| Aminopeptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.22 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
- ^ Johnson MJ (1941). "Isolation and properties of a pure yeast polypeptidase". J. Biol. Chem. 137 (2): 575–586. doi: 10.1016/S0021-9258(19)56163-4.
- ^ 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.
- Aminopeptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Aminopeptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.22 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
- ^ Johnson MJ (1941). "Isolation and properties of a pure yeast polypeptidase". J. Biol. Chem. 137 (2): 575–586. doi: 10.1016/S0021-9258(19)56163-4.
- ^ 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.
- Aminopeptidase+I at the U.S. National Library of Medicine Medical Subject Headings (MeSH)