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Literature summary extracted from

  • Zarepour, M.; Kaspari, K.; Stagge, S.; Rethmeier, R.; Mendel, R.R.; Bittner, F.
    Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity (2009), Plant Mol. Biol., 72, 301-310.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.1.4 sulfide/dithionite treatment increases the specific activity of AtXDH1 Arabidopsis thaliana
1.17.3.2 sulfide/dithionite treatment increases the specific activity of AtXDH1 Arabidopsis thaliana

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.1.4 expression of His-tagged wild-type and mutant XDH1 variants in Pichia pastoris strain KM71 Arabidopsis thaliana
1.17.1.4 expression of His-tagged XDH1 in Pichia pastoris Arabidopsis thaliana
1.17.3.2 expression of His-tagged XDH1 in Pichia pastoris Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.17.1.4 E1297A site-directed mutagenis Arabidopsis thaliana
1.17.1.4 E831A site-directed mutagenis Arabidopsis thaliana
1.17.1.4 R909A site-directed mutagenis Arabidopsis thaliana
1.17.1.4 W364A site-directed mutagenis Arabidopsis thaliana
1.17.1.4 Y421A site-directed mutagenis Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.1.4 allopurinol
-
 Arabidopsis thaliana
1.17.1.4 additional information NAD+ inhibits NADH-dependent superoxide formation of AtXDH1 Arabidopsis thaliana
1.17.1.4 NADH suppresses NAD+-dependent xanthine oxidation Arabidopsis thaliana
1.17.3.2 allopurinol
-
 Arabidopsis thaliana
1.17.3.2 additional information NAD+ and diphenylene iodonium inhibit NADH-dependent superoxide formation of AtXDH1; NAD+ inhibits NADH-dependent superoxide formation of AtXDH1 Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.1.4 Fe a molybdenum-iron-flavoenzyme Arabidopsis thaliana
1.17.1.4 Iron a molybdenum-iron-flavoenzyme, contains [2Fe-2S] centers Arabidopsis thaliana
1.17.1.4 Mo a molybdenum-iron-flavoenzyme Arabidopsis thaliana
1.17.1.4 Molybdenum a molybdenum-iron-flavo enzyme, which contains a C-terminal molybdenum cofactor-binding domain of 85 kDa Arabidopsis thaliana
1.17.3.2 Fe a molybdenum-iron-flavoenzyme Arabidopsis thaliana
1.17.3.2 Mo a molybdenum-iron-flavoenzyme Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.4 hypoxanthine + NAD+ + H2O Arabidopsis thaliana
-
 xanthine + NADH + H+
-
 ?
1.17.1.4 additional information Arabidopsis thaliana XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% ?
-
 ?
1.17.1.4 xanthine + NAD+ + H2O Arabidopsis thaliana
-
 urate + NADH + H+
-
 ?
1.17.3.2 additional information Arabidopsis thaliana XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% ?
-
 ?
1.17.3.2 additional information Arabidopsis thaliana XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% ?
-
 ?
1.17.3.2 xanthine + O2 + H2O Arabidopsis thaliana
-
 urate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Arabidopsis thaliana
-
-
-
1.17.1.4 Arabidopsis thaliana Q8GUQ8
-
-
1.17.3.2 Arabidopsis thaliana
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.1.4 flavoprotein
-
 Arabidopsis thaliana
1.17.3.2 flavoprotein
-
 Arabidopsis thaliana

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.4 recombinant His-tagged wild-type and mutant XDH1 variants from Pichia pastoris strain KM71 by nickel affinity chromatography and anion exchange chromatography Arabidopsis thaliana
1.17.1.4 recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography Arabidopsis thaliana
1.17.3.2 recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography Arabidopsis thaliana

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.1.4 0.044
-
 purified recombinant enzyme, substrate xanthine, pH 8.0 Arabidopsis thaliana
1.17.1.4 0.65
-
 purified recombinant enzyme, pH 8.0, 25°C Arabidopsis thaliana
1.17.1.4 0.702
-
 purified recombinant enzyme, substrate NADH, pH 6.6 Arabidopsis thaliana
1.17.1.4 1.712
-
 purified recombinant enzyme, in presence of sulfide/dithionite Arabidopsis thaliana
1.17.3.2 0.044
-
 purified recombinant enzyme, substrate xanthine, pH 8.0 Arabidopsis thaliana
1.17.3.2 0.702
-
 purified recombinant enzyme, substrate NADH, pH 6.6 Arabidopsis thaliana
1.17.3.2 1.712
-
 purified recombinant enzyme, in presence of sulfide/dithionite Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.4 hypoxanthine + NAD+ + H2O
-
 Arabidopsis thaliana xanthine + NADH + H+
-
 ?
1.17.1.4 additional information XDH can be converted into XO, EC 1.17.3.2, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% Arabidopsis thaliana ?
-
 ?
1.17.1.4 additional information AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved Arabidopsis thaliana ?
-
 ?
1.17.1.4 additional information by an alternative activity, AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide. In comparison to the specific activity with xanthine as substrate, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher. Each sub-activity is determined by specific conditions such as the availability of substrates and co-substrates, which allows regulation of superoxide production by AtXDH1 Arabidopsis thaliana ?
-
 ?
1.17.1.4 xanthine + NAD+ + H2O
-
 Arabidopsis thaliana urate + NADH + H+
-
 ?
1.17.3.2 additional information XDH, EC 1.17.1.4, can be converted into xanthine oxidase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% Arabidopsis thaliana ?
-
 ?
1.17.3.2 additional information XDH, EC 1.17.1.4, can be converted into xanthine oxidoreductase, XO, either reversibly by oxidation of the sulfhydryl groups of two conserved cysteine residues. Under physiological conditions the XDH form appears to dominate with 80% over the XO form with 20% Arabidopsis thaliana ?
-
 ?
1.17.3.2 additional information AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production and is dependent on sulfurated molybdenum cofactor, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved Arabidopsis thaliana ?
-
 ?
1.17.3.2 additional information AtXDH1 is capable of oxidizing NADH with concomitant formation of NAD+ and superoxide, the specific activity of recombinant AtXDH1 with NADH as substrate is about 15times higher than the activity with xanthine accompanied by a doubling in superoxide production, overview. FAD is crucial for NADH-based superoxide formation of AtXDH1, whereas the molybdenum cofactor has only little or no influence on the activity, residues E831, R909, E1297, W364, and Y421 are involved Arabidopsis thaliana ?
-
 ?
1.17.3.2 xanthine + O2 + H2O
-
 Arabidopsis thaliana urate + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.1.4 homodimer composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa Arabidopsis thaliana
1.17.3.2 homodimer composed of two identical subunits of about 145 kDa, each being subdivided into three domains: a N-terminal iron-sulfur-binding domain of 20 kDa, a 40 kDa domain harboring a FAD-binding site, and a C-terminal molybdenum cofactor-binding domain of 85 kDa Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.17.1.4 AtXDH1
-
 Arabidopsis thaliana
1.17.1.4 More mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO Arabidopsis thaliana
1.17.1.4 xanthine oxidoreductase
-
 Arabidopsis thaliana
1.17.1.4 XDH1
-
 Arabidopsis thaliana
1.17.1.4 XOR
-
 Arabidopsis thaliana
1.17.3.2 xanthine oxidoreductase
-
 Arabidopsis thaliana
1.17.3.2 XOR
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.1.4 25
-
 assay at Arabidopsis thaliana
1.17.3.2 25
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.1.4 6.6
-
 substrate NADH Arabidopsis thaliana
1.17.1.4 8
-
 assay at Arabidopsis thaliana
1.17.1.4 8
-
 substrate xanthine Arabidopsis thaliana
1.17.3.2 6.6
-
 substrate NADH Arabidopsis thaliana
1.17.3.2 8
-
 substrate xanthine Arabidopsis thaliana

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.17.1.4 6.6 8
-
 Arabidopsis thaliana
1.17.3.2 6.6 8
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.4 FAD a molybdenum-iron-flavoenzyme Arabidopsis thaliana
1.17.1.4 FAD a molybdenum-iron-flavoenzyme, activity-to-flavin ratio of 8 with xanthine as substrate and NAD+ as final electron acceptor, recombinant enzyme Arabidopsis thaliana
1.17.1.4 molybdenum cofactor C-terminal Arabidopsis thaliana
1.17.1.4 additional information both NAD+ and NADH compete for the same binding site Arabidopsis thaliana
1.17.1.4 NAD+
-
 Arabidopsis thaliana
1.17.1.4 NAD+ NAD+ inhibits NADH oxidase activity of AtXDH1 Arabidopsis thaliana
1.17.1.4 NADH suppresses NAD+-dependent xanthine oxidation Arabidopsis thaliana
1.17.1.4 [2Fe-2S] cluster two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type Arabidopsis thaliana
1.17.3.2 FAD a molybdenum-iron-flavoenzyme Arabidopsis thaliana
1.17.3.2 molybdenum cofactor C-terminal Arabidopsis thaliana
1.17.3.2 additional information negligible reactivity toward NAD+ Arabidopsis thaliana
1.17.3.2 [2Fe-2S] cluster two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.17.1.4 additional information mammalian XOR exists in two interconvertible forms, the xanthine dehydrogenase, XDH, form and the xanthine oxidase, XO, form. The primary gene product is XDH, which can be converted into XO Arabidopsis thaliana
1.17.1.4 physiological function xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid Arabidopsis thaliana
1.17.1.4 physiological function AtXDH1 is a key enzyme in purine degradation where it oxidizes hypoxanthine to xanthine and xanthine to uric acid Arabidopsis thaliana
1.17.3.2 physiological function xanthine oxidoreductase is a ubiquitous molybdenum-iron-flavo enzyme with a central role in purine catabolism where it catalyzes the oxidation of hypoxanthine to xanthine and of xanthine to uric acid Arabidopsis thaliana