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hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
xanthine + NAD+ + H2O
urate + NADH + H+
1-methylhypoxanthine + NAD+ + H2O
1-methylxanthine + NADH
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH
-
10% of the activity compared to hypoxanthine
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
2,6-diaminopurine + NAD+ + H2O
? + NADH + H+
-
poor substrate
-
-
?
2-hydroxy-6-methylpurine + NAD+ + H2O
? + NADH + H+
-
poor substrate
-
-
?
2-hydroxypurine + NAD+ + H2O
? + NADH
-
35% of the activity compared to hypoxanthine, purine not oxidized
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
4-hydroxypyrazolo(3,4-d)pyrimidine + nitroblue tetrazolium + H2O
4,6-dihydroxypyrazolo(3,4-d)pyrimidine + reduced nitroblue tetrazolium
-
i.e. allopurinol
-
?
6,8-dihydropurine + NAD+ + H2O
? + NADH
-
50% of the activity compared to hypoxanthine
-
?
6-thioxanthine + NAD+ + H2O
6-thiourate + NADH + H+
-
effective substrate
-
-
?
6-thioxanthine + NAD+ + H2O
? + NADH + H+
-
good substrate
-
-
?
8-azahypoxanthine + NAD+ + H2O
8-azaxanthine + NADH
-
39% 0f the activity compared to hypoxanthine
-
?
acetaldehyde + 2,6-dichloroindophenol + H2O
?
-
0.1% of activity with xanthine
-
-
?
glyceraldehyde + 2,6-dichloroindophenol + H2O
?
-
0.3% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + 2 H2O
urate + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
hypoxanthine + uric acid imine
?
-
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
-
-
-
r
pterin + 2,6-dichloroindophenol + H2O
?
-
9.7% of activity with xanthine
-
-
?
purine + 2,6-dichloroindophenol + H2O
?
-
8.5% of activity with xanthine
-
-
?
xanthine + DCIP + H2O
urate + reduced DCIP
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
xanthine + NAD+ + H2O
urate + NADH + H+
xanthine + O2 + H2O
urate + O2- + 2 H+
-
-
-
?
xanthine + ureic acid imine
?
-
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
-
-
?
additional information
?
-
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
mechanism of substrate binding at the active site, importance of beta subunit residue Glu232 for substrate positioning, overview. The oxygen atom at the C-6 position of both substrates is oriented toward ArgB-310 in the active site
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
mechanism of substrate binding at the active site, importance of beta subunit residue Glu232 for substrate positioning, overview. The oxygen atom at the C-6 position of both substrates is oriented toward ArgB-310 in the active site
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
10fold reduced kred-value compared to xanthine
-
-
?
1-methylxanthine + NAD+ + H2O
1-methylurate + NADH + H+
-
rather less effective than xanthine as a substrate
-
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
good substrate
-
-
?
2-thioxanthine + NAD+ + H2O
2-thiourate + NADH + H+
-
effective substrate
-
-
?
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
preferred substrate
-
ir
hypoxanthine + NAD+ + H+ + O2- + H2O
xanthine + NADH + H2O2
-
19% of activity with xanthine
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
?
hypoxanthine + NAD+ + H2O
xanthine + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH
-
67% of the activity compared to hypoxanthine
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
-
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH
-
-
?
xanthine + NAD+ + H2O
urate + NADH + H+
product release is principally rate-limiting in catalysis
-
-
?
additional information
?
-
-
model in which good substrates are bound correctly in the active site in an orientation that allows Arg310 to stabilize the transition state for the first step of the overall reaction via an electrostatic interaction at the C-6 position, thereby accelerating the reaction rate. Poor substrates bind upside down relative to this correct orientation and are unable to avail themselves of the additional catalytic power provided by Arg310 in wild-type enzyme but are significantly less affected by mutations at this position. Analysis of rapid reaction kinetic parameters
-
-
?
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
?
-
-
xanthine and 2-hydroxy-6-methylpurine are substrates. Substrate binding structures, overview
-
-
?
additional information
?
-
ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of xanthine
-
-
?
additional information
?
-
pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Method development and evaluation, overview
-
-
?
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
-
-
?
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molybdopterin
-
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
FAD
-
FAD
-
0.9 mol per subunit
FAD
a molybdenum-containing flavoenzyme
FAD
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
molybdenum cofactor
-
binding involves residues GluB730, GlnA102, CysA103, CysA106, CysA134, and CysA13 of the alpha and beta subunits
molybdenum cofactor
-
structure-function analysis, mechanism, overview
molybdenum cofactor
-
a molybdenum-containing flavoprotein
molybdenum cofactor
-
MoCo, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups
NAD+
-
-
NAD+
-
cannot be replaced by NADP+
[2Fe-2S]-center
-
-
[2Fe-2S]-center
-
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
additional information
-
-
-
additional information
-
-
-
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. Rhodobacter capsulatus alpha2beta2 XDH arranges the FAD and [2Fe-2S] domains and the Moco domain into 2 separate subunits
-
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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Fe
-
8 atoms iron per mol enzyme
Mo
-
2 molybdenum per mol enzyme
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
Fe2+
-
in a [Fe4-S4] domain
Fe2+
-
in the [2Fe-2S] center
Fe2+
in the [2Fe-2S] center
Fe2+
in the [Fe2-S2] redox center
Iron
-
FeS center, EPR spectra, wild type 3.7 mol per subunit, active form of mutant R135C 2.8 mol per subunit, inactive form of mutant R135C 1.2 mol per subunit
Iron
-
the enzyme is a molybdo-flavoprotein, the enzyme tetramer contains two [2Fe-2S] clusters
Molybdenum
-
-
Molybdenum
-
active form of mutant R135C Moco content 97%, inactive form of mutant R135C Moco content 3.8%
Molybdenum
-
protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor
Molybdenum
-
the enzyme is molybdo-flavoprotein, one cofactor molecule per enzyme tetramer
Molybdenum
in the molybdenum cofactor
Molybdenum
-
a molybdenum-containing flavoprotein
Molybdenum
-
in the molybdenum cofactor, the metal ion binds a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups. Oxidized wild-type and mutant Q179A reveal a similar Mo(VI) ion with each one molybdopterin, Mo=O, Mo-O-, and Mo=S ligand, and a weak Mo-O(E730) bond at alkaline pH
Molybdenum
molybdenum-containing flavoenzyme, in the molybdenum cofactor (Moco)
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additional information
additional information
-
0.0809
DCPIP
-
pH 7.8, 25°C, mutants Q102A and Q102G
0.0823
DCPIP
-
pH 7.8, 25°C, wild-type enzyme
0.0328
NAD+
-
pH 7.8, 25°C, wild-type enzyme
0.036
NAD+
pH 8.5, 40°C, Split166 mutant
0.036
NAD+
pH 8.5, 40°C, Split178 mutant
0.0373
NAD+
-
pH 7.8, 25°C, mutant Q102G
0.0402
NAD+
-
pH 7.8, 25°C, mutant Q102A
0.044
NAD+
pH 8.5, 40°C, wild-type enzyme
0.103
NAD+
-
wild-type, pH 7.8, 25°C
0.0227
xanthine
-
pH 7.8, 25°C, mutant Q102G, with NAD+
0.0293
xanthine
-
pH 7.8, 25°C, mutant Q102A, with NAD+
0.0442
xanthine
-
pH 7.8, 25°C, wild-type enzyme, with NAD+
0.055
xanthine
pH 8.5, 40°C, Split178 mutant
0.064
xanthine
-
wild-type, pH 7.8, 25°C
0.068
xanthine
pH 8.5, 40°C, wild-type enzyme
0.096
xanthine
pH 8.5, 40°C, Split166 mutant
0.163
xanthine
-
mutant E232A, pH 7.8, 25°C
additional information
additional information
-
rapid reaction kinetic parameters for substrates xanthine, 2-thioxanthine, 6-thioxanthine, 1-methylxanthine, 2-hydroxy-6-methylpurine, and 2,6-diaminopurine, in wild-type and mutants R310K and R310M
-
additional information
additional information
-
2-position hydroxylation is crucial for 8-position hydroxylation. Stopped-flow studies indicate that the rate-limiting step of the reductive half-reaction is not electron transfer from the xanthine substrate to the molybdenum center, but product release
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
steady-state kinetics and reductive half-reaction, stopped flow kinetics, kinetic analysis of wild-type and mutant xanthine dehydrogenases, overview. kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme. 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. The product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release is not as great in the bacterial enzyme as compared with the vertebrate forms. The faster turnover observed with the bacterial enzyme isdue to a faster rate constant for product release than is seen with the vertebrate enzyme
-
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evolution
-
the enzyme belongs to the xanthine oxidase family
evolution
-
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
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. Physiological roles and applications of bacterial XDHs, overview
additional information
-
active site structure, overview
additional information
-
analysis of the mechanism of transfer of an oxygen atom to the substrate
additional information
the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH
additional information
-
the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
additional information
XDH active site structure with conserved Glu232 and Arg310 residues. Analysis of crystal structure of xanthine dehydrogenase, PDB ID 2W3S, where an ionized glutamate 802/232 acts as a hydrogen bonding acceptor from the substrate N3 nitrogen
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EB232Q
catalytically inactive active site mutant, inactive desulfo enzyme form
C134A/C136A
-
site-directed mutagenesis, an inactive subunit A mutant
C44A/C47A
-
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
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
E730D
-
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
R330M
-
the activity with substrate 2-hydroxy-6-methylpurine is only slightly affected
E232A
-
decrease in kcat value, increase in KM-value
E232A
site-directed mutagenesis, the mutant exhibits a 12fold decrease in kred compared to wild-type
E730A
-
no enzymic activity
E730A
-
crystal structure determination and analysis, comparison with wild-type enzyme structure, the sulfido is replaced with an oxo ligand in the inactive E730A mutant, further showing another oxo and one Mo-OH ligand at Mo, which are independent of pH
R310K
-
absorption spectra similar to wild-type. 20fold decrease of kred-value
R310K
-
kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20-fold decreased
R310M
-
absorption spectra similar to wild-type. 20000fold decrease of kred-value
R310M
-
kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20000-fold decreased
additional information
pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Macroporous ITO electrodes are used as an immobilization platform for the fabrication of HX-sensitive electrodes. The efficient polymer/enzyme interaction can be advantageously combined with the open structure of an electrode material of controlled pore size, resulting in good processability, stability, and defined signal transfer in the presence of a substrate. Method development and evaluation, overview
additional information
succesfull mechanism-based metabolic engineering of Escherichia coli strain BL21(DE3) cell factory for production of functionally active, highly-producing xanthine dehydrogenase by co-overexpression of enzyme XDH from Rhodobacter capsulatus with three global regulators (IscS, TusA and NarJ) and four chaperone proteins (DsbA, DsbB, NifS and XdhC) to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH, method devlopment, overview. Three helper proteins, NifS, IscS and DsbB improve the specific activity of RcXDH significantly by 30%, 94% and 49%, respectively. The combination of NifS and IscS synergistically increases the specific activity by 1.29fold, and enhances the total enzyme activity by an impressive 3.9fold
additional information
-
the enzyme mutants show alterations in the Mo site structure, which changes in a pH range of 5-10, and in the influence of amino acids (Glu730 and Gln179) close to molybdenum cofactor in wild-type, and Q179A and E730A mutants, enzyme kinetics and quantum chemical studies, overview
additional information
two (alphabetagamma)2 XDH variants, Split166 and Split178, are designed and constructed by splitting the small subunit (alphabeta)2 XDH at the N- and C-terminal ends of the L167-A178 peptide linking the iron-sulfur clusters and flavin adenine dinucleotide domains, respectively. Subunit composition of recombinant wild-type and split XDHsAs, overview. As for the co-substrate NAD+, mutant Split178 has a 1.07fold increased catalytic efficiency, while Split166 has a 3.8fold decreased catalytic efficiency compared to the wild-type XDH, for the substrate xanthine, the Split178 variant shows 1.21fold increased turnover number and 1.66fold increased catalytic efficiency, while the mutant Split166 shows a 4.31fold decrease in comparison to the wild-type enzyme
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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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
-
brenda
Kalimuthu, P.; Leimkuehler, S.; Bernhardt, P.V.
Catalytic electrochemistry of xanthine dehydrogenase
J. Phys. Chem. B
116
11600-11607
2012
Rhodobacter capsulatus
brenda
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)
-
brenda
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)
-
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda