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Class of enzymes
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
⇌
{\displaystyle \rightleftharpoons }
5-hydroxyisourate + FAD+ + H2 O
References
^ 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 .
^ 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 .
^ 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 .
External links
Activity Regulation Classification Kinetics Types