Bacterial leucyl aminopeptidase
| Bacterial leucyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.10 | ||||||||
| CAS no. | 37288-67-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Bacterial leucyl aminopeptidase (EC 3.4.11.10, Aeromonas proteolytica aminopeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
This is a zinc enzyme.
References
- ^ Prescott, J.M.; Wilkes, S.H. (1966). "Aeromonas aminopeptidase: purification and some general properties". Arch. Biochem. Biophys. 117: 328–336. doi:10.1016/0003-9861(66)90420-6. PMID 4961737.
- ^ Dick, A.J.; Matheson, A.T.; Wang, J.H. (1970). "A ribosomal-bound aminopeptidase in Escherichia coli B: purification and properties". Can. J. Biochem. 48: 1181–1188. doi:10.1139/o70-184. PMID 4920230.
- ^ Rabier, D.; Desmazeaud, M.J. (1973). "Inventaire des différentes activités peptidasiques intracellulaires de Streptococcus thermophilus. Purification et propriétés d’une dipeptide-hydrolase et d’une aminopeptidase". Biochimie. 55: 389–404. doi:10.1016/s0300-9084(73)80204-4. PMID 4749719.
External links
- Bacterial+leucyl+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)