Molecular elucidation of a urate oxidase from deinococcus radiodurans for hyperuricemia and gout therapy
Journal
International Journal of Molecular Sciences
Journal Volume
22
Journal Volume
22
Journal Issue
11
Journal Issue
11
ISSN
16616596
Date Issued
2021-06-01
Author(s)
Abstract
Urate oxidase initiates the uric acid degradation pathways and is extensively used for protein drug development for gout therapy and serum uric acid diagnosis. We first present the biochemical and structural elucidation of a urate oxidase from the extremophile microorganism Deinococcus radiodurans (DrUox). From enzyme characterization, DrUox showed optimal catalytic ability at 30? C and pH 9.0 with high stability under physiological conditions. Only the Mg2+ ion moderately elevated its activity, which indicates the characteristic of the cofactor-free urate oxidase family. Of note, DrUox is thermostable in mesophilic conditions. It retains almost 100% activity when incubated at 25? C and 37? C for 24 h. In this study, we characterized a thermostable urate oxidase, DrUox with high catalytic efficiency and thermal stability, which strengthens its potential for medical applications.
Subjects
Deinococcus radiodurans
Gout therapy
Uricase
SDGs
Publisher
MDPI
Description
Article number: 5611
Type
journal article