The human protein disulphide isomerase family: substrate interactions and functional properties.
The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells was one of the first mechanisms of catalysed protein folding to be discovered. Protein disulphide isomerase (PDI) is now known to catalyse all of the reactions that are involved in native disulphide bond formation, but despite more than 40 years of study, its mechanism of action is still not fully understood. This review discusses recent advances in our understanding of the human PDI family of enzymes and focuses on their functional properties, substrate interactions and some recently identified family members.
Ellgaard
Lars
L
Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
Ruddock
Lloyd W
LW
D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D013379:Substrate Specificity; D013879:Thioredoxins / Q000378:metabolism
D013879:Thioredoxins; D019704:Protein Disulfide-Isomerases