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Information on EC 1.17.1.4 - xanthine dehydrogenase and Organism(s) Bos taurus and UniProt Accession P80457
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1.17.1.4 xanthine dehydrogenaseIUBMB 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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Word Map
- 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
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine dehydrogenase-1, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD-xanthine dehydrogenase
-
-
-
-
Rosy locus protein
-
-
-
-
xanthine oxidoreductase
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
XDH/XO
-
-
-
-
XOR
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
xanthine oxidoreductase
-
-
-
-
XOR
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
catalytically labile Mo-OH oxygen forms a bond with a carbon atom of substrate, the Mo=S group of the oxidized enzyme becomes protonated to afford Mo-SH on reduction of the molybdenum center
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -
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
9054-84-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
2-amino-4-hydroxypterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
1.2% of activity with xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
12.1% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
12.4% of activity with xanthine
-
-
?
xanthine + p-benzoquinone + H2O
hypoxanthine + hydroquinone + ?
-
electron donor only for oxidase type
-
?
xanthine + p-benzoquinone + H2O
p-benzosemiquinone + urate
-
electron acceptor p-benzoquinone for both dehydrogenase and oxidase types
-
?
xanthine + NAD+ + H2O
urate + NADH
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
additional information
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
additional information
?
-
-
The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-4-hydroxy-pterin + NAD+ + H2O
isoxanthopterin + NADH
-
i.e. pterin
-
?
xanthine + NAD+ + H2O
urate + NADH
-
xanthine dehydrogenase form has distinct xanthine/oxygen activity, 35-42% of electrons transferred to O2 to form O2-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
conversion of dehydrogenase to oxidase type due to oxidation of sulfhydryl groups by molecular oxygen, dehydrogenase activity recovered by treatment with dithiothreitol
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH
-
NAD+-dependent dehydrogenase type D
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
catalytically relevant binding mode of the substrate xanthine, overview
-
-
?
xanthine + O2 + H2O
urate + O2- + 2 H+
-
xanthine oxidase form transfers 22% electrons to oxygen to form superoxide
-
?
additional information
?
-
-
xanthine oxidoreductase plays a physiological role in milk equal in importance to its catalytic function as an enzyme
-
-
?
additional information
?
-
-
xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
FAD
-
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
molybdopterin
-
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
additional information
-
one molybdopterin-cofactor, two Fe2-S2-cluster, one FAD per subunit
-
additional information
-
cofactor conformation, binding structure analysis and mechanism, overview
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur-center
Molybdenum
molybdenum-center
Iron-sulfur-center
-
2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(3-cyano-4-isobutoxyphenyl)-4-methyl-5-thiazolecarboxylic acid
i.e. TEI-6720, mixed type inhibitor, binds very tightly to active and inactive desulfo-form of enzyme
4-(5-pyridin-4-yl-1H-1,2,4-triazol-3-yl)pyridine-2-carbonitrile
i.e. FYX-051, strong, in absence of xanthine slow hydroxylation of inhibitor
2-amino-4-hydroxypteridine-6-carboxyaldehyde
-
competitive inhibition of 2-amino-4-hydoxy-pterine oxidation, Ki: 0.000016 mM
8-Azaguanine
-
competitive inhibition of 2-amino-4-hydroxypterine oxidation, Ki: 0.0012 mM
allopurinol
-
mechanism-based inhibitor. Allopurinol is oxidized by xanthine oxidoreductase itself to oxypurinol which forms a covalent bond with the reduced molybdenium atom
ammeline
-
competitive inhibition of 2-amino-4-hydroxy-pterine oxidation, Ki: 0.016 mM
febuxostat
-
structure-based inhibitor, forms numerous hydrogen bonds, slat bridges, and hydrophobic interactions with amino acids in the active site and nearly completely fills the narrow channel leading to the molydbenum center of the enzyme
FYX-051
-
inhibitor has features of both a mechanism-based and a structure-based inhibitor. It is a slow substrate and forms a stable reaction intermediate with the molybdenum atom in the enzyme
Guanidine-HCl
-
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. Above 3 M gunandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis
NADH
-
partial reduction of dehydrogenase activity under anaeroboic conditions, oxidase activity more slowly reduced
NO
-
dose-dependent inhibition of xanthine dehydrogenase and oxidase activity, reaction with an essential sulfur in the molybdenum center, that damages the molybdopterin
Oxipurinol
-
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. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261
Urea
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiol active compounds
-
reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
644555, 644564, 644567, 644587, 644588, 644595, 659210, 659580, 671830, 689276, 689277, 703626, 715273, 744450
-
only oxidase type in stored milk, 94% NAD+-dependent dehydrogenase type in fresh milk
-
xanthine oxidoreductase associated with milk phospholipid membranes was found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
milk phospholipid membrane, mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
physiological function
additional information
physiological function
-
xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation
physiological function
-
XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts
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
additional information
-
Glu802 binds the substrate and stabilizes the transition state, Glu1261 is the catalytic base, Arg880 and Thr1010 bind the substrate and decrease the reaction activation energy, Phe914 and Phe1009 orientate the substrate via pi-pi stacking, Val1011 is the key residue channeling the substrate, and Gln758 is responsible for releasing the product. There is an obvious variation of key residues channeling the substrate and binding pocket, which affect the substrate entry and product release, resulting in different catalytic activity and enzymatic properties. Surprisingly, the 2 pairs of cysteines, C535 and C992, and C1316 and C1324 numbering in bovine XDH, which are proposed to control the reversible post-translational conversion from XDH to XOD, EC 1.17.3.2, by forming 2 cysteine disulfide bonds, are totally absent in other XDHs. Bovine milk XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XDH_BOVIN
1332
0
146790
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
high-resolution crystal structure of XDH at 1.65 A resolution confirms the overall fold of the dimeric protein, the location of the cofactors and the mobile stretches of the polypeptide chain. 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
in complex with inhibitor FYX051, which is slowly hydroxylated by the enzyme
2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor
-
batch method, 2.5 and 3.3 A resolution for irreversible proteolytically cleaved xanthine oxidase form, 2.1 A resolution for dehydrogenase form
-
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
-
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. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38
-
dehydrogenase type unstable, change to oxidase type inhibited under anaerobic conditions
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 0.1 M sodium diphosphate, 0.3 mM EDTA, pH 7.5, 1 mM salicylate, 2.5 mM DTT, 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
highly active bovine XOR in its XDH form is prepared by folate affinity chromatography
-
to homogeneity, 2 types: dehydrogenase type, chromatography techniques, oxidase type: affinity chromatography
-
to homogeneity, presence of DTT required for purification of the dehydrogenase form
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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. Above 3 M guandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
nutrition
-
xanthine oxidoreductase associated with milk phospholipid membranes is found to be distributed among an intra-membranous pool in which it takes the form of a mixture of xanthine oxidase and xanthine dehydrogenase, with a clear predominance of xanthine dehydrogenase, and a free pool of xanthine oxidase, of which 33% is found in the outer surface of milk fat globule membrane, 20.5% in the outer surface of whey membrane particles, and the remaining 46.7% in apparent solution. The inner-membrane xanthine oxidoreductase may play a nonenzymatic role in fat secretion, whereas extramembranous xanthine oxidase is freely available for a role in the innate gland immune system and may affect milk quality
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eger, B.T.; Okamoto, K.; Enroth, C.; Sato, M.; Nishino, T.; Pai, E.F.; Nishino, T.
Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk
Acta Crystallogr. Sect. D
56
1656-1658
2000
Bos taurus
-
Enroth, C.; Eger, B.T.; Okamoto, K.; Nishino, T.; Nishino, T.; Pai, E.F.
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
Proc. Natl. Acad. Sci. USA
97
10723-10728
2000
Bos taurus
Ichimori, K.; Fukahori, M.; Nakazawa, H.; Okamoto, K.; Nishino, T.
Inhibition of xanthine oxidase and xanthine dehydrogenase by nitric oxid
J. Biol. Chem.
274
7763-7768
1999
Bos taurus
Waud, W.R.; Rajagopalan, K.V.
The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O)
Arch. Biochem. Biophys.
172
365-379
1976
Bos taurus, Rattus sp.
Hunt, J.; Massey, V.
Purification and properties of milk xanthine dehydrogenase
J. Biol. Chem.
267
21479-21485
1992
Bos taurus
Yen, T.T.T.; Glassman, E.
Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster: II. Enzyme kinetics
Biochim. Biophys. Acta
146
35-44
1967
Bos taurus, Drosophila melanogaster
Nakamura, M.; Yamazaki, I.
Preparation of bovine milk xanthine oxidase as a dehydrogenase form
J. Biochem.
92
1279-1286
1982
Bos taurus
Okamoto, K.; Eger, B.T.; Nishino, T.; Kondo, S.; Pai, E.F.
An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition
J. Biol. Chem.
278
1848-1855
2003
Bos taurus (P80457)
Leimkuhler, S.; Hodson, R.; George, G.N.; Rajagopalan, K.V.
Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans
J. Biol. Chem.
278
20802-20811
2003
Bos taurus, Rhodobacter capsulatus
Benboubetra, M.; Baghiani, A.; Atmani, D.; Harrison, R.
Physicochemical and kinetic properties of purified sheep's milk xanthine oxidoreductase
J. Dairy Sci.
87
1580-1584
2004
Bos taurus, Capra hircus, Homo sapiens, Ovis aries
Okamoto, K.; Matsumoto, K.; Hille, R.; Eger, B.T.; Pai, E.F.; Nishino, T.
The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition
Proc. Natl. Acad. Sci. USA
101
7931-7936
2004
Bos taurus (P80457)
Godber, B.L.; Schwarz, G.; Mendel, R.R.; Lowe, D.J.; Bray, R.C.; Eisenthal, R.; Harrison, R.
Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres
Biochem. J.
388
501-508
2005
Bos taurus, Homo sapiens (P47989)
Silanikove, N.; Shapiro, F.
Distribution of xanthine oxidase and xanthine dehydrogenase activity in bovine milk: Physiological and technological implications
Int. Dairy J.
17
1188-1194
2007
Bos taurus
Okamoto, K.; Nishino, T.
Crystal structures of mammalian xanthine oxidoreductase bound with various inhibitors: allopurinol, febuxostat, and FYX-051
J. Nippon Med. Sch.
75
2-3
2008
Bos taurus
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
Okamoto, K.; Eger, B.T.; Nishino, T.; Pai, E.F.; Nishino, T.
Mechanism of inhibition of xanthine oxidoreductase by allopurinol: crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol
Nucleosides Nucleotides Nucleic Acids
27
888-893
2008
Bos taurus
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
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)
Ishikita, H.; Eger, B.T.; Okamoto, K.; Nishino, T.; Pai, E.F.
Protein conformational gating of enzymatic activity in xanthine oxidoreductase
J. Am. Chem. Soc.
134
999-1009
2012
Bos taurus (P80457)
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
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