Aminopeptidase I
Aminopeptidase I | |||||||||
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Identifiers | |||||||||
EC number | 3.4.11.22 | ||||||||
CAS number | 9031-94-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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.; 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.; 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.; 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
- Aminopeptidase I at the US National Library of Medicine Medical Subject Headings (MeSH)
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