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Literature summary extracted from

  • Kramer, S.P.; Johnson, J.L.; Ribeiro, A.A.; Millington, D.S.; Rajagopalan, K.V.
    The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase (1987), J. Biol. Chem., 262, 16357-16363.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.3.1 Di-(carboxamidomethyl)molybdopterin
-
Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.1 Mo molybdohemoprotein, structure of molybdopterin Gallus gallus
1.17.3.2 Iron iron-molybdenum protein Bos taurus
1.17.3.2 Molybdenum molybdenum cofactor is a complex between molybdenum and molybdopterin (a 6-alkylpterin with 4-carbon side chain which has an enedithiol at carbon 1' and 2', a hydroxyl at carbon 3', and a terminal phosphate group) Bos taurus
1.17.3.2 Molybdenum an iron-molybdenum protein Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.1 Gallus gallus
-
-
-
1.17.3.2 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.3.2 additional information
-
Bos taurus
1.17.3.2 proteolytic modification
-
Bos taurus

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.3.2 FAD flavoprotein Bos taurus