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  • Title: Isolation and characterization of glycolic acid dehydrogenase from human liver.
    Author: Fry DW, Richardson KE.
    Journal: Biochim Biophys Acta; 1979 Apr 12; 567(2):482-91. PubMed ID: 36161.
    Abstract:
    Glycolic acid dehydrogenase has been purified over 800-fold from human liver by (NH4)2SO4 fractionation and column chromatography with DEAE-cellulose and hydroxyapatite. The enzyme catalyzes the direct oxidation of glycolate to oxalate without forming glyoxylate as a free intermediate. Activity is found only in the liver in the soluble fraction. The enzyme is specific for glycolate and inhibits no activity towards glycine or glyoxylate. Glyoxylate and DL-phenyllactate exhibit the enzyme. Optimum activity occurs sharply at pH 6.1 and the Michaelis constant for glycolate was 6.3.10(-5)M. Molecular oxygen does not appear to be the electron acceptor and no requirement for cofactors has been demonstrated, althoug flavin mononucleotide, ascorbate and cytochrome c stimulate activity. The isolation of this enzyme which may account for a significant part of the normal oxalate excretion in man, provides a more complete understanding of the pathways of oxalate biosynthesis and must be taken into account when considering possible methods for controlling disorders of oxalate metabolism.
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