Raina S, Missiakas D
Centre Médical Universitaire, Département de Biochimie Médicale, Genève, Switzerland.
Annu Rev Microbiol. 1997;51:179-202. doi: 10.1146/annurev.micro.51.1.179.
It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form. The formation of the disulfide bonds usually occurs simultaneously with the folding of the polypeptide, which means in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. In prokaryotes, the existence of redox proteins involved in the formation of disulfide bonds containing proteins has recently been revealed in the periplasm. The discovery of these redox proteins through various genetic approaches will be summarized, as well as the most recent insights regarding their biochemical and biological activities.
现在已经充分证实，蛋白质折叠在体内需要折叠辅助因子的协助。蛋白质中二硫键的形成或异构化是一个需要催化的缓慢过程。在新生多肽链中，半胱氨酸残基呈硫醇形式。二硫键的形成通常与多肽的折叠同时发生，这意味着在真核生物的内质网中或革兰氏阴性细菌的周质中。在原核生物中，最近在周质中发现了参与含二硫键蛋白质形成的氧化还原蛋白。将总结通过各种遗传方法对这些氧化还原蛋白的发现，以及关于它们的生化和生物学活性的最新见解。
