FAD-dependent urate hydroxylase

FAD-dependent urate hydroxylase
Identifiers
EC number 1.14.13.113
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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 + NADH + H+ + O2 5-hydroxyisourate + NAD+ + 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 2842088Freely accessible. 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". Journal of Bacteriology. 190 (24): 7892–7903. doi:10.1128/JB.01022-08. PMC 2593211Freely accessible. 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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