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Literature summary for 2.7.1.107 extracted from

  • Abe, T.; Lu, X.; Jiang, Y.; Boccone, C.E.; Qian, S.; Vattem, K.M.; Wek, R.C.; Walsh, J.P.
    Site-directed mutagenesis of the active site of diacylglycerol kinase alpha: calcium and phosphatidylserine stimulate enzyme activity via distinct mechanisms (2003), Biochem. J., 375, 673-680.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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(Commentary)

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

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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Sus scrofa 16020
-

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partially, recombinant wild-type and point mutant enzymes from yeast by ion exchange chromatography Sus scrofa

Reaction

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 and Products (Substrate)

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

Synonyms Comment Organism
DAGK
-
Sus scrofa
diacylglycerol kinase alpha
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
ATP
-
Sus scrofa