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Literature summary for 1.17.3.2 extracted from

  • Choi, E.Y.; Stockert, A.L.; Leimkuhler, S.; Hille, R.
    Studies on the mechanism of action of xanthine oxidase (2004), J. Inorg. Biochem., 98, 841-848.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,3-dimethylxanthine + H2O + O2
-
Bos taurus 1,3-dimethylurate + H2O2
-
?
1,7-dimethylxanthine + H2O + O2
-
Bos taurus 1,7-dimethylurate + H2o2
-
?
1-methylxanthine + H2O + O2
-
Bos taurus 1-methylurate + H2O2
-
?
2,6-diaminopurine + H2O + O2
-
Bos taurus 2,6-diamino-7,9-dihydro-8H-purin-8-one
-
?
2-amino-6-chloro-purine + H2O + O2
-
Bos taurus 2-amino-6-chloro-7,9-dihydro-purin-8-one + H2O2
-
?
2-thioxanthine + H2O + O2
-
Bos taurus 2-thiourate + H2O2
-
?
3-methylxanthine + H2O + O2
-
Bos taurus 3-methylurate + H2O2
-
?
6-thioxanthine + H2O + O2
-
Bos taurus 6-thiourate + H2O2
-
?
7-methylxanthine + H2O + O2
-
Bos taurus 7-methylurate + H2O2
-
?
guanine + H2O + O2
-
Bos taurus 2-amino-7,9-dihydro-1H-purine-6,8-dione + H2O2
-
?
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
-
?