Occurrence and Subcellular Distribution of Enzymes Involved in the Glycolate Pathway and Their Physiological Function in a Bleached Mutant of Euglena gracilis z

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The streptomycin-bleached, non-photosynthetic mutant of Euglena gracilis contained NADH-glyoxylate reductase, NADPH-glyoxylate reductase, glutamate-glyoxylate aminotransferase and serine-glyoxylate aminotransferase, in addition to glycolate dehydrogenase. Most activities of NADH- and NADPH-glyoxylate reductases and 75% of glutamate-glyoxylate aminotransferase activity in the crude homogenate were recovered in mitochondria. The mutant cells grown under illumination contained three times as high glycolate dehydrogenase activity as the dark-grown cells. Illumination on the dark-grown cells caused an increase in activity to the level of the light-grown cells. Light at 420 nm wavelength was most effective for inducing the enzyme. The enzyme induced by illumination was the mitochondrial one and the specific activity increased 4-fold after illumination for 3 days; the rate of the increase was almost equal to the ratio of the rate of glycolate uptake from incubation mediumby the light-grown mutant to that of the dark-grown cells. However, there was no marked difference in the fate of carboxyl carbon of glycolate metabolized between the two types of cells. It is concluded from these results that mitochondrial glycolate dehydrogenase participates mainly in the glycolate metabolism in the bleached mutant. This is supported by experiments on the metabolism of glycolate in isolated, intact mitochondria of the mutant. The physiological significance of the formation and metabolism of glycolate in the non-photosynthetic mutant of Euglena was discussed.
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Occurrence and Subcellular Distribution of Enzymes Involved in the Glycolate Pathway and Their Physiological Function in a Bleached Mutant of Euglena gracilis z

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