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  • Title: Chemical modification of histidine residue in substrate-binding domain of carbonyl reductase from rabbit kidney.
    Author: Imamura Y, Higuchi T, Otagiri M.
    Journal: Biochem Mol Biol Int; 1993 Dec; 31(6):1105-10. PubMed ID: 8193594.
    Abstract:
    Carbonyl reductase from rabbit kidney was rapidly inactivated by diethylpyrocarbonate (DEPC). A similar inactivation was observed in photooxidation of the enzyme by methylene blue. The inactivation by DEPC was time- and concentration-dependent and followed pseudo-first-order kinetics. The results obtained from the inactivation kinetics and the protective effect of 4-acetylpyridine (4-AP) with NADP+ against the inactivation led to the idea that one essential amino acid is located in substrate-binding domain of the enzyme. The treatment of the enzyme with DEPC formed N-carbethoxyhistidine. Judging from the effect of 4-AP with NADP+ on the formation of N-carbethoxyhistidine, it is concluded that one histidine residue is located in substrate-binding domain of the enzyme. Furthermore, whether one essential amino acid inactivated by DEPC corresponds to one histidine residue modified with DEPC is discussed.
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