过氧化物氧化还原酶是硫氧还蛋白折叠超家族新成员的证据。
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
作者信息
Schröder E, Ponting C P
机构信息
Department of Chemistry, University of Exeter, United Kingdom.
出版信息
Protein Sci. 1998 Nov;7(11):2465-8. doi: 10.1002/pro.5560071125.
Abstract
Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.
摘要
过氧化物酶催化过氧化氢或烷基过氧化物还原为水或相应的醇。对其序列的详细分析表明，这些酶具有类似硫氧还蛋白（Trx）的折叠结构，因此是硫氧还蛋白和谷胱甘肽过氧化物酶（GPx）的同源物。基于序列和结构的多序列比对表明，过氧化物酶活性位点的半胱氨酸和GPx活性位点的硒代半胱氨酸在结构上是等效的。预计同源的过氧化物酶和GPx酶通过相似的反应中间体催化等效反应。
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