Activating Compound | Comment | Organism | Structure |
---|---|---|---|
acidic phospholipids | activation in vitro | Sus scrofa | |
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 | Sus scrofa |
Cloned (Comment) | Organism |
---|---|
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 | Sus scrofa |
Protein Variants | Comment | Organism |
---|---|---|
D434A | site-directed mutagenesis, inactive mutant | Sus scrofa |
D434N | site-directed mutagenesis, inactive mutant | Sus scrofa |
D465A | site-directed mutagenesis, inactive mutant | Sus scrofa |
D465N | site-directed mutagenesis, 0.1% of wild-type activity | Sus scrofa |
D497A | site-directed mutagenesis, inactive mutant | Sus scrofa |
D497N | site-directed mutagenesis, 0.9% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme | Sus scrofa |
D529A | site-directed mutagenesis, 1.1% of wild-type activity | Sus scrofa |
D529N | site-directed mutagenesis, 5.5% of wild-type activity, unaltered stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme | Sus scrofa |
D650A | site-directed mutagenesis, inactive mutant | Sus scrofa |
D650N | site-directed mutagenesis, inactive mutant | Sus scrofa |
D697A | site-directed mutagenesis, 1.4% of wild-type activity | Sus scrofa |
D697N | site-directed mutagenesis, 4.0% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme | Sus scrofa |
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 | Sus scrofa |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Sus scrofa | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates in vitro, interacts via N-terminal RVH motif and EF hands | Sus scrofa | |
Mg2+ | coordidating bivalent metal ion is involved in substrate binding | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1,2-diacylglycerol | Sus scrofa | reaction takes place during stimulated phosphatidylinositol turnover | ADP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Purification (Comment) | Organism |
---|---|
partially, recombinant wild-type and point mutant enzymes from yeast by ion exchange chromatography | Sus scrofa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Sus scrofa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 1,2-diacylglycerol | - |
Sus scrofa | ADP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
ATP + 1,2-diacylglycerol | reaction takes place during stimulated phosphatidylinositol turnover | Sus scrofa | ADP + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DAGK | - |
Sus scrofa |
diacylglycerol kinase alpha | - |
Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Sus scrofa |