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Information on EC 1.17.1.4 - xanthine dehydrogenase and Organism(s) Rattus norvegicus and UniProt Accession P22985

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EC Tree
     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.1 With NAD+ or NADP+ as acceptor
                1.17.1.4 xanthine dehydrogenase
IUBMB Comments
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein . The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
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Rattus norvegicus
UNIPROT: P22985
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine/nad+ oxidoreductase, xanthine dehydrogenase-1, xanthine-nad oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
xanthine dehydrogenase/oxidase
UniProt
xanthine oxidoreductase
-
NAD-xanthine dehydrogenase
-
-
-
-
Rosy locus protein
-
-
-
-
xanthine oxidoreductase
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
xanthine:NAD+ oxidoreductase
-
-
XDH/XO
-
-
-
-
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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
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
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
mechanism of conversion of dehydrogenase form to oxidase form
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
xanthine:NAD+ oxidoreductase
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
CAS REGISTRY NUMBER
COMMENTARY hide
9054-84-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
NADH + O2 + H+
NAD+ + O2- + H2O2
show the reaction diagram
-
xanthine dehydrogenase catalyzes NADH oxidation leading to the formation of one O2- radical and half a H2O2 molecule, at rates three times those observed for xanthine oxidase. NADH efficiently oxidizes xanthine dehydrogenase, but only a great excess of NADH reduces xanthine oxidase
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hypoxanthine + 2 NAD+ + 2 H2O
urate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin
[2Fe-2S]-center
two nonidentical [2Fe-2S] clusters designated as Fe/SI and Fe/SII, distinguished by redox potential and EPR signal
molybdenum cofactor
[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])
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
two [2Fe-2S] centers
Molybdenum
Fe2+
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in the [2Fe-2S] center
Mo
-
XOR is a molybdenum-containing enzyme
Molybdenum
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a molybdenum-containing flavoprotein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenine
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presence of adenine in liver extracts causes a 45-60% decrease in xanthine oxidase and in xanthine oxidase plus xanthine dehydrogenase activities, removal by dialysis results in recovery of both activities to almost pre-treatment levels
allopurinol
ammonium acetate
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inhibits the enzyme in vivo after injection into the brain, blocked by MK-801, which alone does not affect the enzyme activity itself
FYX-051
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i.e. 4-(5-pyridin-4-yl-1H-[1, 2, 4]triazol-3-yl)pyridine-2-carbonitrile, a xanthine oxidoreductase inhibitor, that causes xanthine-mediated nephropathy inrats, but not in monkeys, toxicity study, overview
Guanidine-HCl
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conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
hesperetin
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i.e. 3',5,7-trihydroxy-4'-methoxyflavanone, major flavanone component of orange juice, inhibits hepatic XDH activity and decreases serum uric acid levels, exhibits antioxidative and antihyperuricemic properties
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PD98059
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inhibitor used to block MEK-1/2 kinase, activates the promoter of xanthine oxidoreductase and significantly enhances expression of enzyme induced by insulin, acute phase cytokines, or growth factors
sodium nitroprusside
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i.e. SNP, a NO donor, activates at concentrations of up to 3 mM, preventable by hemoglobin, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052
NAD+
DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C
additional information
additional information
steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
serum uric acid levels in healthy and hypeuricemic rats, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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lung epithelial cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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parenchymal cells, dehydrogenase activity
Manually annotated by BRENDA team
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matrix and core, of parenchymal cells, both oxidase and dehydrogenase activity
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mammalian xanthine oxidoreductase can exist in both dehydrogenase and oxidase forms. The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase. Conversion between the two is implicated in such diverse processes as lactation, anti-bacterial activity, reperfusion injury and a growing number of diseases. The dehydrogenase-oxidase transformation occurs rather readily and the insertion of the C-terminal peptide into the active site cavity of its subunit stabilizes the dehydrogenase form. The intermediate form can be generated (e.g. in endothelial cells) upon interaction of the C-terminal peptide portion of the enzyme with other proteins or the cell membrane. Residues Cys535 and Cys992 are involved in the rapid phase and Cys1316 and Cys1324 in the slow phase of the modification reaction. The irreversible conversion of XDH to XOR by trypsin involves limited proteolysis at the same linker peptide. Triggering events, such as the formation of a disulfide bond between Cys535 and Cys992 or proteolysis of the linker, reorient Phe549 (also a part of the long linker), resulting in disruption of a four amino acid cluster. Arg426 is then released from the cluster and moves the A-loop that blocks the approach of NAD+ to the flavin ring of the FAD moiety, as well as changing the electrostatic environment
evolution
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XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
malfunction
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potassium oxonate-induced hyperuricemia can be reduced by oral application of onions reducing serum uric acid levels in hyperuricemic rats. The compound probably does not act via simple enzyme inhibition mechanism
metabolism
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xanthine dehydrogenase is an enzyme form of the xanthine dehydrogenase/oxidase enzyme, XDH, complex, that catalyzes the end step in the purine catabolic pathway and is directly involved in depletion of the adenylate pool in the cell
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XDH_RAT
1331
0
146243
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 150000, about, C-terminally truncated mutant enzyme DELTAC, SDS-PAGE
homodimer
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the enzyme exists as (alpha)2 form
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
conversion from dehydrogenase to oxidase by incubation with 4,4’-dithiodipyridine
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form
purified recombinant C-terminally truncated mutant enzyme, crystals of the mutant protein are prepared in two ways: (a) crystallization of the protein directly after DTT treatment and (b) crystallization in the presence of DTT followed by extended soaks in mother liquor devoid of DTT to convert most of the protein to the XO form, X-ray diffraction structure determination and analysis at 2.0 A resolution. Comparisons of crystal structures of a stable wild-type XDH enzyme form, the triple mutant C535A/C992R/C1324, and the DELTAC truncated mutant XOR
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
C535A/C992R/C1324S triple mutant XDH crystal structure analysis
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crystal structure determination
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mutant C535A/C992R/C1324S
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C535A/C992R
site-directed mutagenesis, the mutant activity in the presence of sulfhydryl residue modifiers is very low
C535A/C992R/C1316S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
C535A/C992R/C1324S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
W335A/F336L
mutant oxidoreductase displaying xanthine oxidase activity
C535A
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4’-dithiodipyridine
C535A/C992R
-
slow conversion from dehydrogenase to oxidase by incubation with 4,4’-dithiodipyridine, conversion is blocked by NADH
C535A/C992R/C1316S
C535A/C992R/C1324S
C992R
-
resistant to conversion from dehydrogenase to oxidase by incubation with 4,4’-dithiodipyridine
additional information
construction of a variant of the rat liver enzyme that lacks the C-terminal amino acids 1316-1331. The mutant enzymes appears to assume an intermediate form, exhibiting a mixture of dehydrogenase and oxidase activities. The purified mutant protein retains about 50-70% of oxidase activity even after prolonged dithiothreitol treatment. The C-terminal region plays a role in the dehydrogenase to oxidase conversion. In the crystal structure of the protein variant, most of the enzyme stays in an oxidase conformation. But after 15 min of incubation with a high concentration of NADH, the corresponding X-ray structures show a dehydrogenase-type conformation. On the other hand, disulfide formation between Cys535 and Cys992, which can clearly be seen in the electron density map of the crystal structure of the mutant after removal of dithiothreitol, goes in parallel with the complete conversion to oxidase, resulting in structural changes identical to those observed upon proteolytic cleavage of the linker peptide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
30 min, increase in activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase. No increase in presence of adenine
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 24 h, activity of both xanthine oxidase and xanthine oxidase plus dehydrogenase is lower in liver extracts with the combined presence of adenine and dithiotreitol/phenylmethylsulfonyl fluoride
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenine may play a role in preventing the dehydrogenase to oxidase conversion during extract preparation, storage, overnight dialysis and heat treatment
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from liver
-
purification of native XDH
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form
expression analysis
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gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression of liver XDH in insect cell system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
trimetazidine causes no significant differences in XOR expression in kidneys without ischemia, whereas the XOR expression in ischemic kidneys is significantly decreased, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
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XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
medicine
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cocaine-induced cardiac disfunction is associated with an increase in NADPH oxidase and xanthine oxidoreductase activities by 59% and 29%, respectively, and a decrease in catalase activity. Apocynin or allopurinol treatment prevents the cocaine-induced cardiac alteration by restoration of cardiac output, stroke volume and fractional shortening. This is associated with a reduction of the myocardial production of superoxide anions and an enhancement of catalase activity. Apocynin treatment prevents anthine oxidoreductase up-regulation supporting the hypothesis that NADPH oxidase-derived reactive oxygen species play a role in modulating reactive oxygen species production by xanthine oxidoreductase
synthesis
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expression of enzyme in baculovirus-insect cell system, yields a mixture of native dimeric, demolydbo-dimeric and monomeric forms. All forms contain flavin, the monomeric forms lack molybdopterin and the iron-sulfur centers. Monomeric forms require only three electrons for complete reduction
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frederiks, W.M.; Vreeling-Sindelarova, H.
Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells
Acta Histochem.
104
29-37
2002
Rattus norvegicus
Manually annotated by BRENDA team
Nishino, T.; Amaya, Y.; Kawamoto, S.; Kashima, Y.; Okamoto, K.
Purification and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system
J. Biochem.
132
597-606
2002
Rattus norvegicus
Manually annotated by BRENDA team
Nishino, T.; Okamoto, K.; Kawaguchi, Y.; Hori, H.; Matsumura, T.; Eger, B.T.; Pai, E.F.
Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant
J. Biol. Chem.
280
24888-24894
2005
Rattus norvegicus
Manually annotated by BRENDA team
Maia, L.; Vala, A.; Mira, L.
NADH oxidase activity of rat liver xanthine dehydrogenase and xanthine oxidase-contribution for damage mechanisms
Free Radic. Res.
39
979-986
2005
Rattus norvegicus
Manually annotated by BRENDA team
Asai, R.; Nishino, T.; Matsumura, T.; Okamoto, K.; Igarashi, K.; Pai, E.F.; Nishino, T.
Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase
J. Biochem.
141
525-534
2007
Rattus norvegicus (P22985)
Manually annotated by BRENDA team
Roberts, L.E.; Fini, M.A.; Derkash, N.; Wright, R.M.
PD98059 enhanced insulin, cytokine, and growth factor activation of xanthine oxidoreductase in epithelial cells involves STAT3 and the glucocorticoid receptor
J. Cell. Biochem.
101
1567-1587
2007
Rattus norvegicus
Manually annotated by BRENDA team
Hagopian, K.
Rat liver xanthine oxidoreductase: effect of adenine on the oxidase and dehydrogenase activities
Ital. J. Biochem.
56
6-17
2007
Rattus norvegicus
Manually annotated by BRENDA team
Maia, L.; Duarte, R.O.; Ponces-Freire, A.; Moura, J.J.; Mira, L.
NADH oxidase activity of rat and human liver xanthine oxidoreductase: potential role in superoxide production
J. Biol. Inorg. Chem.
12
777-787
2007
Rattus norvegicus
Manually annotated by BRENDA team
Isabelle, M.; Vergeade, A.; Moritz, F.; Dautreaux, B.; Henry, J.P.; Lallemand, F.; Richard, V.; Mulder, P.; Thuillez, C.; Monteil, C.
NADPH oxidase inhibition prevents cocaine-induced up-regulation of xanthine oxidoreductase and cardiac dysfunction
J. Mol. Cell. Cardiol.
42
326-332
2007
Rattus norvegicus
Manually annotated by BRENDA team
Tsujii, A.; Nishino, T.
Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: Effect of guanidine-HCl or urea on the activity
Nucleosides Nucleotides Nucleic Acids
27
881-887
2008
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Sulikowski, T.; Domanski, L.; Ciechanowski, K.; Adler, G.; Pawlik, A.; Safranow, K.; Dziedziejko, V.; Chlubek, D.; Ciechanowicz, A.
Effect of trimetazidine on xanthine oxidoreductase expression in rat kidney with ischemia-reperfusion injury
Arch. Med. Res.
39
459-462
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kaminsky, Y.; Kosenko, C.I.e.
Brain purine metabolism and xanthine dehydrogenase/oxidase conversion in hyperammonemia are under control of NMDA receptors and nitric oxide
Brain Res.
1294
193-201
2009
Rattus norvegicus
Manually annotated by BRENDA team
Nishino, T.; Okamoto, K.; Eger, B.T.; Pai, E.F.; Nishino, T.
Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase
FEBS J.
275
3278-3289
2008
Bos taurus, Gallus gallus, Homo sapiens, Rattus norvegicus, Rhodobacter capsulatus
Manually annotated by BRENDA team
Haidari, F.; Ali Keshavarz, S.; Reza Rashidi, M.; Mohammad Shahi, M.
Orange juice and hesperetin supplementation to hyperuricemic rats alter oxidative stress markers and xanthine oxidoreductase activity
J. Clin. Biochem. Nutr.
45
285-291
2009
Rattus norvegicus
Manually annotated by BRENDA team
Haidari, F.; Rashidi, M.R.; Keshavarz, S.A.; Mahboob, S.A.; Eshraghian, M.R.; Shahi, M.M.
Effects of onion on serum uric acid levels and hepatic xanthine dehydrogenase/xanthine oxidase activities in hyperuricemic rats
Pak. J. Biol. Sci.
11
1779-1784
2008
Rattus norvegicus
Manually annotated by BRENDA team
Shimo, T.; Ashizawa, N.; Moto, M.; Matsumoto, K.; Iwanaga, T.; Nagata, O.
FYX-051, a xanthine oxidoreductase inhibitor, induces nephropathy in rats, but not in monkeys
Toxicol. Pathol.
37
438-445
2009
Rattus norvegicus
Manually annotated by BRENDA team
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
J. Am. Chem. Soc.
132
17080-17083
2010
Bos taurus, Rattus norvegicus (P22985)
Manually annotated by BRENDA team
Wang, C.H.; Zhang, C.; Xing, X.H.
Xanthine dehydrogenase an old enzyme with new knowledge and prospects
Bioengineered
7
395-405
2016
Acinetobacter baumannii, Acinetobacter phage Ab105-3phi, Arabidopsis thaliana (Q8GUQ8), Arthrobacter luteolus, Bos taurus, Clostridium cylindrosporum, Drosophila melanogaster, Enterobacter cloacae, Escherichia coli (Q46799 AND Q46800), Gallus gallus, Homo sapiens, Micrococcus sp., Ovis aries, Pseudomonas putida, Rattus norvegicus, Rhodobacter capsulatus, Rhodobacter capsulatus B10XDHB, Streptomyces cyanogenus
Manually annotated by BRENDA team
Nishino, T.; Okamoto, K.; Kawaguchi, Y.; Matsumura, T.; Eger, B.T.; Pai, E.F.; Nishino, T.
The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase
FEBS J.
282
3075-3090
2015
Rattus norvegicus (P22985)
Manually annotated by BRENDA team