Any feedback?
Literature summary extracted from
- Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli (1990), J. Biol. Chem., 265, 4111-4115.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.65 | S254C | mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase | Escherichia coli |
| 4.1.1.65 | S254T | mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.65 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.65 | Phosphatidyl-L-serine | - |
Escherichia coli | Phosphatidylethanolamine + CO2 | - |
? |  |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
