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Information on EC 1.14.11.48 - xanthine dioxygenase
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1.14.11.48 xanthine dioxygenaseIUBMB Comments
Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine.
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The enzyme appears in viruses and cellular organisms
Synonyms
alpha-ketoglutarate-dependent xanthine hydroxylase, XanA, xanthine/alpha-ketoglutarate dioxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
XanA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xanthine + 2-oxoglutarate + O2 = urate + succinate + CO2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
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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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
additional information
?
-
-
no activity with pyruvate, 2-oxobutyrate, phenyl pyruvate, and 4-hydroxyphenyl pyruvate
-
-
?
xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
-
-
-
?
xanthine + 2-oxoglutarate + O2
urate + succinate + CO2
-
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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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
reqired. Half-maximal activity at 0.007 mM when the recombinant apoprotein isolated from the Escherichia coli is used
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+
-
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
NaCl
-
0.5 M NaCl increases the Km of 2-oxoglutarate, increases the Km of xanthine and decreased the kcat
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
2-oxoadipate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.0311
2-oxoglutarate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.05
2-oxoglutarate
-
30°C, pH 7.4, enzyme isolated from Aspergillus nidulans
0.0452
xanthine
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
0.046
xanthine
-
30°C, pH 7.4, enzyme isolated from Aspergillus nidulans
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.6
2-oxoadipate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
15 - 30
2-oxoglutarate
-
30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans
66.5
2-oxoglutarate
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
15 - 30
xanthine
-
30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans
71.4
xanthine
-
25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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). XANA_EMEND
370
0
41305
Swiss-Prot
other Location (Reliability: 4)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E137A
enhanced activity towards 9-methylxanthine as compared to wild-type enzyme. Significant decrease in Ki(app) for 6,8-dihydroxypurine
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
Q356A
significant decrease in Ki(app) for 6,8-dihydroxypurine. Elevated ferroxidase activity in the absence of substrates
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from both the fungal mycelium and recombinant Escherichia coli cells
-
wild-type enzyme variants are purified from recombinant Escherichia coli cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction of His6-tagged enzyme in Aspergillus nidulans and Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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