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Aminopeptidase I
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From Wikipedia, the free encyclopedia
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
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Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide.
Aminoacyl-arylamides are poor substrates
References
[edit]
^ Metz G, Röhm KH (May 1976). "Yeast aminopeptidase I. Chemical composition and catalytic properties". Biochimica et Biophysica Acta (BBA) - Enzymology. 429 (3): 933–49. doi:10.1016/0005-2744(76)90338-7. PMID 5147.
^ Chang YH, Smith JA (April 1989). "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae". The Journal of Biological Chemistry. 264 (12): 6979–83. doi:10.1016/S0021-9258(18)83527-X. PMID 2651436.
^ Oda MN, Scott SV, Hefner-Gravink A, Caffarelli AD, Klionsky DJ (March 1996). "Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I". The Journal of Cell Biology. 132 (6): 999–1010. doi:10.1083/jcb.132.6.999. PMC 2120762. PMID 8601598.
External links
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Aminopeptidase_I&oldid=1172339839"
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