Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates
aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I
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
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Metz, G. and Rohm, K.-H. Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochim. Biophys. Acta429 (1976) 933–949. [DOI] [PMID: 5147]
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]
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]