Casalone E, Allocati N, Ceccarelli I, Masulli M, Rossjohn J, Parker M W, Di Ilio C
Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Chieti, Italy.
FEBS Lett. 1998 Feb 20;423(2):122-4. doi: 10.1016/s0014-5793(98)00080-5.
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 may require classification into their own class.
为了研究靠近N端的酪氨酸、半胱氨酸和丝氨酸残基在细菌谷胱甘肽转移酶（GSTB1-1）活性中的作用，采用定点诱变来替换以下残基：酪氨酸-4、酪氨酸-5、丝氨酸-9、半胱氨酸-10、丝氨酸-11和丝氨酸-13。此处给出的结果表明，与迄今为止研究的所有其他α、μ、π、θ和σ类谷胱甘肽转移酶不同，GSTB1-1不利用任何酪氨酸、丝氨酸或半胱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可能需要分类为它们自己的类别。
