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Literature summary for 1.17.1.4 extracted from

  • Ishikita, H.; Eger, B.T.; Okamoto, K.; Nishino, T.; Pai, E.F.
    Protein conformational gating of enzymatic activity in xanthine oxidoreductase (2012), J. Am. Chem. Soc., 134, 999-1009.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution crystal structure of XDH at 1.65 A resolution confirms the overall fold of the dimeric protein, the location of the cofactors and the mobile stretches of the polypeptide chain. Crystal structures of the NAD(H) complexes of XDH reveal that, given the proper oxidation states, the nicotinamide rings of the dinucleotides locate at van der Waals distance to the flavin ring Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P80457
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-

Subunits

Subunits Comment Organism
dimer crystal structure Bos taurus

Synonyms

Synonyms Comment Organism
xanthine dehydrogenase
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Bos taurus
XDH
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Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH crystal structures of the NAD(H) complexes of XDH reveal that, given the proper oxidation states, the nicotinamide rings of the dinucleotides locate at van der Waals distance to the flavin ring Bos taurus