Activating Compound | Comment | Organism | Structure |
---|---|---|---|
sulfide/dithionite | treatment increases the specific activity of AtXDH1 | Arabidopsis thaliana |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged XDH1 in Pichia pastoris | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
allopurinol | - |
Arabidopsis thaliana | |
additional information | NAD+ and diphenylene iodonium inhibit NADH-dependent superoxide formation of AtXDH1; NAD+ inhibits NADH-dependent superoxide formation of AtXDH1 | Arabidopsis thaliana |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | a molybdenum-iron-flavoenzyme | Arabidopsis thaliana | |
Mo | a molybdenum-iron-flavoenzyme | Arabidopsis thaliana |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Arabidopsis thaliana | XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% | ? | - |
? | |
additional information | Arabidopsis thaliana | XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% | ? | - |
? | |
xanthine + O2 + H2O | Arabidopsis thaliana | - |
urate + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
flavoprotein | - |
Arabidopsis thaliana |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography | Arabidopsis thaliana |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.044 | - |
purified recombinant enzyme, substrate xanthine, pH 8.0 | Arabidopsis thaliana |
0.702 | - |
purified recombinant enzyme, substrate NADH, pH 6.6 | Arabidopsis thaliana |
1.712 | - |
purified recombinant enzyme, in presence of sulfide/dithionite | Arabidopsis thaliana |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% | Arabidopsis thaliana | ? | - |
? | |
additional information | XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% | Arabidopsis thaliana | ? | - |
? | |
additional information | AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved | Arabidopsis thaliana | ? | - |
? | |
additional information | AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved | Arabidopsis thaliana | ? | - |
? | |
xanthine + O2 + H2O | - |
Arabidopsis thaliana | urate + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa | Arabidopsis thaliana |
Synonyms | Comment | Organism |
---|---|---|
xanthine oxidoreductase | - |
Arabidopsis thaliana |
XOR | - |
Arabidopsis thaliana |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Arabidopsis thaliana |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.6 | - |
substrate NADH | Arabidopsis thaliana |
8 | - |
substrate xanthine | Arabidopsis thaliana |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.6 | 8 | - |
Arabidopsis thaliana |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | a molybdenum-iron-flavoenzyme | Arabidopsis thaliana | |
molybdenum cofactor | C-terminal | Arabidopsis thaliana | |
additional information | negligible reactivity toward NAD+ | Arabidopsis thaliana | |
[2Fe-2S] cluster | two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type | Arabidopsis thaliana |
General Information | Comment | Organism |
---|---|---|
physiological function | xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid | Arabidopsis thaliana |