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Information on EC 2.7.1.174 - diacylglycerol kinase (CTP) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12382

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IUBMB Comments
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.
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Saccharomyces cerevisiae
UNIPROT: Q12382
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
dgk1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CTP-dependent DAG kinase
-
CTP-dependent diacylglycerol kinase
-
CTP-dependent diacylglycerol kinase
-
-
-
-
DAG kinase
-
-
-
-
diacylglycerol kinase (CTP dependent)
-
-
-
-
additional information
formerly HSD1 protein
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
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
the CTP transferase domain is sufficient for diacylglycerol kinase activity
-
-
?
dCTP + 1,2-diacyl-sn-glycerol
dCDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
both a substrate and competitive inhibitor
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP-diacylglycerol
-
dCTP
both a substrate and competitive inhibitor
diacylglycerol diphosphate
-
lyso-phosphatidate
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidylcholine
-
phosphatidylethanolamine
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phosphatidylglycerol
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phosphatidylinositol
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phosphatidylserine
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
N-ethylmaleimide
Saccharomyces cerevisiae
pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.018
wild-type cells, pH 7.5, 30°C
130
DAG kinase in the membrane fraction of galactose-grown cells, pH 7.5, 30°C
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * about 30000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the enzyme is phosphorylated by casein kinase II at serine residues Ser45 and Ser46. The casein kinase II-mediated phosphorylation of the enzyme regulates its function in the production of phosphatidic acid. The enzyme is inhibited by dephosphorylation with alkaline phosphatase
PROTEIN VARIANTS
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
S44A
the mutation does not affect phosphorylation of the enzyme
S44A/S45A/S46A
the mutations abolish the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutations decrease enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
S46A
the mutation abolishes the stationary phase-dependent stimulation of enzyme activity. The phosphorylation-deficient mutation decreases enzyme function in phosphatidic acid production and in eliciting pah1DELTA phenotypes, such as the expansion of the nuclear/endoplasmic reticulum membrane, reduced lipid droplet formation, and temperature sensitivity
S5A
the mutation does decreases phosphorylation of the enzyme by about 40% compared to the wild type enzyme
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
-80°C, 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
expressed in Escherichia coli BL21(DE3) cells
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of diacylglycerol kinase is induced by the Reb1p transcription factor, Reb1p directly interacts with the Reb1p-binding sequence in the DGK1 promoter
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, G.S.; OHara, L.; Siniossoglou, S.; Carman, G.M.
Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase
J. Biol. Chem.
283
20443-20453
2008
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (Q12382)
Manually annotated by BRENDA team
Han, G.S.; OHara, L.; Carman, G.M.; Siniossoglou, S.
An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth
J. Biol. Chem.
283
20433-20442
2008
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (Q12382)
Manually annotated by BRENDA team
Qiu, Y.; Fakas, S.; Han, G.S.; Barbosa, A.D.; Siniossoglou, S.; Carman, G.M.
Transcription factor Reb1p regulates DGK1-encoded diacylglycerol kinase and lipid metabolism in Saccharomyces cerevisiae
J. Biol. Chem.
288
29124-29133
2013
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Qiu, Y.; Hassaninasab, A.; Han, G.S.; Carman, G.M.
Phosphorylation of Dgk1 diacylglycerol kinase by casein kinase II regulates phosphatidic acid production in Saccharomyces cerevisiae
J. Biol. Chem.
291
26455-26467
2016
Saccharomyces cerevisiae (Q12382), Saccharomyces cerevisiae BY4741 (Q12382)
Manually annotated by BRENDA team