Alanine carboxypeptidase
| Alanine carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.6 | ||||||||
| CAS no. | 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 CC, Goldman P (August 1969). "Bacterial peptidases. 3. An enzyme specific for N-acyl linkages to alanine". The Journal of Biological Chemistry. 244 (16): 4467–72. 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)
