molybdenum-cofactor has been researched along with Hyperuricemia* in 2 studies
1 review(s) available for molybdenum-cofactor and Hyperuricemia
| Article | Year |
|---|---|
Mechanistic insights into xanthine oxidoreductase from development studies of candidate drugs to treat hyperuricemia and gout.
Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco). Human XOR is considered to be a target of drugs not only for therapy of hyperuricemia and gout, but also potentially for a wide variety of other diseases. In this review, we focus on studies of XOR inhibitors and their implications for understanding the chemical nature and reaction mechanism of the Moco active site of XOR. We also discuss further experimental or clinical studies that would be helpful to clarify remaining issues. Topics: Catalytic Domain; Coenzymes; Enzyme Inhibitors; Gout; Humans; Hyperuricemia; Metalloproteins; Molybdenum Cofactors; Pteridines; Xanthine; Xanthine Dehydrogenase | 2015 |
1 other study(ies) available for molybdenum-cofactor and Hyperuricemia
| Article | Year |
|---|---|
Identification of novel xanthine oxidase inhibitors via virtual screening with enhanced characterization of molybdopterin binding groups.
Xanthine oxidase (XO) is an important therapeutic target for the treatment of hyperuricemia and gout. A virtual screening strategy with enhanced characterization of the molybdopterin binding group (MBG) was applied for the identification of novel XO inhibitors. Briefly, a 3D QSAR pharmacophore with fragment recognition capability was constructed by setting the MBG as a customized-pharmacophore feature. In addition, 2D QSAR was established with descriptors based on density functional theory (DFT), physical and chemical properties as well as topological properties. Descriptors related to metal ion recognition were emphasized to enhance the characterization of the MBG and to improve the screening efficiency. The 3D and 2D QSAR models were combined with the pharmacophore derived from XO-inhibitor complexes and docking with hydrogen bond constraints to screen the compound library of Specs. After two rounds of screening, six compounds with significant inhibition against XO were identified and the most active one XO-33 showed an IC Topics: Enzyme Inhibitors; Humans; Hyperuricemia; Molecular Docking Simulation; Molybdenum Cofactors; Quantitative Structure-Activity Relationship; Xanthine Oxidase | 2022 |