Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
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DOI：
10.1016/s0014-5793(98)00080-5
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发表时间：
1998-02-20
期刊：
影响因子：
3.5
通讯作者：
Di Ilio, C
中科院分区：
文献类型：
--
作者：
Casalone, E;Allocati, N;Di Ilio, C
为了研究近n端Tyr、Cys和Ser残基在细菌谷胱甘肽转移酶（GSTB1-1）活性中的作用，采用定点诱变方法替换了以下残基：酪氨酸-4、酪氨酸-5、丝氨酸-9、酪氨酸-10、丝氨酸-11和丝氨酸-13。本文的研究结果表明，与迄今为止研究的所有其他α、mu、pi、θ和σ类谷胱甘肽转移酶不同，GSTB1-1不利用任何酪氨酸、丝氨酸或酪氨酸残基来激活谷胱甘肽。这些结果还表明，细菌谷胱甘肽转移酶需要单独分类，(C) 1998年欧洲生化学会联合会。
In order to investigate the roles of near N-terminus Tyr, Cys, and Ser residues in the activity of bacterial glutathione transferase (GSTB1-1) site-directed mutagenesis was used to replace the following residues: Tyr-4, Tyr-5, Ser-9, Cys-10, Ser-11, and Ser-13, The results presented here show that, unlike all other alpha, mu, pi, theta and sigma classes of glutathione transferases so far investigated, GSTB1-1 does not utilise any Tyr, Ser or Cys residue to activate glutathione, These results also suggest that the bacterial glutathione transferases mag require classification into their own class, (C) 1998 Federation of European Biochemical Societies.