A genetic variant of human erythrocyte glucose 6-phosphate dehydrogenase

Abstract

Human erythrocyte G6PD activity was measured in more than 500 subjects in Isfahan, Iran, and the percent of enzyme deficiency for males and femals are reported. Some properties of the abnormal enzyme is compared with its normal counterpart. Apparent K m values of glucose 6-phosphate for the variant and normal enzymes were 37 and 101 μM, respectively. The variant enzyme was less resistant to inhibition by 40 μM NADPH (72% inhibition) than the normal enzyme (48% inhibition). The mode of inhibition for both enzymes was competitive with NADP +. ATP at 1.5 mM concentration also inhibited normal and variant enzymes at 17% and 10%, respectively. The inhibition was competitive with glucose 6-phosphate. Polyacrylamide gel electrophores showed that normal enzyme has one major and another weak active bands, while the variant enzyme under identical conditions shows only one active band corresponding to the major band of the normal enzyme. Thermostability of variant G6PD was slightly lower that normal but no significant differences observed in their energy of activation. The activity pH profile of the variant enzyme was truncate.