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Literature summary for 1.17.1.4 extracted from

  • Tsujii, A.; Nishino, T.
    Mechanism of transition from xanthine dehydrogenase to xanthine oxidase: Effect of guanidine-HCl or urea on the activity (2008), Nucleosides Nucleotides Nucleic Acids, 27, 881-887.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C535A/C992R/C1316S mutation in residues involved in conversion of xanthin dehydrogenase to xanthine oxidase by formation of disulfide bonds. Using guanidine-HCl, the mutant can be converted into the oxidase form Rattus norvegicus

General Stability

General Stability Organism
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Rattus norvegicus
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
Guanidine-HCl conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M gunandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis Bos taurus
Guanidine-HCl conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Rattus norvegicus
Urea conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Rattus norvegicus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Rattus norvegicus
conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant. Above 3 M guandine-HCl, even xanthine oxidase activity decreases drastically, but the xanthine oxidase form treated with 1.5 M can be completely reconverted into xanthine dehydrogenase by dialysis Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-
milk
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Rattus norvegicus ?
-
?
additional information conversion of xanthine oxidoreductase from dehydrogenase to oxidase form occurs in the presence of guanidine-HCl or urea. Both forms are in a thermodynamic equilibrium that can be shifted by disruption of the stabilizing amino acid cluster with a denaturant Bos taurus ?
-
?