Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | Escherichia coli | involved in phospholipid biosynthesis | CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
K12, strains: LCD45 and CE1061 | - |
Purification (Comment) | Organism |
---|---|
partial, separated from EC 2.3.1.15 using Triton X-100, the enzyme is not solubilized by Triton X-100 or cholate | Escherichia coli |
Renatured (Comment) | Organism |
---|---|
by mixing 1 vol. of the fraction containing the enzyme with 4 vol. of sonicated phosphatidylcholine/phosphatidylglycerol or total E. coli lipid vesicles | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0008 | - |
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + 1,2-diacyl-sn-glycerol 3-phosphate | i.e. phosphatidic acid | ? | |
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | involved in phospholipid biosynthesis | Escherichia coli | CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
acyl-CoA + 1-palmitoyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + 1-palmitoyl-2-acyl-sn-glycerol 3-phosphate | - |
? | |
acyl-CoA + linoleoyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + ? | - |
? | |
acyl-CoA + myristoyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + ? | - |
? | |
additional information | lysophosphatidic acid, synthesized by EC 2.3.1.15, is utilized by the enzyme without prior mixing with the total membrane-associated pool of lysophosphatidic acid, and suggest a close proximity of the two enzymes in native E. coli membranes. This property of the acyltransferases is lost upon separation and reconstitution of enzyme activities | Escherichia coli | ? | - |
? | |
oleoyl-CoA + 1-acyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + 1-acyl-2-oleoyl-sn-glycerol 3-phosphate | - |
? | |
palmitoyl-CoA + 1-acyl-sn-glycerol 3-phosphate | - |
Escherichia coli | CoA + 1-acyl-2-palmitoyl-sn-glycerol 3-phosphate | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Escherichia coli |