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
[edit]- ^ Prescott JM, Wilkes SH (November 1966). "Aeromonas aminopeptidase: purification and some general properties". Archives of Biochemistry and Biophysics. 117 (2): 328–36. doi:10.1016/0003-9861(66)90420-6. PMID 4961737.
- ^ Dick AJ, Matheson AT, Wang JH (November 1970). "A ribosomal-bound aminopeptidase in Escherichia coli B: purification and properties". Canadian Journal of Biochemistry. 48 (11): 1181–8. doi:10.1139/o70-184. PMID 4920230.
- ^ Rabier D, Desmazeaud MJ (1973). "[Inventory of different intracellular peptidase activities in Streptococcus thermophilus. Purification and properties of a dipeptide hydrolase and an aminopeptidase]". Biochimie. 55 (4): 389–404. doi:10.1016/s0300-9084(73)80204-4. PMID 4749719.
External links
[edit]- Bacterial+leucyl+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
