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

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.

authors

• Begley, Tadhg

published proceedings

• Biochemistry

altmetric score

• 3

author list (cited authors)

• O'Leary, S. E., Hicks, K. A., Ealick, S. E., & Begley, T. P.

citation count

• 10

complete list of authors

• O'Leary, Seán E||Hicks, Katherine A||Ealick, Steven E||Begley, Tadhg P

publication date

• April 2009

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Flavin-adenine Dinucleotide
• Hydroxylation
• Klebsiella Pneumoniae
• Purines
• Urate Oxidase
• Uric Acid

PubMed Central ID

• 19260710

Digital Object Identifier (DOI)

• 10.1021/bi900160b

start page

• 3033

end page

• 3035

volume

• 48

issue

• 14

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fbi900160b