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Substrate Specificity of Aminopeptidase Ey From Hen's (Gallus Domesticus) Egg Yolk

Substrate Specificity of Aminopeptidase Ey From Hen's (Gallus Domesticus) Egg Yolk

T Tanaka, E Ichishima

Comp Biochem Physiol B. 1993 May;105(1):105-10.

PMID: 7684960

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).

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP23815896	Bradykinin Fragment 1-5		23815-89-6	Price

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