Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk

Comp Biochem Physiol B. 1993 May;105(1):105-10. doi: 10.1016/0305-0491(93)90175-5.

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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases / metabolism*
  • Animals
  • Bradykinin / metabolism
  • Brain Chemistry
  • Chickens
  • Egg Yolk / enzymology*
  • Female
  • Molecular Sequence Data
  • Nerve Tissue Proteins / metabolism
  • Peptide Fragments / metabolism
  • Proline / metabolism
  • Substance P / metabolism
  • Substrate Specificity

Substances

  • Nerve Tissue Proteins
  • Peptide Fragments
  • Substance P
  • Proline
  • Aminopeptidases
  • Bradykinin