家蚕未分类谷胱甘肽转移酶活性位点的结构解析
Structural insight into the active site of a Bombyx mori unclassified glutathione transferase.
作者信息
Hossain Md Tofazzal, Yamamoto Kohji
机构信息
a Faculty of Agriculture , Kyushu University Graduate School , Fukuoka , Japan.
出版信息
Biosci Biotechnol Biochem. 2015;79(6):989-91. doi: 10.1080/09168451.2014.1002450. Epub 2015 Jan 22.
Glutathione transferases (GSTs) are major detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here, we identify amino acid residues of an unclassified GST from Bombyx mori, bmGSTu-interacting glutathione (GSH). Site-directed mutagenesis of bmGSTu mutants indicated that amino acid residues Asp103, Ser162, and Ser166 contribute to catalytic activity.
谷胱甘肽转移酶（GSTs）是主要的解毒酶，在抵御各种环境毒物以及氧化应激中发挥核心作用。在此，我们鉴定了家蚕中一种未分类的GST（bmGSTu）与谷胱甘肽（GSH）相互作用的氨基酸残基。bmGSTu突变体的定点诱变表明，氨基酸残基Asp103、Ser162和Ser166对催化活性有贡献。
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