Manta Bruno, Boyd Dana, Berkmen Mehmet
New England Biolabs, Ipswich, MA 01938.
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.
EcoSal Plus. 2019 Feb;8(2). doi: 10.1128/ecosalplus.ESP-0012-2018.
The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in all domains of life. With the discovery in the early 1990s that disulfide bond formation is catalyzed by enzymes, the field of oxidative folding of proteins was born. played a central role as a model organism for the elucidation of the disulfide bond-forming machinery. Since then, many of the enzymatic players and their mechanisms of forming, breaking, and shuffling disulfide bonds have become understood in greater detail. This article summarizes the discoveries of the past 3 decades, focusing on disulfide bond formation in the periplasm of the model prokaryotic host .
二硫键的形成对于生命所有领域中许多胞外蛋白的折叠至关重要。随着20世纪90年代初发现二硫键的形成由酶催化,蛋白质氧化折叠领域应运而生。 作为阐明二硫键形成机制的模式生物发挥了核心作用。从那时起,许多参与形成、断裂和重排二硫键的酶及其机制已得到更详细的了解。本文总结了过去30年的发现,重点关注模式原核宿主周质中二硫键的形成。