Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers

Bioorg Med Chem Lett. 2005 Feb 1;15(3):777-81. doi: 10.1016/j.bmcl.2004.11.005.


PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Buffers
  • Catalysis / drug effects
  • Humans
  • Kinetics
  • Oxidation-Reduction
  • Protein Disulfide-Isomerases / chemistry
  • Protein Disulfide-Isomerases / metabolism*
  • Protein Folding
  • Ribonuclease, Pancreatic / chemistry
  • Structure-Activity Relationship
  • Sulfhydryl Compounds / pharmacology*


  • Buffers
  • Sulfhydryl Compounds
  • Ribonuclease, Pancreatic
  • Protein Disulfide-Isomerases