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

Jonathan D Gough; Watson J Lees

doi:10.1016/j.bmcl.2004.11.005

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.

Authors

Jonathan D Gough¹, Watson J Lees

Affiliation

¹ Department of Chemistry, Syracuse University, Syracuse, NY 13244, USA.

PMID: 15664856
DOI: 10.1016/j.bmcl.2004.11.005

Abstract

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*

Substances

Buffers
Sulfhydryl Compounds
Ribonuclease, Pancreatic
Protein Disulfide-Isomerases