Ellgaard Lars, Ruddock Lloyd W
Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
EMBO Rep. 2005 Jan;6(1):28-32. doi: 10.1038/sj.embor.7400311.
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.
真核细胞内质网中二硫键形成的过程是最早被发现的催化蛋白质折叠机制之一。现在已知蛋白质二硫键异构酶（PDI）催化天然二硫键形成过程中涉及的所有反应，但尽管经过了40多年的研究，其作用机制仍未完全了解。本综述讨论了我们对人类PDI酶家族认识的最新进展，并重点关注其功能特性、底物相互作用以及一些最近鉴定出的家族成员。
