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.
FAD-dependent urate hydroxylase | |||||||||
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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 | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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This enzyme catalyses the following chemical reaction
- urate + FADH + H+ + O2 5-hydroxyisourate + FAD+ + H2O
References
edit- ^ 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
edit- FAD-dependent+urate+hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)