Biology:Clostridial aminopeptidase
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Short description: Class of enzymes
| Clostridial aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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
- ↑ "A novel aminopeptidase from Clostridium histolyticum". Biochemical and Biophysical Research Communications 50 (2): 405–12. January 1973. doi:10.1016/0006-291x(73)90855-3. PMID 4631895.
- ↑ "An extracellular aminopeptidase from Clostridium histolyticum". European Journal of Biochemistry 63 (1): 271–87. March 1976. doi:10.1111/j.1432-1033.1976.tb10229.x. PMID 4318.
- ↑ Extracellular aminopeptidase from Clostridium histolyticum. Methods in Enzymology. 45. 1976. pp. 544–52. doi:10.1016/s0076-6879(76)45048-6.
External links
- Clostridial+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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