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
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uric
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1.2.1.37
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1.1.1.204
- allopurinol
- environmental protection
-
ureide
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1.1.3.22
- medicine
-
1.2.3.1
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xanthinuria
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oxypurines
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butyrophilins
- synthesis
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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 (Cofactor
Cofactor on EC 1.17.1.4 - xanthine dehydrogenase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
molybdopterin cytosine dinucleotide
localized in subunit PaoC
[4Fe-4S]-center
cluster is anchored to an additional 40 residues subdomain of subunit PaoB
FAD
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trypsin-treated oxidase type O shows absence of FAD, heat-treated oxidase type O shows small measurable FAD
FAD
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substitutions G348E, G353D, S357F located within the flavin/NAD+/NADH-domain
FAD
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deflavo-enzyme completely loses xanthine/NAD+ activity, no loss of xanthine/2,6-dichorophenolindophenol activity, xanthine dehydrogenase form stabilizes the neutral form of flavin, xanthine oxidase form does not
FAD
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the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview
FAD
a molybdenum-iron-flavoenzyme, activity-to-flavin ratio of 8 with xanthine as substrate and NAD+ as final electron acceptor, recombinant enzyme
FAD
subunit PaoB exhibits a typical FAD binding motif
molybdenum cofactor
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the enzyme contains molybdenum cofactor comprising only molybdopterin and molybdenum
molybdenum cofactor
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binding involves residues GluB730, GlnA102, CysA103, CysA106, CysA134, and CysA13 of the alpha and beta subunits
molybdenum cofactor
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structure-function analysis, mechanism, overview
molybdenum cofactor
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
molybdenum cofactor
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MoCo, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups
molybdopterin
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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
molybdopterin
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in the crystal structure of reduced enzyme in complex with oxipurinol at 2.0 A resolution, electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor
NAD+
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NADH
crystal structures of the NAD(H) complexes of XDH reveal that, given the proper oxidation states, the nicotinamide rings of the dinucleotides locate at van der Waals distance to the flavin ring
[2Fe-2S] cluster
two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type
[2Fe-2S]-center
iron-sulfur subunit PaoA can be divided into two subdomains, each carrying one [2Fe-2S] cluster
[2Fe-2S]-center
two nonidentical [2Fe-2S] clusters designated as Fe/SI and Fe/SII, distinguished by redox potential and EPR signal
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
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XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
[2Fe-2S]-center
protein contains 2 2Fe-2S iron-sulfur-cluster-binding domains
additional information
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molybdoironflavoprotein: molar ratio of molybdenum to iron to acid-labile-sulfur to FAD is 1 : 2 : 1.9 : 0.8
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additional information
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molybdoironflavoprotein: 17.5 mol iron, 18.4 mol acid-labile sulfur, 2.3 mol molybdenum, 1.1 mol tungsten, 0.95 mol selenium
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additional information
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molybdoironflavoprotein: ratio of non-heme iron to acid-labile sulfur to FAD to molybdenum to tungsten to selenium is 7.7 : 7.5 : 1.7 : 1.8 : 0.12 : 0.13
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additional information
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molybdoironflavoprotein: 8 : 8 : 2 : 1.5 ratio of iron to sulfide to flavin to molybdenum
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additional information
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molar ratio of FAD to iron to labile sulfide per mol enzyme is 2 : 14 : 2
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additional information
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one molybdopterin-cofactor, two Fe2-S2-cluster, one FAD per subunit
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additional information
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molybdoironflavoprotein: 1 : 1 : 4 ratio of molybdenum to FAD to iron
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additional information
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molybdoironflavoprotein: ratio of iron to FAD to molybdenum is 4 : 1 : 1
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additional information
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cofactor compostion similar to eukaryotic enzymes
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additional information
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molybdoironflavoprotein: ratio of 2 : 1.4 : 7.6 of FAD to molybdenum to Fe-S
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additional information
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both NAD+ and NADH compete for the same binding site
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additional information
both NAD+ and NADH compete for the same binding site
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additional information
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cofactor conformation, binding structure analysis and mechanism, overview
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additional information
cofactor conformation, binding structure analysis and mechanism, overview
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additional information
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cofactor domain amino acid sequence comparisons, overview
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additional information
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cofactor domain amino acid sequence comparisons, overview
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species
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additional information
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cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species. Rhodobacter capsulatus alpha2beta2 XDH arranges the FAD and [2Fe-2S] domains and the Moco domain into 2 separate subunits
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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
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