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Literature summary for 1.17.3.2 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

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

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged XDH1 in Pichia pastoris Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
allopurinol
-
Arabidopsis thaliana
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

Metals/Ions Comment Organism Structure
Fe a molybdenum-iron-flavoenzyme Arabidopsis thaliana
Mo a molybdenum-iron-flavoenzyme Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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% ?
-
?
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% ?
-
?
xanthine + O2 + H2O Arabidopsis thaliana
-
urate + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
Arabidopsis thaliana

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged XDH1 from Pichia pastoris by nickel affinity and anion exchange chromatography Arabidopsis thaliana

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
xanthine + O2 + H2O
-
Arabidopsis thaliana urate + H2O2
-
?

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
xanthine oxidoreductase
-
Arabidopsis thaliana
XOR
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6
-
substrate NADH Arabidopsis thaliana
8
-
substrate xanthine Arabidopsis thaliana

pH Range

pH Minimum pH Maximum Comment Organism
6.6 8
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
FAD a molybdenum-iron-flavoenzyme Arabidopsis thaliana
molybdenum cofactor C-terminal Arabidopsis thaliana
additional information negligible reactivity toward NAD+ Arabidopsis thaliana
[2Fe-2S] cluster two N-terminal non-identical iron-sulfur clusters of the [2Fe-2S]-type Arabidopsis thaliana

General Information

General Information Comment Organism
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