Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii.
Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, EC 1.1.1.44) were purified approx. 1700 fold and 330 fold, respectively, from Candida boidinii grown on methanol. The final enzyme preparations were homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weights of the enzymes were estimated to be 118 000 and 110 000, respectively. Both enzymes are composed of two probably identical subunits and the molecular weights of the polypeptide chains were calculated to be 61 000 and 58 000, respectively. From a consideration of enzyme activities and types of inhibition by different metabolites the role of these two enzymes in glucose- and methanol-metabolism is discussed.
D002175:Candida / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000432:Methanol / Q000378:metabolism*; D009249:NADP / Q000494:pharmacology; D010734:Phosphogluconate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*
D009249:NADP; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D005947:Glucose; D000432:Methanol