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- W1974409392 abstract "Lys-110 of human NADH-cytochrome b5 reductase was replaced by Ala, Met, or Arg by site-directed mutagenesis to evaluate the role of the residue. Km values of purified Lys-110-->Ala and Lys-110-->Met mutants for NADH were approximately 200-fold and 1,100-fold higher than that of the wild-type, respectively, while the value of the Arg mutant was almost the same as that of the wild-type. These results indicate that the positive charge at position 110 is important for NADH binding. The kcat value of Lys-110-->Ala was not affected, indicating that the residue only participates in the binding process in the reaction by forming an ionic interaction with phosphoryl group of NADH." @default.
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- W1974409392 date "1993-05-03" @default.
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- W1974409392 title "Role of Lys-110 of human NADH-cytochrome <i>b</i> <sub>5</sub> reductase in NADH binding as probed by site-directed mutagenesis" @default.
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- W1974409392 doi "https://doi.org/10.1016/0014-5793(93)81104-8" @default.
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