Molybdoenzyme (Mo-enzyme) (Mo-enzyme)

Molybdoenzymes are a specialized class of metalloenzymes that utilize a molybdenum cofactor (MoCo) to catalyze essential redox reactions, primarily oxygen atom transfer (Hille et al., 2014, Chemical Reviews). In humans, this group consists of four characterized enzymes: xanthine oxidase (XO), sulfite oxidase (SO), aldehyde oxidase (AO), and the mitochondrial amidoxime reducing component (mARC) (Mendel, 2013, Molecules). These enzymes are vital for the catabolism of purines into uric acid, the detoxification of sulfites into sulfates, and the metabolism of various drugs and xenobiotics (StatPearls, 2023). Xanthine oxidase is a major therapeutic target, with inhibitors like allopurinol and febuxostat serving as the primary treatment for gout and hyperuricemia (PubMed, PMID: 29465380). Genetic deficiencies in the molybdenum cofactor lead to Molybdenum Cofactor Deficiency (MoCD), a devastating condition causing severe neurological damage and early death, which can now be treated with cofactor replacement therapy like fosdenopterin (NIH, GARD). Additionally, aldehyde oxidase plays a significant role in the clearance of many clinical drugs, making it a key consideration in modern drug design and safety (UniProt, P07858).

Other names

Molybdenum-containing enzymeMolybdopterin-containing enzymeMo-dependent enzyme

Inhibition of enzyme activity (e.g., xanthine oxidase inhibition) or replacement of essential cofactors (e.g., cyclic pyranopterin monophosphate).