Biology:FAD-dependent urate hydroxylase

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Short description: Class of enzymes
FAD-dependent urate hydroxylase
Identifiers
EC number1.14.13.113
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 + FADH + H+ + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 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. 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. PMID 18849434. PMC 2593211. http://diposit.ub.edu/dspace/bitstream/2445/33551/1/561935.pdf. 
  3. "Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO". Environmental Microbiology Reports 4 (6): 642–647. 2012. doi:10.1111/j.1758-2229.2012.00390.x. PMID 23760935. 

External links