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The human protein disulphide isomerase family: substrate interactions and functional properties
Author(s) -
Ellgaard Lars,
Ruddock Lloyd W.
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400311
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , isomerase , protein folding , folding (dsp implementation) , enzyme , chemistry , biochemistry , substrate specificity , substrate (aquarium) , foldase , chaperone (clinical) , microbiology and biotechnology , biology , medicine , ecology , escherichia coli , groel , gene , electrical engineering , engineering , pathology
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.