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Literature summary extracted from

  • Romao, M.J.; Archer, M.; Moura, I.; Moura, J.J.G.; Legall, J.; Engh, R.; Schneider, M.; Hof, P.; Huber, R.
    Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas (1995), Science, 270, 1170-1176.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.3.2 2.25 A resolution, enzyme contains a molybdoptererin cofactor and two different [2Fe-2S] centers, enzyme is folded into four domains, the first two bind the iron sulfur centers, the last two are involved in molybtopterin binding Megalodesulfovibrio gigas

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.3.2 Iron iron-molybdenum protein Megalodesulfovibrio gigas
1.17.3.2 Molybdenum an iron-molybdenum protein Megalodesulfovibrio gigas

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Megalodesulfovibrio gigas
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information
-
 Megalodesulfovibrio gigas
1.17.3.2 proteolytic modification
-
 Megalodesulfovibrio gigas

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 hypoxanthine + 2 H2O + 2 O2
-
 Megalodesulfovibrio gigas urate + 2 H2O2
-
 ?
1.17.3.2 xanthine + H2O + O2 electron acceptor O2 Megalodesulfovibrio gigas uric acid + H2O2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Megalodesulfovibrio gigas