Information on EC 2.7.1.174 - diacylglycerol kinase (CTP)

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
2.7.1.174
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RECOMMENDED NAME
GeneOntology No.
diacylglycerol kinase (CTP)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
diacylglycerol and triacylglycerol biosynthesis
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monoacylglycerol metabolism (yeast)
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Glycerophospholipid metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
CAS REGISTRY NUMBER
COMMENTARY hide
60382-71-0
cf. EC 2.7.1.107
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations decrease phosphatidate levels decrease nuclear membrane growth in pah1DELTA cells, the inactivation of Pah1p leads to nuclear growth. A dgk1DLETA strain expressing a mutant DGK1 allele in which residue 177 is changed to alanine does not display any CTP-dependent DAG kinase activity
metabolism
phosphatidate metabolism is a critical factor determining nuclear structure by regulating nuclear membrane biogenesis, DGK1 rescues the lethality of dephosphorylated PAH1
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
CTP + 1,2-dioleoyl-sn-glycerol
CDP + 1,2-dioleoyl-sn-glycerol 3-phosphate
show the reaction diagram
dCTP + 1,2-diacyl-sn-glycerol
dCDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + 1,2-diacyl-sn-glycerol
CDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the enzyme requires Ca2+ or Mg2+ ions for activity. Maximum DAG kinase activity obtained with 1 mM Ca2+ ions is slightly greater than the maximum activity obtained with 10 mM Mg2+ ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP-diacylglycerol
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dCTP
both a substrate and competitive inhibitor
diacylglycerol diphosphate
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lyso-phosphatidate
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Mn2+
abolishes detectable DAG kinase activity
R59022
25% inhibition at 0.05 M
R59949
15% inhibition at 0.05 M
Triton X-100
inhibition kinetics, overview. No inhibition by monoacylglycerol
Zn2+
abolishes detectable DAG kinase activity
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidylcholine
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phosphatidylethanolamine
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phosphatidylglycerol
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phosphatidylinositol
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phosphatidylserine
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
N-ethylmaleimide
Saccharomyces cerevisiae
Q12382
pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.018
wild-type cells, pH 7.5, 30C
130
DAG kinase in the membrane fraction of galactose-grown cells, pH 7.5, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
stable up to, labile above
70
loss of about 70% of the activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, the enzyme preparation is completely stable for at least 3 months of storage at, and is stable to several cycles of freezing and thawing
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene DGK1, the DGK1 promoter is substituted with the inducible GAL1/10 promoter in the low copy YCplac111 and high copy YEplac181 vectors, expression of wild-type and mutant enzymes, induction of wild-type DGK1 gene expression from high copy number plasmid YEplac181-GAL1/10-DGK1 results in a massive increase in DAG kinase activity. Temperature sensitivity of dgk1DELTA cells overexpressing DGK1 and its mutant alleles
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D177A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
G184A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity
K77A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity
R76A
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
D177A
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site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
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G184A
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site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity
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K77A
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site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity
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R76A
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site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity
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additional information