Inactivation of rabbit liver carbonyl reductase by phenylglyoxal and 2,3,4-trinitrobenzenesulfonate sodium.
The chemical modifications of rabbit liver carbonyl reductase (RLCR) with phenylglyoxal (PGO) and 2,3,4-trinitrobenzenesulfonate sodium (TNBS), which are respective chemical modifiers of arginine and lysine residues, were examined. RLCR was rapidly inactivated by these modifiers. Kinetic data for the inactivation demonstrated that each one of arginine and lysine residues is essential for catalytic activity of the enzyme. Furthermore, based on the protective effects of NADP+, NAD+ and their constituents against the inactivation of RLCR by PGO and TNBS, we propose the possibility that the functional arginine and lysine residues are located in the coenzyme-binding domain of RLCR and interact with the 2'-phosphate group of NADPH.
Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1, Oe-honmachi Kumamoto 862-0973, Japan. yorishig@gpo.kumamoto-u.ac.jp
Yorishige
Y
Imamura
Toshihisa
T
Koga
Hideaki
H
Shimada
Masaki
M
Otagiri
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D008969:Molecular Sequence Data; D010658:Phenylglyoxal / Q000378:metabolism / Q000494:pharmacology*; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014302:Trinitrobenzenesulfonic Acid / Q000378:metabolism / Q000494:pharmacology*
D014302:Trinitrobenzenesulfonic Acid; D000429:Alcohol Oxidoreductases; D010658:Phenylglyoxal