Dehydrogenation of the phosphonate analogue of glucose 6-phosphate by glucose 6-phosphate dehydrogenase.

Dehydrogenation by gluconate 6-phosphate dehydrogenase of an isosteric phosphonate substrate analogue.

6,7-Dideoxy-D-gluco-heptonic-7-phosphonic acid, the isosteric phosphonate analogue of gluconate 6-phosphate, was prepared by incubation of the corresponding analogue of glucose 6-phosphate with glucose 6-phosphate dehydrogenase and NADP+ in the presence of an enzyme NADPH-NADP+ recycling system. The analogue of gluconate 6-phosphate is a substrate for yeast gluconate 6-phosphate dehydrogenase, ...

MOLECULAR IDENTIFICATION OF THE MOST PREVALENT MUTATION OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE (G6PD) GENE IN DEFICIENT PATIENTS IN GILAN PROVINCE

Glucose-6-Phosphate Dehydrogenase (G6PD) is a cytosolic enzyme which its main function is to produce NADPH in the red blood cells by controlling the step from Glucose-6-Phosphate to 6-Phospho gluconate in the pentose phosphate pathway. G6PD deficiency is the most common X-chromosome linked hereditary enzymopathy in the world, that result in reduced enzyme activity and more than 125 different mu...

Inhibition of Human Erythrocyte Glucose 6-Phosphate Dehydrogenase by Cadmium, Nickel and Aluminium

Evidence for the Essential Arginine and Histidine Residues in Catalytic Activity of Glucose 6-Phosphate Dehydrogenase from Streptomyces aureofaciens

Glucose 6-phosphate dehydrogenase (G6PD) was purified from Streptomyces aureofaciens and inactivated with butanedione and diethylpyrocarbonate. Incubation of the enzyme with butanedione resulted in a rapid activity loss (80%) within 5 min, followed by a slow phase using a molar ratio to enzyme concentration of 100. Fluorescence studies showed a conformational change in the butanedione-modified ...

REASSOCIATION AND REACTIVATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM STREPTOMYCES AUREOFACIENS AFTER DENATURATION BY 6 M UREA

Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...