Alanine carboxypeptidase
| Alanine carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.6 | ||||||||
| CAS number | 37288-70-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alanine carboxypeptidase (EC 3.4.17.6, N-benzoyl-L-alanine-amidohydrolase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups
This enzyme is isolated from soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid.
References
- ↑ Levy, C.C.; Goldman, P. (1969). "Bacterial peptidases". J. Biol. Chem. 244: 4467–4472. PMID 5806587.
- ↑ Miyagawa, E.; Takahiro, H.; Yoshinobu, M. (1986). "Purification and properties of N-benzoyl-L-alanine amidohydrolase from Corynebacterium equii". Agric. Biol. Chem. 50: 1527–1531. doi:10.1080/00021369.1986.10867595.
External links
- Alanine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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