Biology:Aminopeptidase Y
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Short description: Class of enzymes
| Aminopeptidase Y | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Lysyl aminopeptidase dodekamer, Pyrococcus furiosus | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.11.15 | ||||||||
| CAS number | 114796-97-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aminopeptidase Y (EC 3.4.11.15, aminopeptidase Co, aminopeptidase (cobalt-activated), lysyl aminopeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Preferentially, release of N-terminal lysine
This enzyme requires Co2+. It is inhibited by Zn2+ and Mn2+.
References
- ↑ "Aminopeptidase Co, a new yeast peptidase". Biochemical and Biophysical Research Communications 109 (2): 341–7. November 1982. doi:10.1016/0006-291x(82)91726-0. PMID 6758786.
- ↑ "Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B". The Journal of Biological Chemistry 269 (18): 13644–50. May 1994. doi:10.1016/S0021-9258(17)36878-3. PMID 8175799.
- ↑ "Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase". The Journal of Biological Chemistry 269 (18): 13651–5. May 1994. doi:10.1016/S0021-9258(17)36879-5. PMID 8175800.
External links
- Aminopeptidase+Y at the US National Library of Medicine Medical Subject Headings (MeSH)
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