Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.113 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
Search for more literature for 1.14.13.113

Cloned(Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Xanthomonas campestris Q8PDQ6
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Turnover Number [1/s]

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

Cofactor

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

kcat/KM [mM/s]

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