2.7.1.174: diacylglycerol kinase (CTP)
This is an abbreviated version!
For detailed information about diacylglycerol kinase (CTP), go to the full flat file.
Reaction
Synonyms
CTP-dependent DAG kinase, CTP-dependent diacylglycerol kinase, DAG kinase, DGK1, Dgk1p, diacylglycerol kinase (CTP dependent), More
ECTree
2.7.1.174 diacylglycerol kinase (CTP)Advanced search results
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results (Engineering
Engineering on EC 2.7.1.174 - diacylglycerol kinase (CTP)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
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
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
-
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
-
additional information
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
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
additional information
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
additional information
-
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
additional information
-
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
-
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
-
