Purification and Properties of Two Malate Dehydrogenases from Candida sp. N-16 Grown on Methanol(Microbiology & Fermentation Technology)

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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 V_<max(oxaloacetate)>/V_<max(malate)> and K_<cat>s (555 s^<-1> for oxaloacetate, 481 s^<-1> for NADH) of MDH-M2 were higher than the ratio (1.37) of V_<max> and K_<cat>s (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.
社団法人日本農芸化学会の論文
2001-07-23