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Literature summary for 2.3.1.15 extracted from

  • Kessels, J.M.M.; Ousen, H.; Van Den Bosch, H.
    Studies on reconstituted partially purified glycerophosphate acyltransferase from Escherichia coli (1984), Eur. J. Biochem., 138, 543-549.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Phospholipids
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Monoacylglycerophosphate
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
Escherichia coli 5743
-
plasma membrane
-
Escherichia coli 5886
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K-12
-

Purification (Commentary)

Purification (Comment) Organism
solubilized Escherichia coli
solubilized, by non-ionic detergents and reconstituted in unilamellar phospholipid vesicles Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 1-acyl-sn-glycerol 3-phosphate mechanism Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution in phosphatidylcholine/phosphatidylglycerol, ratio 4:1, vesicles, 90% of active site of the reconstituted enzyme are located at the outside surface Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate temperature-dependent specificity of reconstituted enzyme Escherichia coli CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate saturated acyl-CoAs preferred Escherichia coli CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
oleoyl-CoA + sn-glycerol 3-phosphate
-
Escherichia coli CoA + 1-oleoyl-sn-glycerol 3-phosphate
-
?
palmitoyl-CoA + sn-glycerol 3-phosphate i.e. n-hexadecanoyl-CoA, best substrate Escherichia coli CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
reconstituted enzyme Escherichia coli