Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides (C15-1289-881)

General description

Glucose-6-phosphate Dehydrogenase (G6PD) from Leuconostoc mesenteroides catalyzes the oxidation of glucose 6-phosphate in the presence of nicotinamide adenine dinucleotide (NAD⁺) or nicotinamide adenine dinucleotide phosphate (NADP⁺). It corresponds to a molecular weight of 54 kDa and exists as a homodimer.

Application

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides has been used:

• as a component of reaction mixture for assaying mannose- and glucose-6-phosphate activity
• as a component of reaction mixture in the nevirapine inhibition studies in human hepatic microsomes
• in the glucose-phosphorylating activity of chloroplast extracts

Glucose-6-phosphate dehydrogenase was used as a model to test the effect of seed protein fractions on enzyme protection during dehydration. G-6-PDH has been utilized in assays for nicotinamide adenine dinucleotide and tissue pyridine nucleotides.

Biochem/physiol Actions

Glucose-6-phosphate dehydrogenase (G6PD) 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 conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway<<<17>>>.

Lysine 21 in the Glucose-6-phosphate Dehydrogenase (G6PD) is crucial for binding NAD⁺. G6PD uses NAD⁺ or NADP⁺ based on the catabolic or anabolic metabolic pathway.

Unit Definition

One unit will oxidize 1.0 μmole of D-glucose 6-phosphate to 6-phospho-D-gluconate per min in the presence of NAD at pH 7.8 at 30 °C.

Physical form

Suspension in 2.7 M (NH₄)₂SO₄ solution containing 42 mM Tris and 0.8 mM MgCl₂