关键词: MSR PilB Trx disulfide-bond formation (Dsb) D methionine sulfoxide periplasm

来  源:   DOI:10.3390/antiox7100131   PDF(Pubmed)

Abstract:
Neisseria meningitidis, an obligate pathogenic bacterium in humans, has acquired different defense mechanisms to detect and fight the oxidative stress generated by the host\'s defense during infection. A notable example of such a mechanism is the PilB reducing system, which repairs oxidatively-damaged methionine residues. This review will focus on the catalytic mechanism of the two methionine sulfoxide reductase (MSR) domains of PilB, which represent model enzymes for catalysis of the reduction of a sulfoxide function by thiols through sulfenic acid chemistry. The mechanism of recycling of these MSR domains by various \"Trx-like\" disulfide oxidoreductases will also be discussed.
摘要:
脑膜炎奈瑟菌,人类的一种专性致病菌,已经获得了不同的防御机制来检测和对抗感染过程中宿主防御产生的氧化应激。这种机制的一个值得注意的例子是PilB减少系统,修复氧化损伤的蛋氨酸残留物。本文将重点介绍PilB的两个甲硫氨酸亚砜还原酶(MSR)结构域的催化机理,代表通过次磺酸化学催化硫醇还原亚砜功能的模型酶。还将讨论通过各种“Trx样”二硫化物氧化还原酶再循环这些MSR结构域的机制。
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