EC |
3.4.11.15 |
Accepted name: |
aminopeptidase Y |
Reaction: |
Preferentially, release of N-terminal lysine |
Other name(s): |
aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase |
Comments: |
Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more slowly, Arg-NHPhNO2. Type example of peptidase family M28 |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 114796-97-3 |
References: |
1. |
Achstetter, T., Ehmann, C. and Wolf, D.H. Aminopeptidase Co, a new yeast peptidase. Biochem. Biophys. Res. Commun. 109 (1982) 341–347. [DOI] [PMID: 6758786] |
2. |
Yasuhara, T., Nakai, T. and Ohashi, A. Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B. J. Biol. Chem. 269 (1994) 13644–13650. [PMID: 8175799] |
3. |
Nishizawa, M., Yasuhara, T., Nakai, T., Fujiki, Y. and Ohashi, A. Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase. J. Biol. Chem. 269 (1994) 13651–13655. [PMID: 8175800] |
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[EC 3.4.11.15 created 1989, modified 1997] |
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