Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase.

Abstract:

: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 consistent with the proposal that HpxO-bound flavin hydroperoxide is the hydroxylating species. These results confirm the existence of a novel mechanistic paradigm in purine catabolism.

journal_name

Biochemistry

journal_title

Biochemistry

authors

O'Leary SE,Hicks KA,Ealick SE,Begley TP

doi

10.1021/bi900160b

subject

Has Abstract

pub_date

2009-04-14 00:00:00

pages

3033-5

issue

14

eissn

0006-2960

issn

1520-4995

journal_volume

48

pub_type

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