Molecular Elucidation of a Urate Oxidase from Deinococcus radiodurans for Hyperuricemia and Gout Therapy
| Autor: | Chen-Yu Huang, Ting-Syuan Hsu, Chun-Hua Hsu, Yi-Chih Chiu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Gout Urate Oxidase QH301-705.5 Hyperuricemia Catalysis Article Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Deinococcus radiodurans medicine Extremophile Animals Humans Physical and Theoretical Chemistry Biology (General) Molecular Biology QD1-999 Spectroscopy chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry gout therapy Organic Chemistry Urate oxidase General Medicine biology.organism_classification medicine.disease Recombinant Proteins Computer Science Applications 030104 developmental biology Enzyme Biochemistry Uric acid uricase Deinococcus Mesophile |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 22, Iss 5611, p 5611 (2021) Volume 22 Issue 11 |
| ISSN: | 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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