1.17.1.4: xanthine dehydrogenase
This is an abbreviated version!
For detailed information about xanthine dehydrogenase, go to the full flat file.
Word Map on EC 1.17.1.4
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1.17.1.4
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uric
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1.2.1.37
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1.1.1.204
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allopurinol
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environmental protection
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ureide
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1.1.3.22
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medicine
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1.2.3.1
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xanthinuria
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oxypurines
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butyrophilins
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synthesis
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hypouricemic
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agriculture
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biotechnology
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analysis
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nutrition
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molecular biology
- 1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
- synthesis
-
hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
Reaction
Synonyms
AtXDH1, EC 1.1.1.204, EC 1.2.1.37, IAO1, More, NAD-xanthine dehydrogenase, PaoABC, Retinol dehydrogenase, Rosy locus protein, VvXDH, xanthine dehydrogenase, xanthine dehydrogenase-1, xanthine dehydrogenase-2, xanthine dehydrogenase/oxidase, xanthine oxidoreductase, xanthine-NAD oxidoreductase, xanthine/NAD+ oxidoreductase, xanthine:NAD+ oxidoreductase, XDH, XDH/XO, XDH1, XDH2, XdhC, XOR, YagR, YagS, YagT
ECTree
1.17.1.4 xanthine dehydrogenaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 1.17.1.4 - xanthine dehydrogenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Fe
Fe2+
Iron
Iron-sulfur-center
Mo
Molybdenum
molybdenum-center
Se
selenium
Tungsten
additional information
the purified wild-type XDH contains 2.80 iron, 0.94 FAD, and 0.72 Moco per (alphabeta)2 tetrameric subunit, Split178 has 2.73 iron, 0.95 FAD, and 0.70 Moco per (alphabetagamma)2 hexameric subunit, while Split166 incorporates 3.51 iron, 0.95 FAD, and 0.95 Moco per (alphabetagamma)2 hexamer
Fe
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non-heme iron-sulfur groups, 7.7 g-atom Fe, 7.5 g- atom S2- per mol enzyme
Iron
enzyme is about 30% deficient in iron-sulfur centers on basis of UV/vis and CD spectra
Iron
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FeS center, EPR spectra, wild type 3.7 mol per subunit, active form of mutant R135C 2.8 mol per subunit, inactive form of mutant R135C 1.2 mol per subunit
Iron
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the enzyme is a molybdo-flavoprotein, the enzyme tetramer contains two [2Fe-2S] clusters
Iron-sulfur-center
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2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain
Iron-sulfur-center
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substitutions G42E, E89K, L127F located within the iron-sulfur domain
Molybdenum
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superoxide production depends on sulfuration of molybdenum cofactor
Molybdenum
a molybdenum-iron-flavo enzyme, which contains a C-terminal molybdenum cofactor-binding domain of 85 kDa
Molybdenum
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Molybdenum
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in milk, more than 90% of enzyme exists in the inactive demolybdo form
Molybdenum
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1.1 atoms per alphabeta protomer in wild-type, 0.89 atoms per alphabeta protomer after expression of xdhABC genes, 0.24 atoms per alphabeta protomer after expression of xdhAB genes
Molybdenum
molybdopterin-cytosine-dinucleotide localized in subunit PaoC
Molybdenum
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the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
Molybdenum
XOR is a molybdenum-containing enzyme, cofactor geometry, overview
Molybdenum
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active form of mutant R135C Moco content 97%, inactive form of mutant R135C Moco content 3.8%
Molybdenum
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protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor
Molybdenum
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the enzyme is molybdo-flavoprotein, one cofactor molecule per enzyme tetramer
Molybdenum
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in the molybdenum cofactor, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups. Oxidized wild-type and mutant Q179A reveal a similar Mo(VI) ion with each one molybdopterin, Mo=O, Mo-O-, and Mo=S ligand, and a weak Mo-O(E730) bond at alkaline pH
Molybdenum
molybdenum-containing flavoenzyme, in the molybdenum cofactor (Moco)
Molybdenum
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superoxide production depends on sulfuration of molybdenum cofactor
molybdenum-center
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contains molybdopterin mononucleotide rather than molybdopterin dinucleotide
molybdenum-center
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substitutions G800E, G1011E, G1164R, G1266D, S1275F located within the pterin molybdenum cofactor domain
molybdenum-center
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urate, xanthine and 8-bromoxanthine interact with the molybdenum-site of fully reduced xanthine oxidase
