Ontology highlight
ABSTRACT:
SUBMITTER: O'Leary SE
PROVIDER: S-EPMC2842088 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Biochemistry 20090401 14
The HpxO enzyme from Klebsiella pneumoniae was recently proposed, on the basis of genetic studies, to catalyze the hydroxylation of uric acid to 5-hydroxyisourate as part of the purine catabolic pathway. Its primary sequence suggests that the HpxO catalytic activity depends on a flavin cofactor (FAD), contrasting with all previously studied urate oxidase enzymes, which have no cofactor requirement. Here we demonstrate biochemically that HpxO is an FAD-dependent urate oxidase. Our data are consis ...[more]