Carbohydrate and Metal Analyses of Violet-colored Acid Phosphatase of Sweet Potato |
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Authors: | Sadaki Fujimoto Akira Ohara Kihachiro Uehara |
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Affiliation: | 1. Laboratory of Biochemistry, Kyoto College of Pharmacy, Yamashina, Kyoto 607, Japan;2. Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565, Japan |
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Abstract: | Two malate dehydrogenases (MDH-M1 and MDH-M2) were found in a methanol-using yeast, Candida sp. N-16. MDH-M2 was induced with methanol. These enzymes were purified as electrophoretically and isoelectrophoretically homogeneous proteins. The molecular weights of MDH-M1 and MDH-M2 were estimated to be about 78,000 (homodimer) and 160,000 (homotetramer). Several kinetic properties were significantly different between the two enzymes. The value (2.07) of Vmax(oxaloacetate)/Vmax(malate) and Kcats (555 s-1 for oxaloacetate, 481 s-1 for NADH) of MDH-M2 were higher than the ratio (1.37) of Vmax and Kcats(241 s-1 for oxaloacetate, 271 s-1 for NADH) of MDH-M1, respectively. The activity of MDH-M2 was inhibited by a high concentration of NAD+ and the activity of MDH-M1 by oxaloacetate. |
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Keywords: | malate dehydrogenase methanol-using yeast Candida malate metabolism of methanol |
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