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Literature summary for 1.17.1.4 extracted from

  • Neumann, M.; Schulte, M.; Juenemann, N.; Stoecklein, W.; Leimkuehler, S.
    Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase (2006), J. Biol. Chem., 281, 15701-15708.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Cofactor

Cofactor Comment Organism Structure
molybdopterin protein XdhC binds molybdenum cofactor in stoichiometric amounts, which subsequently can be inserted into molybdenum-free apoxanthine dehydrogenase. Protein XdhC is required for the stabilization of the sulfurated form of molybdenum cofactor Rhodobacter capsulatus