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"Resurrected" human-source urate oxidase with high uricolytic activity and stability
Enzyme and Microbial Technology ( IF 3.4 ) Pub Date : 2021-06-16 , DOI: 10.1016/j.enzmictec.2021.109852
Nan Jiang 1 , Chunqin Xu 1 , Linhan Zhang 1 , Jianhua Chen 1
Affiliation  

As evidences showed that UOX(Gene ID: 391051), a single pseudogene formed after multiple mutations during human evolution, could be transcribed to mature mRNA and translated to two short peptides, we hypothesized that urate oxidase with higher homology with deduced human urate oxidase (dHU) might have lower immunogenicity. In this work, we constructed a "resurrected" human-source urate oxidase (rHU19) based on dHU. It obtained better uricolytic activity (8.29 U/mg) and catalytic efficiency (3.32 s-1 μM-1) compared with wild porcine urate oxidase (wPU) and FDA-approved porcine–baboon chimera (PBC). Maintaining high homology with dHU (93.75%), rHU19 could be more suitable for the treatment of gout and hyperuricemia theoretically.



中文翻译:

“复活”的人源尿酸氧化酶具有高尿酸溶解活性和稳定性

有证据表明,人类进化过程中多次突变后形成的单一假基因UOX(Gene ID:391051)可以转录为成熟的mRNA并翻译为两个短肽,我们假设尿酸盐氧化酶与推导的人尿酸盐氧化酶具有更高的同源性( dHU) 可能具有较低的免疫原性。在这项工作中,我们构建了一个基于 dHU 的“复活”人源尿酸氧化酶 (rHU19)。与野生猪尿酸氧化酶 (wPU) 和 FDA 批准的猪狒狒嵌合体 (PBC) 相比,它获得了更好的尿酸溶解活性 (8.29 U/mg) 和催化效率 (3.32 s -1  μM -1 )。rHU19与dHU保持高度同源性(93.75%),理论上更适合治疗痛风和高尿酸血症。

更新日期:2021-06-17
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