Abstract
THE reduction of hydroxypyruvate to glycerate is brought about by crystalline L-lactic dehydrogenase of muscle1 with the production of L-glyceric acid2. A substrate-specific D-glycerate dehydrogenase, which may or may not be accompanied by lactic dehydrogenase, occurs in extracts of higher plants2. Hydroxypyruvic acid phosphate is not able to replace pyruvic acid as a substrate for lactic dehydrogenase3. These enzymes require diphosphopyridine nucleotide, and their equilibrium, being far towards the reduced metabolite, is unfavourable for the study of the oxidative production of hydroxypyruvate. The importance of this substance as a substrate for transketolase4 and transaminase5 led us to study the action on glyceric acid of preparations containing lactic dehydrogenase from yeast, which is not so inhibited by pyruvate and requires no coenzyme6–8.
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DICKENS, F., WILLIAMSON, D. Enzymic Oxidation of Glyceric Acid. Nature 178, 1118 (1956). https://doi.org/10.1038/1781118a0
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DOI: https://doi.org/10.1038/1781118a0
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