A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.

Ähnliche Einträge

• Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin.
  von: Knight, C G
  Veröffentlicht: (1980)
• Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).
  von: Willenbrock, F, et al.
  Veröffentlicht: (1984)
• Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4.
  von: Willenbrock, F, et al.
  Veröffentlicht: (1985)
• L-arginine recognition by yeast arginyl-tRNA synthetase.
  von: Cavarelli, J, et al.
  Veröffentlicht: (1998)
• Chemical synthesis and papain-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-lysine p-nitroanilide.
  von: Mackenzie, N E, et al.
  Veröffentlicht: (1985)