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Literature summary extracted from

  • Enroth, C.; Eger, B.T.; Okamoto, K.; Nishino, T.; Nishino, T.; Pai, E.F.
    Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion (2000), Proc. Natl. Acad. Sci. USA, 97, 10723-10728.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.1.4 thiol active compounds reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.1.4 2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor Bos taurus
1.17.3.2 2.5 A resolution, each enzyme subunit is composed of an N-terminal 20000 Da domain containing two iron sulfur centers, a central 40000 Da FAD domain and a C-terminal 85000 molybdopterin binding domain, the four redox centers are aligned in a linear fashion Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.1.4 Iron-sulfur-center 2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain Bos taurus
1.17.1.4 molybdenum-center C-terminal 85 kDa molybdopterin-binding domain Bos taurus
1.17.3.2 Iron iron-molybdenum protein Bos taurus
1.17.3.2 Molybdenum an iron-molybdenum protein Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.1.4 145000
-
2 * 145000, data from crystallization Bos taurus
1.17.1.4 290000
-
-
Bos taurus

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 Bos taurus
-
xanthine + NADH + H+
-
?
1.17.1.4 xanthine + NAD+ + H2O Bos taurus
-
urate + NADH
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Bos taurus
-
-
-
1.17.3.2 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information reversible conversion of xanthine dehydrogenase to xanthin oxidase can be achieved by modification of Cys535 and Cys992, tryptic proteolysis of xanthine dehydrogenase after Lys551 or pancreatin cleavage after Leu219 and Lys569 results in irreversible transformation to xanthine oxidase Bos taurus
1.17.3.2 proteolytic modification
-
Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.4
-
Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.1.4 milk
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.4 hypoxanthine + NAD+ + H2O
-
Bos taurus xanthine + NADH + H+
-
?
1.17.1.4 xanthine + NAD+ + H2O
-
Bos taurus urate + NADH
-
?
1.17.3.2 hypoxanthine + 2 H2O + 2 O2
-
Bos taurus urate + 2 H2O2
-
?
1.17.3.2 xanthine + H2O + O2 electron acceptor O2 Bos taurus uric acid + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.17.1.4 dimer 2 * 145000, data from crystallization Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.4 FAD one FAD per subunit, central 40 kDa FAD-domain Bos taurus
1.17.1.4 additional information
-
Bos taurus
1.17.1.4 NAD+
-
Bos taurus
1.17.3.2 FAD flavoprotein Bos taurus
1.17.3.2 molybdopterin one cofactor per subunit, oxidation of xanthine takes place at this center, electrons are rapidly distributed to the other centers by intramolecular electron transfer Bos taurus