Mapping the active site of papain with the aid of peptide substrates and inhibitors.

  title={Mapping the active site of papain with the aid of peptide substrates and inhibitors.},
  author={A. Berger and Israel Schechter},
  journal={Philosophical transactions of the Royal Society of London. Series B, Biological sciences},
  volume={257 813},
  • A. Berger, I. Schechter
  • Published 1970
  • Chemistry, Medicine
  • Philosophical transactions of the Royal Society of London. Series B, Biological sciences
The active site of an enzyme performs the twofold function of binding a substrate and catalysing a reaction. [...] Key Method In the present series of investigations on proteolytic enzymes, our approach is to compare the activity of the enzyme towards ( a ) peptides of increasing length, ( b ) diastereoisomeric pairs of peptides in which a particular amino acid residue has been replaced by its antipode, and ( c ) pairs of substrates in which a particular side chain (say a methyl group) has been replaced by…Expand
Studies on the extended active sites of acid proteinases.
The results indicate that the extended active site of pepsin can accommodate a sequence of at least seven amino-acid residues, and give further evidence for the importance of secondary interactions in determining the catalytic efficiency of enzymes that act on oligomeric substrates. Expand
Mapping Toe Active Site of Carboxypeptidase‐A: A Proposed Scheme for Substrate Binding at the Active Site
The aim of the work presented here was to characterize the active site of carboxypeptidase A. The kinetic constants , kcat and for the enzymatic hydrolysis of the C-terminal bond in a number ofExpand
Structure of a Switchable Subtilisin Complexed with a Substrate and with the Activator Azide†
Activity measurements showing that the enzyme is activated more than 3000-fold by azide are reported and the mechanism of anion-dependent proteolysis appears to be a slight modification of the accepted charge-relay mechanism for serine proteases. Expand
The active site of porcine elastase.
  • D. Atlas
  • Chemistry, Medicine
  • Journal of molecular biology
  • 1975
The mapping of the active site of pancreatic porcine elastase is described, and it includes the size of the site, the stereospecificity and the specificity of its various subsites. Expand
Chemical modifications of the subtilisins with special reference to the binding of large substrates. A review
Subtilisin type Carlsberg and subtilisin BPN' are two well characterized extracellular proteases fromBacillus subtilis andBacillus amyloquefaciens, respectively. The present review summarizes theExpand
Clarification of substrate specificity of papain by crystal analyses of complexes with covalent-type inhibitors.
The results show that the hydrophobic regions consisting of Val-133, Val-157 and Asp-158 and of Tyr-61, Gly-66 and Tyr-67 residues interact with the hydrophic P2 and P3 side chains of inhibitors, thus indicating the function of the former and latter binding pockets as S2 and S3 subsites, respectively. Expand
Binding of chloromethyl ketone substrate analogues to crystalline papain.
This study determined by the difference-Fourier technique the binding mode for the substrate in the groove in order to explain the substrate specificity of the enzyme (P2 should have a hydrophobic side chain) and to contribute to an elucidation of the catalytic mechanism. Expand
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC, has been determined by X-ray diffraction at 0.20-nmExpand
Novel kinetic analysis of enzymatic dipeptide synthesis: effect of pH and substrates on thermolysin catalysis.
This article introduces the Michaelis-Menten equation taking pH into account, and applies it to the pH-activity profile of the thermolysin-catalyzed dipeptide synthesis, and succeeds in evaluating the substrates-induced change of the dissociation states of the active site of thermoly sin using the hydrophobicity of substrates. Expand
Mechanism of action of thrombin on fibrinogen. IV. Further mapping of the active sites of thrombin and trypsin.
The data indicate that thrombin specificity is dependent on interactions between the enzyme and all three of the amino acids to the “left” of the arg-gly bond, and is consistent with the hypothesis that the active site cleft ofThrombin may be quite narrow. Expand