4.5 Article

Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme

期刊

BIOCHEMICAL JOURNAL
卷 469, 期 -, 页码 279-288

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BJ20141423

关键词

disulfide formation; electron transfer; endoplasmic reticulum; protein disulfide isomerase; redox potential; thiol-disulfide exchange

资金

  1. Wellcome Trust [088053]
  2. BBSRC [BB/L00593X/1] Funding Source: UKRI
  3. Wellcome Trust [103720/Z/14/Z] Funding Source: researchfish
  4. Wellcome Trust [103720/Z/14/Z] Funding Source: Wellcome Trust

向作者/读者索取更多资源

The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes. These enzymes catalyse the introduction, reduction and isomerization of disulfides. To function continuously they require an oxidase to reform the disulfide at their active site. To determine how each family member can be recycled to catalyse disulfide exchange, we have studied whether disulfides are transferred between individual PDI family members. We studied disulfide exchange either between purified proteins or by identifying mixed disulfide formation within cells grown in culture. We show that disulfide exchange occurs efficiently and reversibly between specific PDIs. These results have allowed us to define a hierarchy for members of the PDI family, in terms of ability to act as electron acceptors or donors during thiol-disulfide exchange reactions and indicate that there is no kinetic barrier to the exchange of disulfides between several PDI proteins. Such promiscuous disulfide exchange negates the necessity for each enzyme to be oxidized by Ero1 (ER oxidoreductin 1) or reduced by a reductive system. The lack of kinetic separation of the oxidative and reductive pathways in mammalian cells contrasts sharply with the equivalent systems for native disulfide formation within the bacterial periplasm.

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