Clostridial aminopeptidase
Clostridial aminopeptidase | |||||||||
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Identifiers | |||||||||
EC number | 3.4.11.13 | ||||||||
CAS number | 59680-69-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Clostridial aminopeptidase (EC 3.4.11.13, Clostridium histolyticum aminopeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-Pro-
This enzyme is secreted enzyme from Clostridium histolyticum. It requiring Mn2+ or Co2+.
References
- ↑ Kessler, E.; Yaron, A. (1973). "A novel aminopeptidase from Clostridium histolyticum". Biochem. Biophys. Res. Commun. 50: 405–412. doi:10.1016/0006-291x(73)90855-3. PMID 4631895.
- ↑ Kessler, E.; Yaron, A. (1976). "An extracellular aminopeptidase from Clostridium histolyticum". Eur. J. Biochem. 63: 271–287. doi:10.1111/j.1432-1033.1976.tb10229.x. PMID 4318.
- ↑ Kessler, E.; Yaron, A. (1976). "Extracellular aminopeptidase from Clostridium histolyticum". Methods Enzymol. 45: 544–552. doi:10.1016/s0076-6879(76)45048-6. PMID 13266.
External links
- Clostridial aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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