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FAD-dependent urate hydroxylase
Identifiers
EC no. 1.14.13.113
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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NCBI proteins

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). [1] [2] A non-homologous isofunctional enzyme (NISE) to HpxO was found, and named HpyO. [3] 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 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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