Synthesis of Oxalic Acid by Enzymes from Lettuce Leaves

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Abstract
A rapid purification of lactate dehydrogenase (EC 1.1.1.27 and glycolate oxidase (EC 1.1.3.1)) from lettuce (L. sativa) leaves is described. The kinetics of both enzymes are reported in relation to their possible roles in the production of oxalate. Lettuce lactate dehydrogenase behaves like mammalian dehydrogenase, catalyzing the dismutation of glyoxylate to glycolate and oxalate. A model is proposed in which glycolate oxidase in the peroxisomes and lactate dehydrogenase in the cytosol are involved in the production of oxalate. The effect of pH on the balance between oxalate and glycolate produced from glyoxylate suggests that in leaves lactate dehydrogenase may function as part of an oxalate-based biochemical, pH-stat.
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