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- W2074560686 abstract "Glycollate oxidase (glycollate: oxygen oxidoreductase, EC 1.1.3.1) from Pisum sativum has an unusual absorption spectrum which suggests that the flavin N(3)-H function of the FMN coenzyme is ionized at pH 8.3. The enzyme is reduced rapidly by the substrate glycollate to yield a normal, reduced FMN coenzyme which is readily reoxidized by O 2 . No evidence for the occurrence of covalent intermediates during reduction, as observed upon reduction of l -lactate oxidase from Mycobacterium smegmatis with the same substrate (Ghisla, S. and Massey, V. (1980) J. Biol. Chem. 255, 5688–5696), could be obtained. The enzyme was determined to be greater than 99.5% specific in the abstraction of the Re -hydrogen of glycollate. d -Lactate dehydrogenase from Lactobacillus leichmanii was shown to be only 97% selective for the Si -side in the reduction of glyoxylate. Glycollate oxidase was shown to be inhibited by α-hydroxybutynoate via covalent modification of the FMN coenzyme, in a fashion similar to that encountered with l -lactate oxidase (Schonbrunn, A., Abeles, R.H., Walsh, Ch.T., Ghisla, S., Ogata, H. and Massey, V. (1976) Biochemistry 15, 1798–1807). This inhibitor serves both as substrate and inactivator of the enzyme." @default.
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- W2074560686 date "1982-04-01" @default.
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- W2074560686 title "Studies on glycollate oxidase from pea leaves determination of stereospecificity and mode of inhibition by α-hydroxybutynoate" @default.
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- W2074560686 doi "https://doi.org/10.1016/0167-4838(82)90509-x" @default.
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