Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus subtilis spores.
Glucose-6-phosphate dehydrogenase [D-glucose-6-phosphate: NADP oxidoreductase, EC. 1. 1. 1. 49] obtained from spores of Bacillus subtilis PCI 219 strain was partially purified by filtration on Sephadex G-200, ammonium sulfate fractionation and chromatography on DEAE-Sephadex A-25 (about 54-fold). The optimum pH for stability of this enzyme was about 6.3 and the optimum pH for the reaction about 8.3. The apparent Km values of the enzyme were 5.7 X 10(-4) M for glucose-6-phosphate and 2.4 X 10(-4) M for nicotinamide adenine dinucleotide phosphate (NADP). The isoelectric point was about pH 3.9. The enzyme activity was unaffected by the addition of Mg++ or Ca++. The inactive glucose-6-phosphate dehydrogenase obtained from the spores heated at 85 C for 30 min was not reactivated by the addition of ethylenediaminetetraacetic acid, dipicolinic acid or some salts unlike inactive glucose dehydrogenase.
D001412:Bacillus subtilis / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D009249:NADP / Q000378:metabolism; D010848:Picolinic Acids / Q000494:pharmacology; D013171:Spores, Bacterial / Q000201:enzymology
D008670:Metals; D010848:Picolinic Acids; D009249:NADP; D004492:Edetic Acid; D005954:Glucosephosphate Dehydrogenase