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Literature summary for 1.17.3.2 extracted from

  • Okamoto, K.; Kawaguchi, Y.; Eger, B.; Pai, E.; Nishino, T.
    Crystal structures of urate bound form of xanthine oxidoreductase: Substrate orientation and structure of the key reaction intermediate (2010), J. Am. Chem. Soc., 132, 17080-17083.
    View publication on PubMed
Search for more literature for 1.17.3.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution Bos taurus
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron two [2Fe-2S] centers Bos taurus
Iron two [2Fe-2S] centers Rattus norvegicus
Molybdenum XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions, in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview Rattus norvegicus
Molybdenum XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions,3a in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxanthine + 2 H2O + 2 O2 Bos taurus
-
 urate + 2 H2O2
-
 ?
hypoxanthine + 2 H2O + 2 O2 Rattus norvegicus
-
 urate + 2 H2O2
-
 ?
xanthine + H2O + O2 Bos taurus catalytically relevant binding mode of the substrate xanthine, overview urate + H2O2
-
 ?
xanthine + H2O + O2 Rattus norvegicus catalytically relevant binding mode of the substrate xanthine, overview urate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Rattus norvegicus P22985
-
-

Reaction

Reaction Comment Organism Reaction ID
xanthine + H2O + O2 = urate + H2O2 reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur Bos taurus
a
xanthine + H2O + O2 = urate + H2O2 reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + 2 H2O + 2 O2
-
 Bos taurus urate + 2 H2O2
-
 ?
hypoxanthine + 2 H2O + 2 O2
-
 Rattus norvegicus urate + 2 H2O2
-
 ?
xanthine + H2O + O2 catalytically relevant binding mode of the substrate xanthine, overview Bos taurus urate + H2O2
-
 ?
xanthine + H2O + O2 catalytically relevant binding mode of the substrate xanthine, overview Rattus norvegicus urate + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
More XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 Rattus norvegicus
More XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 Bos taurus
xanthine oxidoreductase
-
 Bos taurus
xanthine oxidoreductase
-
 Rattus norvegicus
XOR
-
 Bos taurus
XOR
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Bos taurus
FAD role of Asp428 in the FAD reactivity, overview Rattus norvegicus
molybdenum cofactor cofactor geometry, overview Bos taurus
molybdenum cofactor cofactor geometry, overview Rattus norvegicus
additional information cofactor conformation, binding structure analysis and mechanism, overview Bos taurus
additional information cofactor conformation, binding structure analysis and mechanism, overview Rattus norvegicus

General Information

General Information Comment Organism
additional information XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 Rattus norvegicus
additional information XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 Bos taurus