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Literature summary extracted from

  • Michiel, M.; Perchat, N.; Perret, A.; Tricot, S.; Papeil, A.; Besnard, M.; de Berardinis, V.; Salanoubat, M.; Fischer, C.
    Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO (2012), Environ. Microbiol. Rep., 4, 642-647.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.113 expressed in Acinetobacter baylyi strain ADP1 Xanthomonas campestris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.113 0.024
-
 NADH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 0.029
-
 Urate in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 0.055
-
 NADPH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.113 52000
-
 2 * 52000, SDS-PAGE Xanthomonas campestris
1.14.13.113 52519
-
 2 * 52519, calculated from amino acid sequence Xanthomonas campestris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.113 urate + NADH + H+ + O2 Xanthomonas campestris the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH 5-hydroxyisourate + NAD+ + H2O
-
 ?
1.14.13.113 urate + NADPH + H+ + O2 Xanthomonas campestris the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH 5-hydroxyisourate + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.113 Xanthomonas campestris Q8PDQ6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.113 urate + NADH + H+ + O2 the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH Xanthomonas campestris 5-hydroxyisourate + NAD+ + H2O
-
 ?
1.14.13.113 urate + NADPH + H+ + O2 the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH Xanthomonas campestris 5-hydroxyisourate + NADP+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.113 homodimer 2 * 52000, SDS-PAGE Xanthomonas campestris
1.14.13.113 homodimer 2 * 52519, calculated from amino acid sequence Xanthomonas campestris

Synonyms

EC Number Synonyms Comment Organism
1.14.13.113 HpxO
-
 Xanthomonas campestris
1.14.13.113 HpyO isoform Xanthomonas campestris
1.14.13.113 urate hydroxylase
-
 Xanthomonas campestris
1.14.13.113 XCC0279
-
 Xanthomonas campestris

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.113 0.19
-
 NADH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 1.06
-
 Urate in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 1.14
-
 NADPH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.113 FAD dependent on, cannot be replaced by FMN nor by riboflavin Xanthomonas campestris
1.14.13.113 NADH the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH Xanthomonas campestris
1.14.13.113 NADPH the enzyme is slightly more efficient (about 2.6times) with NADPH than NADH Xanthomonas campestris

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.13.113 7.9
-
 NADH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 21
-
 NADPH in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris
1.14.13.113 37
-
 Urate in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C Xanthomonas campestris