EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.17.3.2 | Molybdenum | the enzyme accelerates reaction rate via base-catalyzed chemistry in which a Mo-OH group undertakes nucleophilic attack on the carbon center to be hydroxylated, with concomitant hydride transfer to a catalytically essential Mo=S group in the molybdenum coordination sphere. This chemistry appears to proceed via obligate two-electron chemistry rather than in individual steps to yield a reduced enzyme product complex with product coordinmated to the active site molybdenum by means of the newly introduced hydroxyl group in a sinple end-on fashion | Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.3.2 | Bos taurus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.17.3.2 | milk | - |
Bos taurus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.3.2 | 1,3-dimethylxanthine + H2O + O2 | - |
Bos taurus | 1,3-dimethylurate + H2O2 | - |
? | |
1.17.3.2 | 1,7-dimethylxanthine + H2O + O2 | - |
Bos taurus | 1,7-dimethylurate + H2o2 | - |
? | |
1.17.3.2 | 1-methylxanthine + H2O + O2 | - |
Bos taurus | 1-methylurate + H2O2 | - |
? | |
1.17.3.2 | 2,6-diaminopurine + H2O + O2 | - |
Bos taurus | 2,6-diamino-7,9-dihydro-8H-purin-8-one | - |
? | |
1.17.3.2 | 2-amino-6-chloro-purine + H2O + O2 | - |
Bos taurus | 2-amino-6-chloro-7,9-dihydro-purin-8-one + H2O2 | - |
? | |
1.17.3.2 | 2-thioxanthine + H2O + O2 | - |
Bos taurus | 2-thiourate + H2O2 | - |
? | |
1.17.3.2 | 3-methylxanthine + H2O + O2 | - |
Bos taurus | 3-methylurate + H2O2 | - |
? | |
1.17.3.2 | 6-thioxanthine + H2O + O2 | - |
Bos taurus | 6-thiourate + H2O2 | - |
? | |
1.17.3.2 | 7-methylxanthine + H2O + O2 | - |
Bos taurus | 7-methylurate + H2O2 | - |
? | |
1.17.3.2 | guanine + H2O + O2 | - |
Bos taurus | 2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | the enzyme accelerates reaction rate via base-catalyzed chemistry in which a Mo-OH group undertakes nucleophilic attack on the carbon center to be hydroxylated, with concomitant hydride transfer to a catalytically essential Mo=S group in the molybdenum coordination sphere. This chemistry appears to proceed via obligate two-electron chemistry rather than in individual steps to yield a reduced enzyme product complex with product coordinmated to the active site molybdenum by means of the newly introduced hydroxyl group in a sinple end-on fashion. Product displacement by hydroxide and electron transfer to other redox-active centers in the enzyme complete the catalytic sequence | Bos taurus | uric acid + H2O2 | - |
? |