Abstract
Isolated rat liver peroxisomes catalyze the reduction of glyoxylate to glycolate. The peroxisomal glyoxylate reductase preferentially utilizes NADH and glyoxylate. It also reduces hydroxypyruvate and pyruvate, but no dehydrogenase activity is measurable at pH 9.2. Michaelis constants were 11.5 mM for glyoxylate and 10.5 μM for NADH, and the pH optimum was 6.4. A glutamate-glyoxylate aminotransferase (EC 2.6.1.4) is also present in rat liver peroxisomes. NADH-glyoxylate reductase (EC 1.1.1.26) in liver peroxisomes may function in a substrate-mediated electron shuttle for the oxidation of cellular NADH.
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