Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy
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 <i>Deinococcus radi...
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doaj-1c17429284fc4930a81c9489e170ea792021-06-01T01:06:35ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-05-01225611561110.3390/ijms22115611Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout TherapyYi-Chih Chiu0Ting-Syuan Hsu1Chen-Yu Huang2Chun-Hua Hsu3Genome and Systems Biology Degree Program, National Taiwan University and Academia Sinica, Taipei 115024, TaiwanTaipei First Girl High School, Taipei 10045, TaiwanTaipei First Girl High School, Taipei 10045, TaiwanGenome and Systems Biology Degree Program, National Taiwan University and Academia Sinica, Taipei 115024, TaiwanUrate 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 <i>Deinococcus radiodurans</i> (DrUox). From enzyme characterization, DrUox showed optimal catalytic ability at 30 °C and pH 9.0 with high stability under physiological conditions. Only the Mg<sup>2+</sup> 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.https://www.mdpi.com/1422-0067/22/11/5611uricase<i>Deinococcus radiodurans</i>gout therapy |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yi-Chih Chiu Ting-Syuan Hsu Chen-Yu Huang Chun-Hua Hsu |
spellingShingle |
Yi-Chih Chiu Ting-Syuan Hsu Chen-Yu Huang Chun-Hua Hsu Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy International Journal of Molecular Sciences uricase <i>Deinococcus radiodurans</i> gout therapy |
author_facet |
Yi-Chih Chiu Ting-Syuan Hsu Chen-Yu Huang Chun-Hua Hsu |
author_sort |
Yi-Chih Chiu |
title |
Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy |
title_short |
Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy |
title_full |
Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy |
title_fullStr |
Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy |
title_full_unstemmed |
Molecular Elucidation of a Urate Oxidase from <i>Deinococcus radiodurans</i> for Hyperuricemia and Gout Therapy |
title_sort |
molecular elucidation of a urate oxidase from <i>deinococcus radiodurans</i> for hyperuricemia and gout therapy |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-05-01 |
description |
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 <i>Deinococcus radiodurans</i> (DrUox). From enzyme characterization, DrUox showed optimal catalytic ability at 30 °C and pH 9.0 with high stability under physiological conditions. Only the Mg<sup>2+</sup> 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. |
topic |
uricase <i>Deinococcus radiodurans</i> gout therapy |
url |
https://www.mdpi.com/1422-0067/22/11/5611 |
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