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Literature summary for 1.7.3.3 extracted from

  • Doll, C.; Bell, A.F.; Power, N.; Tonge, P.J.; Tipton, P.A.
    Procatalytic ligand strain. Ionization and perturbation of 8-nitroxanthine at the urate oxidase active site (2005), Biochemistry, 44, 11440-11446.
    View publication on PubMed
Search for more literature for 1.7.3.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
F179A decreases Vmax by 2 orders of magnitude Bacillus subtilis
F179Y mutation decreases Vmax by 2-fold Bacillus subtilis
K9M mutant is not able to generate the dianion of urate and is decreased in activity by over 200-fold Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
8-nitroxanthine
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0000135
-
 Urate mutant enzyme K9M, apparent Km in air-saturated buffer Bacillus subtilis
0.00002
-
 Urate mutant enzyme F179A, apparent Km in air-saturated buffer Bacillus subtilis
0.00156
-
 Urate mutant enzyme F179Y, apparent Km in air-saturated buffer Bacillus subtilis
0.0034
-
 Urate wild type enzyme, apparent Km in air-saturated buffer Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
urate + O2 + H2O
-
 Bacillus subtilis 5-hydroxyisourate + H2O2
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0021
-
 8-nitroxanthine competitive inhibitor versus urate at pH 8.0 Bacillus subtilis