EC Number   |
Protein Variants |
Reference |
|---|
  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 |
-, 687738 |
| 2.7.1.174 | G184A |
site-directed mutagenesis of a conserved residue within the CTP transferase domain causing a loss of diacylglycerol kinase activity |
-, 687738 |
| 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 |
-, 687738 |
| 2.7.1.174 | more |
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 |
-, 687738 |
| 2.7.1.174 | more |
overexpression of DGK1 causes the appearance of phosphatidate-enriched membranes around the nucleus and leads to its expansion, without proliferating the cortical endoplasmic reticulum membrane. Deletion of DGK1 returns the phosphatidate and phosphatidylethanolamine levels of the pah1DELTA cells to normal |
-, 693092 |
| 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 |
-, 687738 |
| 2.7.1.174 | S44A |
the mutation does not affect phosphorylation of the enzyme |
-, 761456 |
| 2.7.1.174 | 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 |
-, 761456 |
| 2.7.1.174 | 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 |
-, 761456 |
| 2.7.1.174 | S5A |
the mutation does decreases phosphorylation of the enzyme by about 40% compared to the wild type enzyme |
-, 761456 |
