6-Phosphogluconic Dehydrogenase from yeast has been used in hexokinase (HK) and xylose reductase (XR) activities in cell lysate.
6-Phosphogluconic Dehydrogenase from yeast comprises of a NADP+ binding domain, α helical hydrophobic interaction domain and a C-terminal domain. It exists as dimer and the C-terminal region is crucial for the substrate binding and release.
Enzyme activity is determined by measuring the reduction of NAD+ or NADP+. High levels of NADPH are believed to inhibit the enzyme, while 6-phosphogluconate acts to activate the enzyme.
