MOXD2 Inhibitors

Monooxygenase DBH-like 2 (MOXD2) inhibitors comprise a diverse group of chemical compounds that exert their inhibitory action by primarily targeting the copper ion binding activity essential for the enzymatic function of MOXD2. The inhibition of MOXD2 is achieved by decreasing the availability of copper ions, which are crucial cofactors for the enzyme's catalytic activity. Compounds such as disulfiram, tetrathiomolybdate, bathocuproine, D-penicillamine, and trientine directly chelate copper ions, lowering their bioavailability and thereby impeding MOXD2's ability to function properly.

The chemical class of MOXD2 inhibitors also includes compounds like ammonium tetrathiomolybdate, clioquinol, zinc acetate, neocuproine, and thiosemicarbazone, which similarly sequester copper ions from the physiological pool, preventing their utilization by MOXD2. Additionally, agents like methimazole and sodium diethyldithiocarbamate interfere with copper absorption or chelate copper, respectively, contributing to the inactivation of MOXD2. Each of these chemicals can bind to copper either within the cellular environment or in the gastrointestinal tract, reducing the concentration of free copper ions required for MOXD2 activity, leading to the inhibition of the protein's function. These inhibitors are characterized by their ability to form complexes with copper, thereby preventing its proper integration into the active site of MOXD2, and ensuring the enzyme remains inactive.