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- W1500619079 abstract "Flavin-dependent external monooxygenases and oxidases could catalyze the same flavin oxidation reaction involving distinct mechanisms. To gain insights into enzyme structure-function relationship, site-directed mutagenesis was carried out for Vibrio harveyi luciferase, a monooxygenase. The substitution of the alpha subunit cysteine 106 by alanine shows unambiguously that the alphaCys106 is not essential to catalysis. The corresponding substitution by valine resulted in a substantial reduction of the bioluminescence activity correlatable with the induction of a new flavin oxidation activity typical for oxidases. These findings indicate that mutation of a single noncatalytic residue at the active center of a flavoenzyme could transform one enzyme type to another, thus highlighting the subtlety of enzyme active site structure in relation to catalysis and the versatility of enzyme evolution." @default.
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- W1500619079 date "1990-03-01" @default.
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- W1500619079 title "Elicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue." @default.
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- W1500619079 doi "https://doi.org/10.1016/s0021-9258(19)39546-8" @default.
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