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IUBMB Comments Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine.
The enzyme appears in viruses and cellular organisms
Synonyms
alpha-ketoglutarate-dependent xanthine hydroxylase, XanA, xanthine/alpha-ketoglutarate dioxygenase,
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alpha-ketoglutarate-dependent xanthine hydroxylase
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xanthine/alpha-ketoglutarate dioxygenase
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XanA
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xanthine + 2-oxoglutarate + O2 = urate + succinate + CO2
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-
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xanthine,2-oxoglutarate:oxygen oxidoreductase
Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine.
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9-methylxanthine + 2-oxoglutarate + O2
?
-
-
-
?
xanthine + 2-oxoadipate + O2
?
-
-
-
-
?
xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
additional information
?
-
-
no activity with pyruvate, 2-oxobutyrate, phenyl pyruvate, and 4-hydroxyphenyl pyruvate
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-
?
xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
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-
-
?
xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
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the enzyme is highly specific for xanthine. On the basis of the spectroscopic assay using standard conditions with 12 nM enzyme, no activity is detected when the enzyme is assayed with 0.08, 0.1, or 0.2 mM hypoxanthine, 1-methylxanthine, 3-methylxanthine, 7-methylxanthine, 9-methylxanthine, purine, 6-methylpurine, 2-hydroxypurine, 8-hydroxypurine, 2,8-dihydroxypurine, 2-hydroxy-6-methylpurine, allopurinol, allantoin, or adenosine diphosphate
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?
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xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
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-
-
?
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Fe2+
Fe2+-dependent enzyme
Fe2+
non-heme mononuclear Fe(II) enzyme
Fe2+
-
reqired. Half-maximal activity at 0.007 mM when the recombinant apoprotein isolated from the Escherichia coli is used
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Co2+
-
0.04 mM, about 65% inhibition
Cu2+
-
0.04 mM, complete inhibition
Fe2+
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depending on the experimental conditions, Fe2+ concentrations of above 0.025 mM can lead to enzyme inhibition of the recombinant enzyme isolated from Escherichia coli, whereas the enzyme from Aspergillus nidulans is not inhibited at Fe2+ concentrations up to 0.080 mM
Mn2+
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0.04 mM, about 80% inhibition
N-oxalylglycine
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competes with 2-oxoglutarate
NaCl
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0.5 M NaCl increases the Km of 2-oxoglutarate, increases the Km of xanthine and decreased the kcat
Zn2+
-
0.04 mM, complete inhibition
6,8-dihydroxypurine
slow-binding competitive inhibitor
6,8-dihydroxypurine
-
0.08 mM, 24% decrease in activity
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0.16
2-oxoadipate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.031 - 0.059
2-oxoglutarate
0.4 - 1.09
9-methylxanthine
additional information
2-oxoglutarate
0.047
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme C357A
0.059
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q101A
0.053
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme D138A
0.05
2-oxoglutarate
-
30°C, pH 7.4, enzyme isolated from Aspergillus nidulans
0.048
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme N358A
0.042
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q356A
0.041
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme E137A
0.032
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme K122A
0.0311
2-oxoglutarate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.031
2-oxoglutarate
pH 7.4, 25°C, wild-type enzyme
1
9-methylxanthine
pH 7.4, 25°C, mutant enzyme N358A
0.88
9-methylxanthine
pH 7.4, 25°C, mutant enzyme K122A
0.78
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q101A
1.09
9-methylxanthine
pH 7.4, 25°C, mutant enzyme E137A
0.68
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q356A
0.58
9-methylxanthine
pH 7.4, 25°C, mutant enzyme D138A
0.55
9-methylxanthine
pH 7.4, 25°C, mutant enzyme C357A
0.4
9-methylxanthine
pH 7.4, 25°C, wild-type enzyme
0.122
xanthine
pH 7.4, 25°C, mutant enzyme Q101A
0.088
xanthine
pH 7.4, 25°C, mutant enzyme K122A
0.071
xanthine
pH 7.4, 25°C, mutant enzyme E137A
0.069
xanthine
pH 7.4, 25°C, mutant enzyme D138A
0.554
xanthine
pH 7.4, 25°C, mutant enzyme N358A
0.058
xanthine
pH 7.4, 25°C, mutant enzyme C357A
0.057
xanthine
pH 7.4, 25°C, mutant enzyme Q356A
0.046
xanthine
-
30°C, pH 7.4, enzyme isolated from Aspergillus nidulans
0.0452
xanthine
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.045
xanthine
pH 7.4, 25°C, wild-type enzyme
additional information
2-oxoglutarate
KM-value determined in crude extract: 0.05 mM
additional information
xanthine
KM-value determined in crude extract: 0.023 mM
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7.6
2-oxoadipate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.66 - 5.9
9-methylxanthine
67
2-oxoglutarate
pH 7.4, 25°C, wild-type enzyme
66.5
2-oxoglutarate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
42
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme K122A
2 - 8
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q356A
31
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme E137A
25
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme D138A
21
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q101A
19
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme C357A
17
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme N358A
15 - 30
2-oxoglutarate
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30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans
1.26
9-methylxanthine
pH 7.4, 25°C, mutant enzyme N358A
5.9
9-methylxanthine
pH 7.4, 25°C, mutant enzyme E137A
4.5
9-methylxanthine
pH 7.4, 25°C, mutant enzyme C357A
4.25
9-methylxanthine
pH 7.4, 25°C, mutant enzyme D138A
3.8
9-methylxanthine
pH 7.4, 25°C, wild-type enzyme
0.66
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q101A
1.4
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q356A
1.9
9-methylxanthine
pH 7.4, 25°C, mutant enzyme K122A
72
xanthine
pH 7.4, 25°C, wild-type enzyme
15 - 30
xanthine
-
30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans
71.4
xanthine
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25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
60
xanthine
pH 7.4, 25°C, mutant enzyme K122A
40
xanthine
pH 7.4, 25°C, mutant enzyme E137A
38
xanthine
pH 7.4, 25°C, mutant enzyme N358A
35
xanthine
pH 7.4, 25°C, mutant enzyme Q356A
34
xanthine
pH 7.4, 25°C, mutant enzyme D138A
32
xanthine
pH 7.4, 25°C, mutant enzyme C357A
3 - 6
xanthine
pH 7.4, 25°C, mutant enzyme Q101A
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340 - 2160
2-oxoglutarate
850 - 9500
9-methylxanthine
340
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme N358A
360
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q101A
400
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme C357A
470
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme D138A
2160
2-oxoglutarate
pH 7.4, 25°C, wild-type enzyme
670
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme Q356A
760
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme E137A
1310
2-oxoglutarate
pH 7.4, 25°C, mutant enzyme K122A
9500
9-methylxanthine
pH 7.4, 25°C, wild-type enzyme
8180
9-methylxanthine
pH 7.4, 25°C, mutant enzyme C357A
7330
9-methylxanthine
pH 7.4, 25°C, mutant enzyme D138A
5410
9-methylxanthine
pH 7.4, 25°C, mutant enzyme E137A
2160
9-methylxanthine
pH 7.4, 25°C, mutant enzyme K122A
2050
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q356A
1260
9-methylxanthine
pH 7.4, 25°C, mutant enzyme N358A
850
9-methylxanthine
pH 7.4, 25°C, mutant enzyme Q101A
1600
xanthine
pH 7.4, 25°C, wild-type enzyme
680
xanthine
pH 7.4, 25°C, mutant enzyme K122A
610
xanthine
pH 7.4, 25°C, mutant enzyme Q356A
560
xanthine
pH 7.4, 25°C, mutant enzyme E137A
550
xanthine
pH 7.4, 25°C, mutant enzyme C357A
490
xanthine
pH 7.4, 25°C, mutant enzyme D138A
300
xanthine
pH 7.4, 25°C, mutant enzyme Q101A
70
xanthine
pH 7.4, 25°C, mutant enzyme N358A
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0.00012
N-oxalylglycine
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pH 7.4, 25°C
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7
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enzyme isolated from Aspergillus nidulans
7 - 8
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the recombinant enzyme isolated from Escherichia coli exhibits a narrow pH optimum of 7.0-8.0 with pH 7.4 yielding optimal activity for Tris, MOPS, MES, imidazole, and HEPES buffers
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UniProt
brenda
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brenda
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UniProt
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brenda
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XANA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
370
0
41305
Swiss-Prot
other Location (Reliability: 4 )
XANA_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
420
0
46410
Swiss-Prot
other Location (Reliability: 2 )
XANA_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
413
0
46604
Swiss-Prot
other Location (Reliability: 2 )
XANA_EMEND
370
0
41305
Swiss-Prot
other Location (Reliability: 4 )
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40000
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12 * 40000, SDS-PAGE
500000
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dodecamer, gel filtration
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dodecamer
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12 * 40000, SDS-PAGE
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glycoprotein
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presence of O-glycosylation as well as N-glycosylation
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C357A
enhanced activity towards 9-methylxanthine as compared to wild-type enzyme. Mutant enzyme is resistant rto thiol-specific reagents that inactivated wild-type enzyme. Elevated ferroxidase activity in the absence of substrates
D138A
enhanced activity towards 9-methylxanthine as compared to wild-type enzyme. Significant decrease in Ki(app) for 6,8-dihydroxypurine
D151A
inactive mutant enzyme
E137A
enhanced activity towards 9-methylxanthine as compared to wild-type enzyme. Significant decrease in Ki(app) for 6,8-dihydroxypurine
H149A
inactive mutant enzyme
H340A
mutant enzyme exhibits 0.17% of the wild-type enzyme activity
K122A
2fold increase in the Kd of 2-oxoglutarate compared to wild-type enzyme
N358A
23fold decrease in kcat/Km compared to wild-type enzyme. Significant decrease in Ki(app) for 6,8-dihydroxypurine
Q101A
elevated ferroxidase activity in the absence of substrates
Q356A
significant decrease in Ki(app) for 6,8-dihydroxypurine. Elevated ferroxidase activity in the absence of substrates
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-80°C, stable for at least 2 months
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4°C, stored in 100 mM Tris buffer (pH 7) containing 300 mM NaCl, 250 mM imidazole, 15% glycerol, and 0.005 mM Fe2+, concentrated enzyme is stable for at least 5 months
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4°C, stored in 100 mM Tris buffer (pH 8.0) containing 300 mM NaCl, 250 mM imidazole, 1 mM EDTA, and 15% glycerol, stable for at least 1 month
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purified from both the fungal mycelium and recombinant Escherichia coli cells
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wild-type enzyme variants are purified from recombinant Escherichia coli cells
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overproduction of His6-tagged enzyme in Aspergillus nidulans and Escherichia coli
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wild-type and mutant enzymes
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Li, M.; Muller, T.A.; Fraser, B.A.; Hausinger, R.P.
Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans
Arch. Biochem. Biophys.
470
44-53
2008
Aspergillus nidulans (Q4QZZ9)
brenda
Montero-Moran, G.M.; Li, M.; Rendon-Huerta, E.; Jourdan, F.; Lowe, D.J.; Stumpff-Kane, A.W.; Feig, M.; Scazzocchio, C.; Hausinger, R.P.
Purification and characterization of the FeII- and alpha-ketoglutarate-dependent xanthine hydroxylase from Aspergillus nidulans
Biochemistry
46
5293-5304
2007
Aspergillus nidulans
brenda
Cultrone, A.; Scazzocchio, C.; Rochet, M.; Montero-Moran, G.; Drevet, C.; Fernandez-Martin, R.
Convergent evolution of hydroxylation mechanisms in the fungal kingdom: molybdenum cofactor-independent hydroxylation of xanthine via alpha-ketoglutarate-dependent dioxygenases
Mol. Microbiol.
57
276-290
2005
Aspergillus nidulans (Q4QZZ9)
brenda
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