The Enzyme Database

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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; 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, 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. [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]
[EC 3.4.11.22 created 1997]
 
 


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