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Literature summary for 1.17.3.2 extracted from

  • Cao, H.; Pauff, J.; Hille, R.
    Substrate orientation and the origin of catalytic power in xanthine oxidoreductase (2011), Indian J. Chem., 50A, 355-362.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determination and analysis of the enzyme in complex with a variety of substrates and substrate analogues, e.g. with 2-hydroxy-6-methylpurine or hypoxanthine, X-ray diffraction structure analysis at 1.8-3.1 A resolution Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
alloxanthine a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in a [Fe2-S2] domain Bos taurus
Molybdenum the molybdenum center is a pyranopterin-MoVI-OS-OH. The pyranopterin cofactor is coordinated to the metall via an enedithiolate side chain, coordination geometry, overview Bos taurus
additional information the molybdenum center is located in a separate subunit from the Fe/S- and flavin-containing parts of the enzyme Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
295000
-
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
xanthine + H2O + O2 = urate + H2O2 reaction mechanism, detailed overview. The reaction is initiated by proton abstraction from the Mo-OH group by Glu1261, the active-site base, followed by nucleophilic attack on the carbon to be hydroxylated, and hydride transfer to the Mo-S double bond. Suitable substrate orientation, overview. Arg880 is involved in stablizing the transition state in the course of nucleophilic attack, overview Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information role of Glu802 is facilitating the tautomerization of hypoxanthine in the course of hydroxylation by the enzyme, substrate binding structures, overview Bos taurus ?
-
?
additional information xanthine and lumazine are good substrates, while 2-hydroxy-6-methylpurine is a slow and poor substrate Bos taurus ?
-
?

Subunits

Subunits Comment Organism
homodimer alpha2, with four redox-active centers in each subunit laid out in discretely folding domains, structure, overview Bos taurus

Synonyms

Synonyms Comment Organism
xanthine oxidoreductase
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Bos taurus
additional information the molybdenum center is located in a separate subunit from the Fe/S- and flavin-containing parts of the enzyme Bos taurus

General Information

General Information Comment Organism
additional information active site structure, overview Bos taurus
physiological function xanthine oxidase functions not only to hydroxylate xanthine at C-8 to give uric acid, but also hypoxanthine at C-2 to give xanthine in the immediate preceding step of purine catabolism Bos taurus