| EC |
3.4.11.22 |
| Accepted name: |
aminopeptidase I |
| Reaction: |
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates |
| Other name(s): |
aminopeptidase III; aminopeptidase yscI (gene name); leucine aminopeptidase IV; yeast aminopeptidase I |
| Comments: |
A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18 |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-94-1 |
| References: |
| 1. |
Johnson, M.J. Isolation and properties of a pure yeast polypeptidase. J. Biol. Chem. 137 (1941) 575–586. |
| 2. |
Metz, G. and Rohm, K.-H. Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochim. Biophys. Acta 429 (1976) 933–949. [DOI] [PMID: 5147] |
| 3. |
Chang, Y-H. and Smith, J.A. Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. J. Biol. Chem. 264 (1989) 6979–6983. [PMID: 2651436] |
| 4. |
Oda, M.N., Scott, S.V., Hefner-Gravink, A., Caffarelli, A.D. and Klionsky, D.J. Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I. J. Cell Biol. 132 (1996) 999–1010. [PMID: 8601598] |
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| [EC 3.4.11.22 created 1997] |
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