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Literature summary for 1.17.1.4 extracted from

  • Okamoto, K.; Matsumoto, K.; Hille, R.; Eger, B.T.; Pai, E.F.; Nishino, T.
    The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition (2004), Proc. Natl. Acad. Sci. USA, 101, 7931-7936.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitor FYX051, which is slowly hydroxylated by the enzyme Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
4-(5-pyridin-4-yl-1H-1,2,4-triazol-3-yl)pyridine-2-carbonitrile i.e. FYX-051, strong, in absence of xanthine slow hydroxylation of inhibitor Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P80457
-
-

Reaction

Reaction Comment Organism Reaction ID
xanthine + NAD+ + H2O = urate + NADH + H+ catalytically labile Mo-OH oxygen forms a bond with a carbon atom of substrate, the Mo=S group of the oxidized enzyme becomes protonated to afford Mo-SH on reduction of the molybdenum center Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
Bos taurus
-