Proteins pp 675-681 | Cite as

Properties of the Hydrolase that Catalyzes Removal of the Blocked NH2-Terminal Amino Acid Residues from Polypeptides

  • Wanda M. Jones
  • Lois R. Manning
  • James M. Manning

Abstract

Acylpeptide hydrolase catalyzes the removal of the terminal blocking group together with the first amino acid residue of a peptide substrate: Acyl – AA1 - AA2 - AA3… AAn → Acyl - AA1 + AA2 - AA3… AAn The enzyme purified from human red cells has no detectable acetylase or carboxypeptidase activity. The enzyme activity is most conveniently assayed by use of blocked amino acid p-nitroanilides as substrates, or by the appearance of a new, free amino group in a peptide substrate1.

Keywords

Iodine Iodide Trypsin Methionine Leucine 

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Wanda M. Jones
    • 1
  • Lois R. Manning
    • 1
  • James M. Manning
    • 1
  1. 1.The Rockefeller UniversityNew YorkUSA

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