The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
MCA Laboissiere, SL Sturley, RT Raines - Journal of Biological Chemistry, 1995 - ASBMB
Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that
catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active
site CGHC. Haploid pdi1Δ Saccharomyces cerevisiae are inviable, but can be
complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI
(shufflease). In contrast, pdi1Δ yeast cannot be complemented with a gene coding for SGHC
PDI. In vitro, shufflease is an efficient catalyst for the isomerization of existing disulfide bonds …
catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active
site CGHC. Haploid pdi1Δ Saccharomyces cerevisiae are inviable, but can be
complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI
(shufflease). In contrast, pdi1Δ yeast cannot be complemented with a gene coding for SGHC
PDI. In vitro, shufflease is an efficient catalyst for the isomerization of existing disulfide bonds …
