EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.174 | dolichol | - |
Saccharomyces cerevisiae | |
2.7.1.174 | additional information | diacylglycerol kinase activity is stimulated by major membrane phospholipids, overview | Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidate | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidylcholine | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidylethanolamine | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidylglycerol | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidylinositol | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phosphatidylserine | - |
Saccharomyces cerevisiae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.1.174 | 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 | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.1.174 | D177A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
2.7.1.174 | G184A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
2.7.1.174 | K77A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
2.7.1.174 | additional information | construction of DGK1 truncation mutants. The DELTA66 and DELTA70 truncations remove most of the N-terminal hydrophilic region of Dgk1p, whereas the DELTA77 truncation removes the entire N-terminal hydrophilic region plus the first two residues contained within the CTP transferase domain, the later mutant is inactive, the other two show reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
2.7.1.174 | R76A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.174 | cardiolipin | - |
Saccharomyces cerevisiae | |
2.7.1.174 | CDP-diacylglycerol | - |
Saccharomyces cerevisiae | |
2.7.1.174 | ceramide | - |
Saccharomyces cerevisiae | |
2.7.1.174 | dCTP | both a substrate and competitive inhibitor | Saccharomyces cerevisiae | |
2.7.1.174 | diacylglycerol diphosphate | - |
Saccharomyces cerevisiae | |
2.7.1.174 | lyso-phosphatidate | - |
Saccharomyces cerevisiae | |
2.7.1.174 | Mn2+ | abolishes detectable DAG kinase activity | Saccharomyces cerevisiae | |
2.7.1.174 | additional information | the enzyme is inhibited by sphingoid bases | Saccharomyces cerevisiae | |
2.7.1.174 | N-ethylmaleimide | - |
Saccharomyces cerevisiae | |
2.7.1.174 | phytosphingosine | - |
Saccharomyces cerevisiae | |
2.7.1.174 | R59022 | 25% inhibition at 0.05 M | Saccharomyces cerevisiae | |
2.7.1.174 | R59949 | 15% inhibition at 0.05 M | Saccharomyces cerevisiae | |
2.7.1.174 | sphinganine | - |
Saccharomyces cerevisiae | |
2.7.1.174 | sphingosine | - |
Saccharomyces cerevisiae | |
2.7.1.174 | triacylglycerol | - |
Saccharomyces cerevisiae | |
2.7.1.174 | Triton X-100 | inhibition kinetics, overview. No inhibition by monoacylglycerol | Saccharomyces cerevisiae | |
2.7.1.174 | Zn2+ | abolishes detectable DAG kinase activity | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.174 | additional information | - |
additional information | the enzyme exhibits positive cooperative kinetics with respect to diacylglycerol and saturation kinetics with respect to CTP, kinetic analysis and modeling, overview | Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.7.1.174 | membrane | - |
Saccharomyces cerevisiae | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.174 | Ca2+ | 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 | Saccharomyces cerevisiae | |
2.7.1.174 | 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 | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.174 | CTP + 1,2-diacyl-sn-glycerol | Saccharomyces cerevisiae | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity | CDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | CTP + 1,2-diacyl-sn-glycerol | Saccharomyces cerevisiae BY4742 | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity | CDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.108 | Saccharomyces cerevisiae | - |
CTP transferase domain that is also present in CDS1-encoded CDP-diacylglycerolsynthase | - |
2.7.1.174 | Saccharomyces cerevisiae | Q12382 | gene DGK1 or YOR311C | - |
2.7.1.174 | Saccharomyces cerevisiae BY4742 | Q12382 | gene DGK1 or YOR311C | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.1.174 | 0.018 | - |
wild-type cells, pH 7.5, 30°C | Saccharomyces cerevisiae |
2.7.1.174 | 130 | - |
DAG kinase in the membrane fraction of galactose-grown cells, pH 7.5, 30°C | Saccharomyces cerevisiae |
EC Number | Storage Stability | Organism |
---|---|---|
2.7.1.174 | -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 | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.174 | CTP + 1,2-diacyl-sn-glycerol | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity | Saccharomyces cerevisiae | CDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | CTP + 1,2-diacyl-sn-glycerol | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity | Saccharomyces cerevisiae BY4742 | CDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | CTP + 1,2-dioleoyl-sn-glycerol | the CTP transferase domain is sufficient for diacylglycerol kinase activity | Saccharomyces cerevisiae | CDP + 1,2-dioleoyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | CTP + 1,2-dioleoyl-sn-glycerol | the CTP transferase domain is sufficient for diacylglycerol kinase activity | Saccharomyces cerevisiae BY4742 | CDP + 1,2-dioleoyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | dCTP + 1,2-diacyl-sn-glycerol | both a substrate and competitive inhibitor | Saccharomyces cerevisiae | dCDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
2.7.1.174 | dCTP + 1,2-diacyl-sn-glycerol | both a substrate and competitive inhibitor | Saccharomyces cerevisiae BY4742 | dCDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.1.174 | More | Dgk1p contains a CTP transferase domain, the CTP transferase domain is sufficient for diacylglycerol kinase activity | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.1.108 | Sec59p | - |
Saccharomyces cerevisiae |
2.7.1.174 | CTP-dependent diacylglycerol kinase | - |
Saccharomyces cerevisiae |
2.7.1.174 | DGK1 | - |
Saccharomyces cerevisiae |
2.7.1.174 | Dgk1p | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.174 | 30 | - |
assay at | Saccharomyces cerevisiae |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.174 | 40 | - |
stable up to, labile above | Saccharomyces cerevisiae |
2.7.1.174 | 70 | - |
loss of about 70% of the activity | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.174 | 7 | 7.5 | - |
Saccharomyces cerevisiae |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.174 | 6.5 | 9 | activity range, profile overview | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.108 | CTP | - |
Saccharomyces cerevisiae | |
2.7.1.174 | CTP | dependent on | Saccharomyces cerevisiae |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.174 | additional information | - |
additional information | surface dilution kinetic model, overview, positive cooperative kinetics with respect to the surface concentration of 1,2-dioleoyl-sn-glycerol | Saccharomyces cerevisiae |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.7.1.174 | 0.1 | - |
pH 7.5, 30°C | Saccharomyces cerevisiae | N-ethylmaleimide |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.1.174 | additional information | Dgk1p contains a CTP transferase domain that is present in the SEC59-encoded dolichol kinase and CDS1-encoded CDP-diacylglycerol synthase enzymes | Saccharomyces cerevisiae |
2.7.1.174 | physiological function | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity. DGK1 counteracts the PAH1-encoded PA phosphatase | Saccharomyces cerevisiae |