Reinvestigation of the roles of the carboxyl groups of glutathione with yeast glyoxalase I

FEBS Letters

D'Silva, Claudius¹ 

[1] Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, USA

关键词: (Yeast);    Glyoxalase;    Coenzyme analog;    Competitive inhibition;    Glutathione;   

DOI  :  10.1016/0014-5793(86)80694-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A number of carboxyl-substituted s-blocked glutathiones have been shown to be competitive inhibitors of yeast glyoxalase I at 25°C, pH 6.6. Amidation of the glycyl carboxyl group of S-(p-bromobenzyl)glutathione has no appreciable effect on binding whilst methylation reduces binding by 8.9-fold, indicating a steric constraint and the possible presence of a hydrogen bond in this region of the enzyme. Amidation of both carboxyl groups of S-(p-bromobenzyl)glutathione reduces binding significantly by 237-fold; this result agrees with electrostatic interaction of the Glu COO⁻ group with a group located within the enzyme surface as opposed to the Gly COO⁻ group, previously proposed.

【 授权许可】

Unknown