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FAD-dependent urate hydroxylase

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Class of enzymes
FAD-dependent urate hydroxylase
Identifiers
EC no.1.14.13.113
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FAD-dependent urate hydroxylase (EC 1.14.13.113, HpxO enzyme, FAD-dependent urate oxidase, urate hydroxylase) is an enzyme with systematic name urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming). A non-homologous isofunctional enzyme (NISE) to HpxO was found, and named HpyO. HpyO was determined to be a typical Michaelian enzyme. These FAD-dependent urate hydroxylases are flavoproteins.

This enzyme catalyses the following chemical reaction

urate + FADH + H + O2 {\displaystyle \rightleftharpoons } 5-hydroxyisourate + FAD + H2O

References

  1. O'Leary, S.E.; Hicks, K.A.; Ealick, S.E.; Begley, T.P. (2009). "Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase". Biochemistry. 48 (14): 3033–3035. doi:10.1021/bi900160b. PMC 2842088. PMID 19260710.
  2. de la Riva L; Badia J; Aguilar J; Bender RA; Baldoma L. (2008). "The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: gene organization and transcriptional regulation" (PDF). Journal of Bacteriology. 190 (24): 7892–7903. doi:10.1128/JB.01022-08. PMC 2593211. PMID 18849434.
  3. Michiel M, Perchat N, Perret A, Tricot S, Papeil A, Besnard M, de Berardinis V, Salanoubat M, Fischer C (2012). "Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO". Environmental Microbiology Reports. 4 (6): 642–647. doi:10.1111/j.1758-2229.2012.00390.x. PMID 23760935.

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Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate
1.14.13: NADH or NADPH
1.14.14: reduced flavin or flavoprotein
1.14.15: reduced iron–sulfur protein
1.14.16: reduced pteridine (BH4 dependent)
1.14.17: reduced ascorbate
1.14.18-19: other
1.14.99 - miscellaneous
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