title: Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk.
abstract: 1. Aminopeptidase Ey, purified from the egg yolk of the hen (Gallus gallus domesticus), was studied for its specificity against oligopeptides at pH 7.5. The enzyme has a broad specificity for amino acid residues at P1 position. 2. The enzyme hydrolyzed N-terminal Xaa-Pro bonds in chicken brain peptide (Leu-Pro-Leu-Arg-PheNH2), substance P fragment 1-4 (Arg-Pro-Lys-Pro) and bradykinin fragment 1-5 (Arg-Pro-Pro-Gly-Phe), but did not hydrolyze substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-MetNH2) or bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg). 3. The enzyme released proline from Pro-Phe-Gly-Lys, while it was unable to release proline from melanocyte, stimulating the hormone release-inhibiting factor (Pro-Leu-GlyNH2) and schistoFMRF-amide (Pro-Asp-Val-Asp-His-Val-Phe-Leu-Arg-PheNH2).
authors.affiliation: Research Institute, Q.P. Corp., Tokyo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Tanaka
authors.forename: E
authors.initials: E
authors.lastname: Ichishima
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D001923:Brain Chemistry; D002645:Chickens; D004530:Egg Yolk / Q000201:enzymology*; D005260:Female; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D011392:Proline / Q000378:metabolism; D013373:Substance P / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D013373:Substance P; D011392:Proline; D000626:Aminopeptidases; D001920:Bradykinin