Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.1.4 highly active bovine XOR in its XDH form is soaked in a large excess of NADH under strictly anaerobic conditions in order to reduce both FAD cofactor and iron sulfur centers and to block any electron transfer from the Mo center. The Mo ions in the crystal are fully reduced by soaking in 4 mM titanium citrate solution followed by 0.25 mM urate, crystal structure determination and analysis, superimposition, modelling Bos taurus
1.17.1.4 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
1.17.3.2 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
1.17.3.2 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.3.2 extracellular
-
Bos taurus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.1.4 Iron two [2Fe-2S] centers Bos taurus
1.17.1.4 Iron two [2Fe-2S] centers Rattus norvegicus
1.17.1.4 Molybdenum XOR is a molybdenum-containing enzyme, cofactor geometry, overview Bos taurus
1.17.1.4 Molybdenum XOR is a molybdenum-containing enzyme, cofactor geometry, overview Rattus norvegicus
1.17.3.2 Iron two [2Fe-2S] centers Bos taurus
1.17.3.2 Iron two [2Fe-2S] centers Rattus norvegicus
1.17.3.2 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
1.17.3.2 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Bos taurus
-
-
-
1.17.1.4 Rattus norvegicus P22985 cf. EC 1.17.3.2
-
1.17.3.2 Bos taurus
-
-
-
1.17.3.2 Rattus norvegicus P22985
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.4 highly active bovine XOR in its XDH form is prepared by folate affinity chromatography Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.17.1.4 xanthine + NAD+ + H2O = urate + NADH + H+ 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
1.17.1.4 xanthine + NAD+ + H2O = urate + NADH + H+ 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
1.17.3.2 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
1.17.3.2 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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.1.4 milk
-
Bos taurus
-
1.17.3.2 milk
-
Bos taurus
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.17.1.4 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 Bos taurus
1.17.1.4 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
1.17.1.4 XDH
-
Bos taurus
1.17.1.4 XDH
-
Rattus norvegicus
1.17.1.4 XOR
-
Bos taurus
1.17.1.4 XOR
-
Rattus norvegicus
1.17.3.2 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
1.17.3.2 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
1.17.3.2 xanthine oxidoreductase
-
Bos taurus
1.17.3.2 xanthine oxidoreductase
-
Rattus norvegicus
1.17.3.2 XOR
-
Bos taurus
1.17.3.2 XOR
-
Rattus norvegicus

Cofactor

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

General Information

EC Number General Information Comment Organism
1.17.1.4 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 Bos taurus
1.17.1.4 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
1.17.3.2 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
1.17.3.2 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