molecular species
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
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enzyme requires Ca2+, dissociation constant is 0.0099 mM, hydrophobic region of the enzyme is masked by addition of Ca2+
Ca2+
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2 mol of Ca2+ per mol of enzyme. Ca2+ plus phosphatidylserine markedly activates by reducing the Km value for ATP
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylinositol
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2.5 mol% results in 50% inhibition of the phosphatidylcholine-dependent kinase activity
Triton X-100
-
extremely inhibitory to the 80000 Da enzyme and the 150000 Da enzyme form
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lysophosphatidylcholine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylcholine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylethanolamine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
Phospholipid
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enhances activity. Activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
sphingomyelin
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylserine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylserine
-
10-20 mol% result in 7.5-7.8fold activation of the recombinant wild-type enzyme, 3.8fold of the recombinant mutant DELTA196, and 6.5fold of the recombinant mutant DELTA332
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
pH 6.5: about 35% of maximal activity, pH 9.0: about 65% of maximal activity, phosphatidylcholine-dependent activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
malfunction
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
physiological function
isoform DGKalpha positively regulates tumor nuclear factor-alpha-dependent necrosis factor-kappaB activation via the protein kinase Czeta-mediated Ser311 phosphorylation of p65/RelA, isoform DGKalpha does not affect phosphorylation of IkappaB, DGKalpha enhances phosphorylation of p65 at Ser311 but not at Ser468 or Ser536
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). DGKA_PIG
734
0
82606
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
the 80000 Da enzyme form is phosphorylated by an unidentified protein kinase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D497N
-
site-directed mutagenesis, 0.9% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
D529N
-
site-directed mutagenesis, 5.5% of wild-type activity, unaltered stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
D697N
-
site-directed mutagenesis, 4.0% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
additional information
-
construction of deletion mutants DELTA196, lacking the RVH motif and the EF hand, and DELTA332, lacking the RVH motif, the EF hand, and the C1 domain, mutant DELTA332 shows 50% of wild-type activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the 150000 Da enzyme is very unstable but can be stored at -80°C in presence of bovine serum albumin
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially, recombinant wild-type and point mutant enzymes from yeast by ion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA subcloned into the EcoRI site of the simian virus 40-based expression vector pSRE
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expression of wild-type and deletion mutant enzymes in COS-1 cells, expression of wild-type and point mutant enzymes in the enzyme-deficient Saccharomyces cerevisiae strain WY294
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanoh, H.; Sakane, F.; Yamada, K.
Diacylglycerol kinase isozymes from brain and lymphoid tissues
Methods Enzymol.
209
162-172
1992
Sus scrofa
Kanoh, H.; Kondoh, H.; Ono, T.
Diacylglycerol kinase from pig brain. Purification and phospholipid dependencies
J. Biol. Chem.
258
1767-1774
1983
Sus scrofa
Sakane, F.; Kanoh, H.
Molecules in focus: diacylglycerol kinase
Int. J. Biochem. Cell Biol.
29
1139-1143
1997
Homo sapiens, Mesocricetus auratus, Rattus norvegicus, Sus scrofa
Yamada, K.; Sakane, F.; Matsushima, N.; Kanoh, H.
EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes
Biochem. J.
321
59-64
1997
Homo sapiens, Rattus norvegicus, Sus scrofa, Sus scrofa DGKalpha
Abe, T.; Lu, X.; Jiang, Y.; Boccone, C.E.; Qian, S.; Vattem, K.M.; Wek, R.C.; Walsh, J.P.
Site-directed mutagenesis of the active site of diacylglycerol kinase alpha: calcium and phosphatidylserine stimulate enzyme activity via distinct mechanisms
Biochem. J.
375
673-680
2003
Sus scrofa
Cai, J.; Abramovici, H.; Gee, S.H.; Topham, M.K.
Diacylglycerol kinases as sources of phosphatidic acid
Biochim. Biophys. Acta
1791
942-948
2009
Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Sus scrofa, Mus musculus (Q80UP3)
Kai, M.; Yasuda, S.; Imai, S.; Toyota, M.; Kanoh, H.; Sakane, F.
Diacylglycerol kinase alpha enhances protein kinase Czeta-dependent phosphorylation at Ser311 of p65/RelA subunit of nuclear factor-kappaB
FEBS Lett.
583
3265-3268
2009
Sus scrofa (P20192), Homo sapiens (P23743)
Sato, Y.; Murakami, C.; Yamaki, A.; Mizuno, S.; Sakai, H.; Sakane, F.
Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes
Biochim. Biophys. Acta
1864
1170-1176
2016
Homo sapiens (O75912), Homo sapiens (P49619), Homo sapiens (P52429), Homo sapiens (P52824), Homo sapiens (Q13574), Homo sapiens (Q16760), Homo sapiens (Q5KSL6), Homo sapiens (Q86XP1), Sus scrofa (P20192), Rattus norvegicus (P68403)
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