Clostridial aminopeptidase
Appearance
Clostridial aminopeptidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.11.13 | ||||||||
CAS no. | 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
[edit]- ^ Kessler E, Yaron A (January 1973). "A novel aminopeptidase from Clostridium histolyticum". Biochemical and Biophysical Research Communications. 50 (2): 405–12. doi:10.1016/0006-291x(73)90855-3. PMID 4631895.
- ^ Kessler E, Yaron A (March 1976). "An extracellular aminopeptidase from Clostridium histolyticum". European Journal of Biochemistry. 63 (1): 271–87. doi:10.1111/j.1432-1033.1976.tb10229.x. PMID 4318.
- ^ Kessler E, Yaron A (1976). "Extracellular aminopeptidase from Clostridium histolyticum". Part B: Proteolytic Enzymes. Methods in Enzymology. Vol. 45. pp. 544–52. doi:10.1016/s0076-6879(76)45048-6. ISBN 978-0-12-181945-3. PMID 13266.
External links
[edit]- Clostridial+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)