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| Product | Description | |
|---|---|---|
| enzyme-thiol transhydrogenase (glutathione-disulfide) | Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents. Group: Enzymes. Synonyms: [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Enzyme Commission Number: EC 1.8.4.7. CAS No. 85030-79-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1673; enzyme-thiol transhydrogenase (glutathione-disulfide); EC 1.8.4.7; 85030-79-1; [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Cat No: EXWM-1673. |  |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| xanthine oxidase | An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: hypoxanthine o. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1088; xanthine oxidase; EC 1.17.3.2; 9002-17-9; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: EXWM-1088. | |
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