Inactivation of Rabbit Liver Carbonyl Reductase by Phenylglyoxal and 2,3,4-Trinitrobenzenesulfonate Sodium |
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Authors: | Yorishige Imamura Toshihisa Koga Hideaki Shimada Masaki Otagiri |
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Institution: | 1. Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1, Oe-honmachi Kumamoto 862-0973, Japan;2. Faculty of Education, Kumamoto University, 2-40-1, Kurokami, Kumamoto 860-8555, Japan |
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Abstract: | 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. |
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Keywords: | Carbonyl Reductase Chemical Modification Rabbit Liver Arginine Residue Lysine Residue Coenzyme-binding Domain |
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