G6pd2 Inhibitors

G6pd2 inhibitors are a class of chemical compounds that can inhibit the activity of G6pd2, an isoform of the enzyme glucose-6-phosphate dehydrogenase. This enzyme plays a critical role in the pentose phosphate pathway, which is essential for producing NADPH, a key molecule in maintaining the redox balance of the cell and in biosynthetic reactions. Inhibition of G6pd2 can lead to altered cellular redox states and reduced availability of NADPH, which can affect various cell processes dependent on these factors.

The chemicals listed act through diverse mechanisms to inhibit the function of the enzyme. Compounds like DHEA and 6-Aminonicotinamide act as competitive inhibitors by occupying the NADP+ binding site, preventing the normal binding and function of the enzyme. Polyphenols such as EGCG, quercetin, apigenin, and chrysin can intercalate into the enzyme or otherwise bind to it, disrupting its normal function. Oxidized glutathione affects enzyme activity by forming a bond with the enzyme, while compounds such as hydroxychloroquine and methylene blue can affect the enzyme's activity indirectly through effects on the cellular redox state. Menadione and emodin work by redox cycling, which leads to the depletion of NADPH, thus reducing G6pd2 activity.