Biology:Aspartyl aminopeptidase
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Short description: Class of enzymes
| Aspartyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Aspartyl aminopeptidase dodekamer, Bos taurus | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.11.21 | ||||||||
| CAS number | 9074-83-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aspartyl aminopeptidase (EC 3.4.11.21) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
Aminoacyl-arylamides are poor substrates.
References
- ↑ "An aminopeptidase from mouse brain cytosol that cleaves N-terminal acidic amino acid residues". Journal of Neurochemistry 40 (6): 1727–34. June 1983. doi:10.1111/j.1471-4159.1983.tb08148.x. PMID 6854330.
- ↑ "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase". The Journal of Biological Chemistry 273 (26): 15961–70. June 1998. doi:10.1074/jbc.273.26.15961. PMID 9632644.
External links
- Aspartyl+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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