Any feedback?
Literature summary for 4.1.1.65 extracted from
- Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli (1988), Bioorg. Chem., 16, 184-188.
No PubMed abstract available
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| pyruvate | dependent on | Escherichia coli |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | bound to | Escherichia coli | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| phosphatidyl-L-serine = phosphatidylethanolamine + CO2 | reaction is completely stereospecific with overall retention of configuration | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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
