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Information on EC 1.17.1.4 - xanthine dehydrogenase and Organism(s) Rhodobacter capsulatus and UniProt Accession O54050

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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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Rhodobacter capsulatus
UNIPROT: O54050
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Word Map
The taxonomic range for the selected organisms is: Rhodobacter capsulatus
The enzyme appears in selected viruses and cellular organisms
Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, xanthine dehydrogenase-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD-xanthine dehydrogenase
-
-
-
-
Rosy locus protein
-
-
-
-
xanthine dehydrogenase
-
-
xanthine oxidoreductase
xanthine-NAD oxidoreductase
-
-
-
-
xanthine/NAD+ oxidoreductase
-
-
-
-
XDH/XO
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
the catalytic sequence of Rhodobacter capsulatus XDH is initiated by abstraction of a proton from the Mo-OH group by the highly conserved active site subunit B residue Glu730, followed by nucleophilic attack of the resulting Mo-O on the carbon center of the substrate (C-2 in hypoxanthine and C-8 in xanthine) and concomitant hydride transfer to the Mo-S of the molybdenum center, reaction and substrate binding mechanisms, overview
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
-
oxidation
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-
-
-
reduction
-
-
-
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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 + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
show the reaction diagram
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
show the reaction diagram
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
show the reaction diagram
2,6-diaminopurine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
poor substrate
-
-
?
2-hydroxy-6-methylpurine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
poor substrate
-
-
?
2-hydroxypurine + NAD+ + H2O
? + NADH
show the reaction diagram
-
35% of the activity compared to hypoxanthine, purine not oxidized
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
show the reaction diagram
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
show the reaction diagram
-
i.e. allopurinol
-
?
6,8-dihydropurine + NAD+ + H2O
? + NADH
show the reaction diagram
-
50% of the activity compared to hypoxanthine
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH + H+
show the reaction diagram
-
effective substrate
-
-
?
6-thioxanthine + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
show the reaction diagram
-
39% 0f the activity compared to hypoxanthine
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
0.1% of activity with xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
0.3% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
hypoxanthine + uric acid imine
?
show the reaction diagram
-
uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
r
pterin + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
9.7% of activity with xanthine
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
show the reaction diagram
-
8.5% of activity with xanthine
-
-
?
xanthine + DCIP + H2O
urate + reduced DCIP
show the reaction diagram
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
xanthine + ureic acid imine
?
show the reaction diagram
-
uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system
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-
?
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 + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
show the reaction diagram
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
show the reaction diagram
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
show the reaction diagram
xanthine + NAD+ + H2O
urate + NADH
show the reaction diagram
xanthine + NAD+ + H2O
urate + NADH + H+
show the reaction diagram
xanthine + O2 + H2O
urate + O2- + 2 H+
show the reaction diagram
-
-
-
?
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
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
[2Fe-2S] cluster
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[2Fe-2S]-center
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
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8 atoms iron per mol enzyme
Mo
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2 molybdenum per mol enzyme
Molybdenum
additional information
O54050; O54051; Q9X7K2
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
allopurinol
i.e. 1-H-pyrazolo [3,4-d] pyrimidine-4-one
pterin-6-aldehyde
competitive inhibition pattern, mechanism of inhibitor binding at the active site, overview
1-methylhypoxanthine
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17% inhibition of xanthine dehydrogenase at 0.25 mM
4-hydroxypyrazolo(3,4-d)pyrimidine
8-Azaadenine
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complete inhibition of xanthine dehydrogenase at 0.2 mM
8-Azaguanine
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complete inhibition of xanthine dehydrogenase at 0.2 mM
8-azohypoxanthine
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40% inhibition of xanthine dehydrogenase at 0.25 mM
adenine
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competitive inhibition, Ki: 0.05 mM
allopurinol
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-
alloxanthine
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a mechanism-based inhibitor, binding structure, overview. Inhibition mechanism involves binding to molybdenum, overview
Urate
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competitive inhibition of xanthine dehydrogenase, Ki: 0.144 mM
xanthine
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40% inhibition of xanthine dehydrogenase at 0.25 mM
additional information
-
no substrate inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
activation mechanism based on the results of mutations at the positions of the second Glu and Arg residues, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0809 - 0.0823
DCPIP
0.0525
hypoxanthine
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-
0.0328 - 0.103
NAD+
0.0227 - 0.163
xanthine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19 - 191
NAD+
4.4 - 200
xanthine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
530 - 5310
NAD+
230 - 3640
xanthine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
oxypurinol
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0.1036
pterin-6-aldehyde
pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.5
-
purified enzyme, pH and temperature not specified in the publication
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11.5
O54050; O54051; Q9X7K2
activity range, bell-shaped pH-activity relationships for both the recombinant split variants
4.5 - 9
the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above
additional information
comparison of the pH dependence of both kred and kred/Kd from reductive half-reaction experiments between wild-type enzyme and mutant E232Q, overview. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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highest activity, but unstable
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O54050_RHOCA
462
0
49293
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
345000
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gel filtration
84200
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4 * 84200, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
(alphabeta)2 heterotetramer
heterohexamer
O54050; O54051; Q9X7K2
an (alphabetagamma)2 heterohexameric enzyme
heterotetramer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
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-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme and subunit beta mutants E232A and E232Q with or without molybdenum cofactor, hanging drop vapor diffusion method, 15 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM EDTA, 200 mM NaCl,and 2.5 mM dithiothreitol are mixed 1 mM NAD+ and inhibitor pterin-6-aldehyde and with the reservoir solution containing 6-8 mM BaCl2, 6-8% polyethylene glycol 8000, 100 mM Tris-HCl, pH 8.3, 5-25mM dithiothreitol, and 3-4% isopropanol, whereas the EB232Q variant is mixed in a 1:2 ratio with the same reservoir solution, X-ray diffraction structure determination and analysis at 2.6-3.4 A resolution, overview
2.7 A resolution, direct coordination of alloxanthine to the molybdenum via a nitrogen atom
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crystal structure determination
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crystal structure determination of the free enzyme and the enzyme in complex with inhibitor alloxanthine
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EB232Q
catalytically inactive active site mutant, inactive desulfo enzyme form
C134A/C136A
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site-directed mutagenesis, an inactive subunit A mutant
C44A/C47A
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site-directed mutagenesis, an instable subunit A mutant that cannot be purified
E220R/D517R
-
site-directed mutagenesis, a subunit B mutant that is mainly dimeris incontrast to the tetrameric wild-type enzyme, inactive mutant
E232A
E232Q
site-directed mutagenesis, kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, the mutant exhibits a 12fold decrease in kred, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme
E730A
E730D
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no enzymic activity
E730Q
-
no enzymic activity
E730R
-
no enzymic activity
Q102A
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
Q102G
-
site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme
Q179A
-
crystal structure determination and analysis, comparison with wild-type enzyme structure, a similar acidic pK for the wild-type and Q179A variants, as well as the metrical parameters of the Mo site and density functional theory calculations, suggested protonation at the equatorial oxo group. 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
R135C
-
mutation corresponding to human protein variant of a patient suffering from xanthinuria I. Mutation results in an active (alphabeta)2 heterotetrameric form besides an inactive alphabeta heterodimeric form missing the FeSI center
R310K
R310M
R330M
-
the activity with substrate 2-hydroxy-6-methylpurine is only slightly affected
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11.5
O54050; O54051; Q9X7K2
both the recombinant split variants display similar bell-shaped pH-activity relationships with the optimum activity at pH 8.5 and remain stable in buffers ranging from pH 4.0-11.5 after incubation at 25°C for 24 h
744255
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
stable for 4 min
51.6
O54050; O54051; Q9X7K2
t1/2 for the wild-type enzyme, pH 8.5, 30 min
63
O54050; O54051; Q9X7K2
t1/2 for the mutant Split166 enzyme, pH 8.5, 30 min
63.2
O54050; O54051; Q9X7K2
t1/2 for the mutant Split178 enzyme, pH 8.5, 30 min
65
O54050; O54051; Q9X7K2
all the XDHs exhibit a bell-shaped temperature-activity relationship with maximum activity at 40°C, the recombinant split variants are more thermostable than the wild-type. Both Split166 and Split178 maintain about 60% of maximal activity at 65°C, while the wild-type shows below 20% remaining activity after 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes with or without molybdenum cofactor by nickel affinity and anion exchange chromatography, followed by gel filtration
purification of native XDH
-
recombinant His-tagged enzyme from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant His-tagged wild-type and mutant XDHs from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by ultrafiltration and gel filtration
-
to homogeneity, affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes
C-terminally His6-tagged wild-type and mutant XDHs expression in Escherichia coli strain TP1000
-
expressed in Escherichia coli
-
gene Xdh, recombinant expression in Escherichia coli strain BL21(DE3), co-overexpression with three global regulators from Escherichia coli, IscS, TusA and NarJ and two Escherichia coli as well as two Rhodobacter capsulatus chaperone proteins, i.e. DsbA and DsbB, and NifS and XdhC (UniProt ID Q9X7K2), respectively, to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
-
gene XDH1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
genes xdhA-C, development of a method that translates active Rhodobacter capsulatus (alphabetagamma)2 XDH by directly expressing the iron-sulfur domain, the flavin adenine dinucleotide domain and the sulfurated molybdenum domain as three separate proteins in Escherichia coli, recombinant expression of wild-type enzyme and mutant enzymes, i.e. an (alphabetagamma)2 heterohexameric enzyme and two (alphabetagamma)2 XDH variants, in Escherichia coli
O54050; O54051; Q9X7K2
recombinant expression in Escherichia coli
-
recombinant expression of His-tagged enzyme in Escherichia coli strain TP1000
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
-
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Truglio, J.J.; Theis, K.; Leimkuhler, S.; Rappa, R.; Rajagopalan, K.V.; Kisker, C.
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus
Structure
10
115-125
2002
Rhodobacter capsulatus
Manually annotated by BRENDA team
Aretz, W.; Kaspari, H.; Klemme, J.H.
Molecular and kinetic characterization of xanthine dehydrogenase from the phototrophic bacterium Rodopseudomonas capsulata
Z. Naturforsch. C
36
933-941
1981
Rhodobacter capsulatus
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Leimkuhler, S.; Stockert, A.L.; Igarashi, K.; Nishino, T.; Hille, R.
The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase
J. Biol. Chem.
279
40437-40444
2004
Rhodobacter capsulatus
Manually annotated by BRENDA team
Neumann, M.; Schulte, M.; Juenemann, N.; Stoecklein, W.; Leimkuehler, S.
Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase
J. Biol. Chem.
281
15701-15708
2006
Rhodobacter capsulatus
Manually annotated by BRENDA team
Pauff, J.M.; Hemann, C.F.; Juenemann, N.; Leimkuehler, S.; Hille, R.
The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus
J. Biol. Chem.
282
12785-12790
2007
Rhodobacter capsulatus
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
Schumann, S.; Saggu, M.; Moeller, N.; Anker, S.D.; Lendzian, F.; Hildebrandt, P.; Leimkuehler, S.
The mechanism of assembly and cofactor insertion into Rhodobacter capsulatus xanthine dehydrogenase
J. Biol. Chem.
283
16602-16611
2008
Rhodobacter capsulatus
Manually annotated by BRENDA team
Dietzel, U.; Kuper, J.; Doebbler, J.A.; Schulte, A.; Truglio, J.J.; Leimkuehler, S.; Kisker, C.
Mechanism of substrate and inhibitor binding of Rhodobacter capsulatus xanthine dehydrogenase
J. Biol. Chem.
284
8768-8776
2009
Rhodobacter capsulatus (O54050)
Manually annotated by BRENDA team
Cao, H.; Pauff, J.; Hille, R.
Substrate orientation and the origin of catalytic power in xanthine oxidoreductase
Indian J. Chem.
50
355-362
2011
Rhodobacter capsulatus
-
Manually annotated by BRENDA team
Kalimuthu, P.; Leimkuehler, S.; Bernhardt, P.V.
Catalytic electrochemistry of xanthine dehydrogenase
J. Phys. Chem. B
116
11600-11607
2012
Rhodobacter capsulatus
Manually annotated by BRENDA team
Sarauli, D.; Borowski, A.; Peters, K.; Schulz, B.; Fattakhova-Rohlfing, D.; Leimkuehler, S.; Lisdat, F.
Investigation of the pH-dependent impact of sulfonated polyaniline on bioelectrocatalytic activity of xanthine dehydrogenase
ACS Catal.
6
7152-7159
2016
Rhodobacter capsulatus (O54050 AND O54051)
-
Manually annotated by BRENDA team
Wang, C.; Li, G.; Zhang, C.; Xing, X.
Enhanced catalytic properties of novel (alphabetagamma)2 heterohexameric Rhodobacter capsulatus xanthine dehydrogenase by separate expression of the redox domains in Escherichia coli
Biochem. Eng. J.
119
1-8
2017
Rhodobacter capsulatus (O54050 AND O54051 AND Q9X7K2), Rhodobacter capsulatus CGMCC 1.3366 (O54050 AND O54051 AND Q9X7K2)
-
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
Wang, C.H.; Zhang, C.; Xing, X.H.
Metabolic engineering of Escherichia coli cell factory for highly active xanthine dehydrogenase production
Biores. Technol.
245
1782-1789
2017
Rhodobacter capsulatus (O54050 AND O54051), Rhodobacter capsulatus CGMCC 1.3366 (O54050 AND O54051)
Manually annotated by BRENDA team
Reschke, S.; Mebs, S.; Sigfridsson-Clauss, K.G.; Kositzki, R.; Leimkuehler, S.; Haumann, M.
Protonation and sulfido versus oxo ligation changes at the molybdenum cofactor in xanthine dehydrogenase (XDH) variants studied by X-ray absorption spectroscopy
Inorg. Chem.
56
2165-2176
2017
Rhodobacter capsulatus
Manually annotated by BRENDA team
Hall, J.; Reschke, S.; Cao, H.; Leimkuehler, S.; Hille, R.
The reductive half-reaction of xanthine dehydrogenase from Rhodobacter capsulatus the role of Glu232 in catalysis
J. Biol. Chem.
289
32121-32130
2014
Rhodobacter capsulatus (O54050 AND O54051)
Manually annotated by BRENDA team