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| Name = FAD-dependent urate hydroxylase
| EC_number = 1.14.13.113
| CAS_number =
| IUBMB_EC_number = 1/14/13/113
| GO_code =
| image =
| width =
| caption =
}}FAD-dependent urate hydroxylase ({{EC number|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+ + O25-hydroxyisourate + FAD+ + H2O
References
1. ^{{cite journal | title = Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase |author1 = O'Leary, S.E. |author2 =Hicks, K.A. |author3 =Ealick, S.E. |author4 =Begley, T.P. |journal = Biochemistry |year = 2009 |volume = 48 |pages = 3033–3035 |pmid = 19260710 |doi=10.1021/bi900160b |issue=14 |pmc=2842088}}
2. ^{{cite journal | title = The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: gene organization and transcriptional regulation |author1 = de la Riva L |author2 =Badia J |author3 =Aguilar J |author4 =Bender RA |author5 =Baldoma L. |journal = Journal of Bacteriology |year = 2008 |volume = 190 |pages = 7892–7903 |pmid=18849434 |doi=10.1128/JB.01022-08 |issue=24 |pmc=2593211|url=http://diposit.ub.edu/dspace/bitstream/2445/33551/1/561935.pdf }}
3. ^{{cite journal | title = Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO |vauthors = Michiel M, Perchat N, Perret A, Tricot S, Papeil A, Besnard M, de Berardinis V, Salanoubat M, Fischer C |journal = Environmental Microbiology Reports |year = 2012 |volume = 4 |pages = 642–647 |pmid=23760935 |doi=10.1111/j.1758-2229.2012.00390.x |issue=6}}
2. ^{{cite journal | title = The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: gene organization and transcriptional regulation |author1 = de la Riva L |author2 =Badia J |author3 =Aguilar J |author4 =Bender RA |author5 =Baldoma L. |journal = Journal of Bacteriology |year = 2008 |volume = 190 |pages = 7892–7903 |pmid=18849434 |doi=10.1128/JB.01022-08 |issue=24 |pmc=2593211|url=http://diposit.ub.edu/dspace/bitstream/2445/33551/1/561935.pdf }}
3. ^{{cite journal | title = Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO |vauthors = Michiel M, Perchat N, Perret A, Tricot S, Papeil A, Besnard M, de Berardinis V, Salanoubat M, Fischer C |journal = Environmental Microbiology Reports |year = 2012 |volume = 4 |pages = 642–647 |pmid=23760935 |doi=10.1111/j.1758-2229.2012.00390.x |issue=6}}
External links
- {{MeshName|FAD-dependent+urate+hydroxylase}}
1 : EC 1.14.13