Tubbs & Greville (1961) showed that D-2- hydroxy acid dehydrogenase (EC 1.1.2.4), present in liver and kidney in several animal species, cata- lyses the oxidation of D-lactate, D-malate and various straight-chain homologues. Similar NAD- independent D-lactate dehydrogenases have been isolated from micro-organisms (Haugaard, 1959; de Ley & Schel, 1959; Snoswell, 1959; Nygaard, 1960). However, the metabolic significance of the enzyme, or enzymes, has still to be determined since this involves an assessment of the roles of those reactions that result in the formation of D-lactate, D-malate and other D-2-hydroxy acids. When maleate is formed in metabolism it is usually isomerized to fumarate before hydration to give L-malate. This reaction was shown to occur when nicotinic acid is degraded by a strain ofPseudomona8 fluore8cen8 (Behrman & Stanier, 1957) and a similar isomerase is induced when Ataligene8 faecati8 is
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Hopper et al. (1968) studied this question.