Recognition site of yeast glutathione reductase for 2′-phosphate of NADP

Abstract

Phenyl glyoxal in borate buffer specifically inactivates the NADPH-linked activity of yeast glutathione reductase. While NAD + is ineffective, NADP + prevents the enzyme from inactivation, and in the process, protects two arginine residues from glyoxalation. These two arginine residues presumably function as the recognition site for the anionic 2′-phosphate group of NADP +.