Relaxed thiol substrate specificity of glutathione transferase effected by a non‐substrate glutathione derivative

FEBS Letters

Principato, Giovanni B.¹  Danielson, U.Helena¹  Mannervik, Bengt¹ 

[1] Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden

关键词: Conformational change;    Thiol substrate specificity;    Reaction mechanism;    Glutathione transferase;    Glutathione derivative;    CDNB;    1-chloro-2;    4-dinitrobenzene;   

DOI  :  10.1016/0014-5793(88)80722-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat glutathione transferase 4-4 catalysed the conjugation of 2-mercaptoethanol with 1-chloro-2,4-dinitrobenzene in the presence of S-methyl-glutathione. The reaction was linearly dependent on enzyme concentration and saturation was seen with respect to both 2-mercaptoethanol and S-methyl-glutathione concentration. High concentrations of S-methyl-gluta-thione were inhibitory. The results suggest that the natural substrate glutathione has two distinct functions in the normal catalytic reaction, (i) induction of a catalytically competent conformation of the enzyme and (ii) provision of the substrate sulfhydryl group in the reaction catalyzed.

【 授权许可】

Unknown