Glycolate oxidase [EC 1.1.3.1, glycolate: oxygen oxidoreductase, kidney] was purified 740 fold from hog kidney renal cortex by calcium phosphate gel treatment, ammonium sulfate fractionation and column chromatography on DEAE-cellulose and hydroxylapatite. The glycolate oxidase utilized glycolic acid most rapidly, and DL-glyceric, α-hydro-xybutyric and l- and D-lactic acids much more slowly. The Km for glycolate was 0.30 mM. FMN was found to be a cofactor of the enzyme, as judged by the absorption spectrum, activating effect, and paper electrophoretic analysis. The Km for FMN was 0.71 mM. Employing a newly devised microassay method including solvent extraction of radioactive compounds, glyoxylic acid was shown to be the enzymatic product of the oxidase reaction, but not oxalic acid; in the absence of catalase [EC 1.11.1.6] glyoxylic acid was further oxidized nonenzymatically to yield formic acid and CO2 by H2O2, which was generated during the oxidase reaction.
No takes yet. Share an insight, caveat, or question.
Tokushige et al. (1967) studied this question.