Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Environmental Microbiology Reports Année : 2012

Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO

Nadia Perchat
  • Fonction : Auteur
  • PersonId : 920751
Alain Perret
Sabine Tricot
  • Fonction : Auteur
  • PersonId : 920749
Véronique de Berardinis
Marcel Salanoubat
Cécile Fischer

Résumé

In aerobic cells, urate is oxidized to 5-hydroxyisourate by two distinct enzymes: a coenzyme-independent urate oxidase (EC 1.7.3.3) found in eukaryotes and bacteria like Bacillus subtilis and a prokaryotic flavoprotein urate hydroxylase (HpxO) originally found in some Klebsiella species. More cases of analogous or non-homologous isofunctional enzymes (NISE) for urate catabolism have been hypothesized by inspecting bacterial genomes. Here, we used a functional complementation approach in which a candidate gene for urate oxidation is integrated by homologous recombination in the Acinetobacter baylyi ADP1 genome at the locus of its original hpxO gene. Catabolism of urate was restored in A. baylyi ADP1 expressing a FAD-dependent protein from Xanthomonas campestris, representing a new urate hydroxylase family that we called HpyO. This enzyme was kinetically characterized and compared with other HpxO enzymes. In contrast to the latter, HpyO is a typical Michaelian enzyme. This work provides the first experimental evidences for the function of HpyO in bacterial urate catabolism and establishes it as a NISE of HpxO.

Dates et versions

hal-02503747 , version 1 (10-03-2020)

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Magalie Michiel, Nadia Perchat, Alain Perret, Sabine Tricot, Aude Papeil, et al.. Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO. Environmental Microbiology Reports, 2012, pp.n/a-n/a. ⟨10.1111/j.1758-2229.2012.00390.x⟩. ⟨hal-02503747⟩
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