Biology:Aminopeptidase I
From HandWiki
Short description: Class of enzymes
| Aminopeptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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
- ↑ "Isolation and properties of a pure yeast polypeptidase". J. Biol. Chem. 137 (2): 575–586. 1941. doi:10.1016/S0021-9258(19)56163-4.
- ↑ "Yeast aminopeptidase I. Chemical composition and catalytic properties". Biochimica et Biophysica Acta (BBA) - Enzymology 429 (3): 933–49. May 1976. doi:10.1016/0005-2744(76)90338-7. PMID 5147.
- ↑ "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae". The Journal of Biological Chemistry 264 (12): 6979–83. April 1989. doi:10.1016/S0021-9258(18)83527-X. PMID 2651436.
- ↑ "Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I". The Journal of Cell Biology 132 (6): 999–1010. March 1996. 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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