Aminopeptidase I
Aminopeptidase I (EC 3.4.11.22, aminopeptidase III, aminopeptidase yscI, leucine aminopeptidase IV, yeast aminopeptidase I) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide.
Aminoacyl-arylamides are poor substrates
References
- ↑ Johnson, M.J. (1941). "Isolation and properties of a pure yeast polypeptidase". J. Biol. Chem. 137: 575–586.
- ↑ Metz, G. and Rohm, K.-H. (1976). "Yeast aminopeptidase I. Chemical composition and catalytic properties". Biochim. Biophys. Acta 429: 933–949. doi:10.1016/0005-2744(76)90338-7. PMID 5147.
- ↑ Chang, Y-H. and Smith, J.A. (1989). "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae". J. Biol. Chem. 264: 6979–6983. PMID 2651436.
- ↑ Oda, M.N., Scott, S.V., Hefner-Gravink, A., Caffarelli, A.D. and Klionsky, D.J. (1996). "Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I". J. Cell Biol. 132: 999–1010. doi:10.1083/jcb.132.6.999. PMID 8601598.
External links
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|