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Literature summary 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
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.65 | pyruvate | dependent on | Escherichia coli |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.1.1.65 | membrane | bound to | Escherichia coli | 16020 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.65 | Escherichia coli | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.1.1.65 | phosphatidyl-L-serine = phosphatidylethanolamine + CO2 | reaction is completely stereospecific with overall retention of configuration | 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 | - |
? | |
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Release 2023.1 (January 2023)
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