Aminopeptidase Y | |||||||||
---|---|---|---|---|---|---|---|---|---|
Lysyl aminopeptidase dodekamer, Pyrococcus furiosus | |||||||||
Identifiers | |||||||||
EC no. | 3.4.11.15 | ||||||||
CAS no. | 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. This enzyme catalyses the following chemical reaction
- Preferentially, release of N-terminal lysine
This enzyme requires Co. It is inhibited by Zn and Mn.
References
- Achstetter T, Ehmann C, Wolf DH (November 1982). "Aminopeptidase Co, a new yeast peptidase". Biochemical and Biophysical Research Communications. 109 (2): 341–7. doi:10.1016/0006-291x(82)91726-0. PMID 6758786.
- Yasuhara T, Nakai T, Ohashi A (May 1994). "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. doi:10.1016/S0021-9258(17)36878-3. PMID 8175799.
- Nishizawa M, Yasuhara T, Nakai T, Fujiki Y, Ohashi A (May 1994). "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. doi:10.1016/S0021-9258(17)36879-5. PMID 8175800.
External links
- Aminopeptidase+Y at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: proteases (EC 3.4) | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
3.4.11-19: Exopeptidase |
| ||||||||||||||
3.4.21-25: Endopeptidase | |||||||||||||||
3.4.99: Unknown |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|