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The reactions of several mutants at position 244 and 261 of bacterial glycine oxidase (GO) were studied by stopped-flow and steady-state kinetic methods. Substituting H244 with phenylalanine, glutamate, and glutamine and M261 with histidine and tyrosine did not affect the expression of GO and the physicochemical properties of bound FAD. All the H244 and M261 mutants of GO we prepared retained activity...
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