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Literature summary for 1.17.3.2 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
Search for more literature for 1.17.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Metals/Ions Comment Organism Structure
Iron iron-molybdenum protein Bos taurus
Molybdenum an iron-molybdenum protein Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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
proteolytic modification
-
 Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + 2 H2O + 2 O2
-
 Bos taurus urate + 2 H2O2
-
 ?
xanthine + H2O + O2 electron acceptor O2 Bos taurus uric acid + H2O2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Bos taurus
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