期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 28, 期 1, 页码 32-40出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0968-0004(02)00003-8
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资金
- NIGMS NIH HHS [GM-50389, R01 GM050389] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM050389] Funding Source: NIH RePORTER
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 activesite 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.
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