A comparison between the binding modes of a substrate and inhibitor to papain as observed in complex crystal structures

This publication has 10 references indexed in Scilit:

• On the size of the active site in proteases. I. Papain
  Published by Elsevier ,2005
• Mode of binding of E‐64‐c, a potent thiol protease inhibitor, to papain as determined by X‐ray crystal analysis of the complex
  FEBS Letters, 1989
• Crystal structure of a papain-E-64 complex
  Biochemistry, 1989
• 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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide)
  Biochemical Journal, 1984
• L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
  Biochemical Journal, 1982
• Inhibition of Epoxide Derivatives on Chicken Calcium-Activated Neutral Protease (CANP) In Vitro and In Vivo1
  The Journal of Biochemistry, 1980
• Purification and Properties of a New Cathepsin from Rat Liver1
  The Journal of Biochemistry, 1978
• Structure and synthesis of E-64, a new thiol protease inhibitor.
  Agricultural and Biological Chemistry, 1978
• Isolation and characterization of E-64, a new thiol protease inhibitor.
  Agricultural and Biological Chemistry, 1978
• Binding of chloromethyl ketone substrate analogs to crystalline papain
  Biochemistry, 1976