Abstract:
:Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Jessop CE,Chakravarthi S,Watkins RH,Bulleid NJdoi
10.1042/BST0320655keywords:
subject
Has Abstractpub_date
2004-11-01 00:00:00pages
655-8issue
Pt 5eissn
0300-5127issn
1470-8752pii
BST0320655journal_volume
32pub_type
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