Zheng Y J, Ornstein R L
Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, USA.
J Biomol Struct Dyn. 1996 Oct;14(2):231-3. doi: 10.1080/07391102.1996.10508112.
The recently proposed catalytic role of the alpha-carboxylate of the Glu residue of glutathione in glutathione S-transferases (Widersten et al, Biochemistry 35, 7731-7742 (1996)) was examined. Based on structural considerations, it is clear that conformational changes in both glutathione and glutathione S-transferase are required. Recent kinetic studies by Ricci and coworkers (Ricci et al, J. Biol. Chem. 271, 16187-16192 (1996) and Caccuri et al, J. Biol. Chem. 271, 16193-16198 (1996)) may provide the missing evidence for these conformational changes. Possible ways to test this hypothesis are discussed.
我们研究了最近提出的谷胱甘肽的谷氨酸残基的α-羧酸盐在谷胱甘肽S-转移酶中的催化作用（Widersten等人，《生物化学》35卷，7731 - 7742页（1996年））。基于结构上的考虑，很明显谷胱甘肽和谷胱甘肽S-转移酶都需要发生构象变化。Ricci及其同事最近的动力学研究（Ricci等人，《生物化学杂志》271卷，16187 - 16192页（1996年）以及Caccuri等人，《生物化学杂志》271卷，16193 - 16198页（1996年））可能为这些构象变化提供了缺失的证据。本文讨论了检验这一假设的可能方法。
