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Literature summary for 2.7.1.174 extracted from
- Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase (2008), J. Biol. Chem., 283, 20443-20453.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dolichol | - |
Saccharomyces cerevisiae |  |
| additional information | diacylglycerol kinase activity is stimulated by major membrane phospholipids, overview | Saccharomyces cerevisiae | |
| phosphatidate | - |
Saccharomyces cerevisiae | |
| phosphatidylcholine | - |
Saccharomyces cerevisiae | |
| phosphatidylethanolamine | - |
Saccharomyces cerevisiae | |
| phosphatidylglycerol | - |
Saccharomyces cerevisiae | |
| phosphatidylinositol | - |
Saccharomyces cerevisiae | |
| phosphatidylserine | - |
Saccharomyces cerevisiae | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D177A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
| G184A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
| K77A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing an almost complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
| 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 |
| R76A | site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a complete loss of diacylglycerol kinase activity | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| cardiolipin | - |
Saccharomyces cerevisiae | |
| CDP-diacylglycerol | - |
Saccharomyces cerevisiae | |
| ceramide | - |
Saccharomyces cerevisiae | |
| dCTP | both a substrate and competitive inhibitor | Saccharomyces cerevisiae | |
| diacylglycerol diphosphate | - |
Saccharomyces cerevisiae | |
| lyso-phosphatidate | - |
Saccharomyces cerevisiae | |
| Mn2+ | abolishes detectable DAG kinase activity | Saccharomyces cerevisiae | |
| additional information | the enzyme is inhibited by sphingoid bases | Saccharomyces cerevisiae | |
| N-ethylmaleimide | - |
Saccharomyces cerevisiae | |
| phytosphingosine | - |
Saccharomyces cerevisiae | |
| R59022 | 25% inhibition at 0.05 M | Saccharomyces cerevisiae | |
| R59949 | 15% inhibition at 0.05 M | Saccharomyces cerevisiae | |
| sphinganine | - |
Saccharomyces cerevisiae | |
| sphingosine | - |
Saccharomyces cerevisiae | |
| triacylglycerol | - |
Saccharomyces cerevisiae | |
| Triton X-100 | inhibition kinetics, overview. No inhibition by monoacylglycerol | Saccharomyces cerevisiae | |
| Zn2+ | abolishes detectable DAG kinase activity | Saccharomyces cerevisiae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Saccharomyces cerevisiae | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| 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 | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | Q12382 | gene DGK1 or YOR311C | - |
| Saccharomyces cerevisiae BY4742 | Q12382 | gene DGK1 or YOR311C | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.018 | - |
wild-type cells, pH 7.5, 30°C | Saccharomyces cerevisiae |
| 130 | - |
DAG kinase in the membrane fraction of galactose-grown cells, pH 7.5, 30°C | Saccharomyces cerevisiae |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| dCTP + 1,2-diacyl-sn-glycerol | both a substrate and competitive inhibitor | Saccharomyces cerevisiae | dCDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
| dCTP + 1,2-diacyl-sn-glycerol | both a substrate and competitive inhibitor | Saccharomyces cerevisiae BY4742 | dCDP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | Dgk1p contains a CTP transferase domain, the CTP transferase domain is sufficient for diacylglycerol kinase activity | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CTP-dependent diacylglycerol kinase | - |
Saccharomyces cerevisiae |
| DGK1 | - |
Saccharomyces cerevisiae |
| Dgk1p | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
stable up to, labile above | Saccharomyces cerevisiae |
| 70 | - |
loss of about 70% of the activity | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 7.5 | - |
Saccharomyces cerevisiae |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9 | activity range, profile overview | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| CTP | dependent on | Saccharomyces cerevisiae | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.1 | - |
pH 7.5, 30°C | Saccharomyces cerevisiae | N-ethylmaleimide | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| physiological function | in vivo functions of Dgk1p are specifically due to its diacylglycerol kinase activity. DGK1 counteracts the PAH1-encoded PA phosphatase | Saccharomyces cerevisiae |
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