Biology:Aminopeptidase Ey
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Short description: Class of enzymes
| Aminopeptidase Ey | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.20 | ||||||||
| 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 | ||||||||
| |||||||||
Aminopeptidase Ey (EC 3.4.11.20) is an enzyme.[1][2][3] This enzyme catalyses differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position
This enzyme is zinc glycoprotein.
References
- ↑ "Soluble and bound forms of aminopeptidase in hens egg-yolk". Agric. Biol. Chem. 53: 1867–1872. 1989. doi:10.1271/bbb1961.53.1867.
- ↑ "Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk". Comparative Biochemistry and Physiology. B, Comparative Biochemistry 105 (1): 105–10. May 1993. doi:10.1016/0305-0491(93)90175-5. PMID 7684960.
- ↑ "Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme". The International Journal of Biochemistry 25 (11): 1681–8. November 1993. doi:10.1016/0020-711x(93)90528-m. PMID 8288037.
External links
- Aminopeptidase+Ey at the US National Library of Medicine Medical Subject Headings (MeSH)
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