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Literature summary for 3.4.17.1 extracted from
- On the origin of the catalytic power of carboxypeptidase A and other metalloenzymes (2009), Proteins, 77, 536-550.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R127A | the mutation causes kcat to decrease from 12 to 0.012 which corresponds to a 6 kcal/mol decrease in the stabilization of transition state in the rate determining step | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | zinc metalloenzyme | Homo sapiens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gly-L-Tyr + H2O | slow substrate | Homo sapiens | Gly + L-Tyr | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Anson's enzyme | formerly | Homo sapiens |
| carboxypeptidase-A | - |
Homo sapiens |
| CPA | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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