Component of a complex that catalyzes the oxidation of glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required for E.coli to grow on glycolate as a sole source of carbon (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with a similar rate (PubMed:4557653). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown (PubMed:4557653). A + glycolate = AH2 + glyoxylate (R)-lactate + A = AH2 + pyruvate In vitro the glycolate oxidase activity is inhibited by the sulfhydryl inhibitors CuSO4 and PCMB, by KCN, but not by the metal complexing agent EDTA. Parameters measured from a partially purified enzyme from extracts of glycolate grown cells. Optimum pH is 8.0-8.8. The glycolate oxidase likely consists of three subunits, GlcD, GlcE and GlcF. Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes. Part of the glcDEFGB operon, which is induced by growth on glycolate, under the positive control of GlcC. Also induced by growth on acetate. Expression of the glc operon is strongly dependent on the integration host factor (IHF) and is repressed by the global respiratory regulator ArcA-P. Abolishes glycolate oxidase activity. Is unable to grow on glycolate as the sole source of carbon, in contrast to wild type. Fuses together glcE and glcF.