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Literature summary extracted from

  • Amini, K.; Sorouraddin, M.; Rashidi, M.
    Activity and stability of rat liver xanthine oxidase in the presence of pyridine (2011), Can. J. Chem., 89, 1-7.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.3.2 Pyridine highly reduced activity of xanthine oxidase in the presence of pyridine, overview Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.3.2 additional information
-
additional information thermodynamics and kinetics of xanthine oxidase in the presence of pyridine, Km for xanthine is increased 4.8fold and Vmax is reduced 1.8fold at 0.5% pyridine, overview Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.3.2 xanthine + H2O + O2 Rattus norvegicus
-
urate + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.17.3.2 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.3.2 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.3.2 xanthine + H2O + O2
-
Rattus norvegicus urate + H2O2
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.17.3.2 additional information
-
the thermostability of xanthine oxidase in the presence of pyridine is highly increased compared to the unbound enzyme, overview Rattus norvegicus