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Literature summary for 1.14.11.48 extracted from

  • 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 (2007), Biochemistry, 46, 5293-5304.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
overproduction of His6-tagged enzyme in Aspergillus nidulans and Escherichia coli Aspergillus nidulans

Inhibitors

Inhibitors Comment Organism Structure
6,8-dihydroxypurine 0.08 mM, 24% decrease in activity Aspergillus nidulans
Co2+ 0.04 mM, about 65% inhibition Aspergillus nidulans
Cu2+ 0.04 mM, complete inhibition Aspergillus nidulans
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 Aspergillus nidulans
Mn2+ 0.04 mM, about 80% inhibition Aspergillus nidulans
N-oxalylglycine competes with 2-oxoglutarate Aspergillus nidulans
NaCl 0.5 M NaCl increases the Km of 2-oxoglutarate, increases the Km of xanthine and decreased the kcat Aspergillus nidulans
Zn2+ 0.04 mM, complete inhibition Aspergillus nidulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0311
-
 2-oxoglutarate 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans
0.0452
-
 xanthine 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans
0.046
-
 xanthine 30°C, pH 7.4, enzyme isolated from Aspergillus nidulans Aspergillus nidulans
0.05
-
 2-oxoglutarate 30°C, pH 7.4, enzyme isolated from Aspergillus nidulans Aspergillus nidulans
0.16
-
 2-oxoadipate 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ reqired. Half-maximal activity at 0.007 mM when the recombinant apoprotein isolated from the Escherichia coli is used Aspergillus nidulans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 12 * 40000, SDS-PAGE Aspergillus nidulans
500000
-
 dodecamer, gel filtration Aspergillus nidulans

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein presence of O-glycosylation as well as N-glycosylation Aspergillus nidulans

Purification (Commentary)

Purification (Comment) Organism
purified from both the fungal mycelium and recombinant Escherichia coli cells Aspergillus nidulans

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
 Aspergillus nidulans
-

Storage Stability

Storage Stability Organism
-80°C, stable for at least 2 months Aspergillus nidulans
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 Aspergillus nidulans
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 Aspergillus nidulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with pyruvate, 2-oxobutyrate, phenyl pyruvate, and 4-hydroxyphenyl pyruvate Aspergillus nidulans ?
-
 ?
xanthine + 2-oxoadipate + O2
-
 Aspergillus nidulans ?
-
 ?
xanthine + 2-oxoglutarate + O2 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 Aspergillus nidulans urate + succinate + CO2
-
 ?

Subunits

Subunits Comment Organism
dodecamer 12 * 40000, SDS-PAGE Aspergillus nidulans

Synonyms

Synonyms Comment Organism
XanA
-
 Aspergillus nidulans
xanthine/alpha-ketoglutarate dioxygenase
-
 Aspergillus nidulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.6
-
 2-oxoadipate 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans
15 30 2-oxoglutarate 30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans Aspergillus nidulans
15 30 xanthine 30°C, pH 7.4, value depending on preparation, enzyme isolated from Aspergillus nidulans Aspergillus nidulans
66.5
-
 2-oxoglutarate 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans
71.4
-
 xanthine 25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli Aspergillus nidulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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 Aspergillus nidulans
7
-
 enzyme isolated from Aspergillus nidulans Aspergillus nidulans

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 11 stable Aspergillus nidulans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00012
-
 N-oxalylglycine pH 7.4, 25°C Aspergillus nidulans