Aminopeptidase Ey
| Aminopeptidase Ey | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.20 | ||||||||
| 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 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
[edit]- ^ Ichishima E, Yamagata Y, Chiba H, Sawaguchi K, Tanaka T (1989). "Soluble and bound forms of aminopeptidase in hens egg-yolk". Agric. Biol. Chem. 53: 1867–1872. doi:10.1271/bbb1961.53.1867.
- ^ Tanaka T, Ichishima E (May 1993). "Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk". Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 105 (1): 105–10. doi:10.1016/0305-0491(93)90175-5. PMID 7684960.
- ^ Tanaka T, Ichishima E (November 1993). "Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme". The International Journal of Biochemistry. 25 (11): 1681–8. doi:10.1016/0020-711x(93)90528-m. PMID 8288037.
External links
[edit]- Aminopeptidase+Ey at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
