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Literature summary extracted from

  • Schopfer, L.M.; Massey, V.; Nishino, T.
    Rapid reaction studies on the reduction and oxidation of chicken liver xanthine dehydrogenase by the xanthine/urate and NAD/NADH couples (1988), J. Biol. Chem., 263, 13528-13538.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.1.4 Iron-sulfur-center
-
 Gallus gallus
1.17.1.4 molybdenum-center urate, xanthine and 8-bromoxanthine interact with the molybdenum-site of fully reduced xanthine oxidase Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.4 xanthine + NAD+ + H2O Gallus gallus xanthine dehydrogenase can be partially reduced in a triphasic reaction by either xanthine or NADH, oxidation of fully, 6-electron-reduced xanthine dehydrogenase by either urate or NAD+ is monophasic and depends on the oxidant concentration urate + NADH NADH-binding to the 2-electron reduced enzyme is implicated in fixing end-point position in reactions involving pyridine nucleotides, urate-binding is involved in fixing end-point reactions involving xanthine and urate r

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Gallus gallus
-
 chicken
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.1.4 liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.4 xanthine + NAD+ + H2O xanthine dehydrogenase can be partially reduced in a triphasic reaction by either xanthine or NADH, oxidation of fully, 6-electron-reduced xanthine dehydrogenase by either urate or NAD+ is monophasic and depends on the oxidant concentration Gallus gallus urate + NADH NADH-binding to the 2-electron reduced enzyme is implicated in fixing end-point position in reactions involving pyridine nucleotides, urate-binding is involved in fixing end-point reactions involving xanthine and urate r

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.4 FAD generally viewed as the site at which NADH reacts Gallus gallus
1.17.1.4 NAD+
-
 Gallus gallus
1.17.1.4 NADH
-
 Gallus gallus