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Structure, mechanism and regulation of peroxiredoxins.
Trends in Biochemical Sciences ( IF 13.8 ) Pub Date : 2003-01-09 , DOI: 10.1016/s0968-0004(02)00003-8
Zachary A Wood 1 , Ewald Schröder , J Robin Harris , Leslie B Poole
Affiliation  

Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerization states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidized to a sulfenic acid by the peroxide substrate. The recycling of the sulfenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity.

中文翻译:

过氧化物酶的结构,机理和调控。

过氧化物酶(Prxs)是抗氧化剂酶的一个普遍存在的家族,它也控制细胞因子诱导的过氧化物水平,该水平介导哺乳动物细胞中的信号转导。可以通过改变磷酸化,氧化还原和可能的低聚状态来调节Prx。Prxs分为三类:典型的2-Cys Prxs;典型的2-Cys Prxs。非典型2 Cys Prxs; 和1-Cys Prxs。所有Prx具有相同的基本催化机理,其中活性部位的半胱氨酸(过氧化物半胱氨酸)被过氧化物底物氧化为亚磺酸。将亚硫酸循环回硫醇是区分这三种酶的区别。使用晶体结构,已经得出了典型的2-Cys Prxs的详细催化循环,包括提议用来控制酶活性的氧化还原调节的低聚物状态模型。
更新日期:2019-11-01
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