Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates

Bioorg Med Chem Lett. 1999 Jan 18;9(2):187-92. doi: 10.1016/s0960-894x(98)00715-x.

Abstract

Anisylazoformyllysine (CH3OC6H4-N = N-CO-Lys-OH) is rapidly hydrolyzed at the acyl-lysine linkage by the zinc-enzyme porcine carboxypeptidase B. The catalytic reaction is readily monitored spectrophotometrically by disappearance of the intense absorption (348.5 nm, epsilon 18400) of the azo chromophore, which chemically fragments after substrate cleavage. Carboxypeptidase Y has no activity toward this type of substrate.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Carboxypeptidase B
  • Carboxypeptidases / chemistry*
  • Catalysis
  • Cathepsin A
  • Dose-Response Relationship, Drug
  • Hydrolysis
  • Spectrophotometry
  • Swine
  • Time Factors
  • Yeasts

Substances

  • Carboxypeptidases
  • Cathepsin A
  • Carboxypeptidase B