Glucose-6-phosphate Dehydrogenase from baker′s yeast (S. cerevisiae)

Glucose-6-phosphate dehydrogenase is used:

• To test ketose reductase activity in developing maize endosperm.
• For recycling microassay of β-NADP and β-NADPH.
• To measure the intracellular levels of NADPH and total NADP.
• To measure the nicotinamide adenine dinucleotide (NAD) kinase kinetic assay activity.

Glucose-6-phosphate dehydrogenase catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway.

Glucose-6-phosphate dehydrogenase catalyzes the rate-limiting step in the pentose phosphate pathway. Its function involves the conversion of glucose-6-phosphate to 6-phosphogluconolacetone while generating NADPH, which is essential for the regeneration of glutathione The glutathione system utilizes nicotinamide adenine dinucleotide phosphate hydrogen (NADPH) to effectively eliminate excess hydrogen peroxide. Glucose-6-phosphate dehydrogenase (G6PD) plays an important role in regulating cell growth and survival. Their levels are higher in cells undergoing normal and neoplastic growth. Increased glucose-6-phosphate dehydrogenase activity plays a pivotal role in preventing reactive oxygen species mediated cell death. Glucose-6-phosphate dehydrogenase is over expressed in several cancers whereas its activity is reduced in hyperglycemia. A deficiency in glucose-6-phosphate dehydrogenase causes hemolysis.

Research area: Cell Signaling

Glucose-6-phosphate dehydrogenase (G6PD) is a key metabolic enzyme of the pentose phosphate pathway. In S. cerevisiae, it is encoded by the ZWF1 gene. G6PD exists as a tetramer in its active form.

One unit will oxidize 1.0 μmole of D-glucose 6-phosphate to 6-phospho-D-gluconate per min in the presence of NADP at pH 7.4 at 25 °C.

Lyophilized powder essentially sulfate-free, containing approx. 20% sodium citrate