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首页> 外文期刊>Bulletin of the Korean Chemical Society >Engineering High Catalytic Efficiency of the Steroid Isomerase Activity of Human Glutathione S-transferase P1-1
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Engineering High Catalytic Efficiency of the Steroid Isomerase Activity of Human Glutathione S-transferase P1-1

机译:谷胱甘肽S-转移酶P1-1的类固醇异构酶活性的工程高催化效率。

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摘要

Glutathione S-transferases (GSTs) are a family of multifunctional enzymes that catalyze the formation of conjugates between reduced glutathione (GSH) and a variety of carcinogenic, mutagenic, toxic and pharmacologically active compounds.1'2 GSTs have also been shown to participate in other biological process. Certain GSTs can detoxify lipid and DNA hydroperoxide by their intrinsic peroxidase activity, while others can catalyze the isomerization of certain steroids. Mammalian cytosolic GSTs, which exist as homo- or hetero-dimers, are grouped into at least seven distinct classes -alpha, mu, pi, sigma, theta, sigma, kappa and zeta - according to their physical, chemical, immunological and structural properties.
机译:谷胱甘肽S-转移酶(GST)是一类多功能酶,催化还原型谷胱甘肽(GSH)与多种致癌,诱变,有毒和药理活性化合物之间的结合物形成。1'2GST也已证明参与其中。其他生物过程。某些GST可以通过其固有的过氧化物酶活性使脂质和DNA氢过氧化物解毒,而其他GST则可以催化某些类固醇的异构化。哺乳动物胞质GST以同型或异型二聚体形式存在,根据其物理,化学,免疫学和结构特性,至少分为七个不同的类别-α,μ,pi,σ,θ,σ,κ和zeta。 。

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