酶促燃料电池葡萄糖氧化酶H516r和H516d突变的原位硅分析

P. Puspita, L. Ambarsari, Adrian Adiva, T. Sumaryada
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引用次数: 2

摘要

葡萄糖氧化酶(GOx)是一种氧化还原酶,可将葡萄糖催化成过氧化氢和葡萄糖醛酸δ内酯(GDL)。GOx具有在医疗领域应用的潜力。关于使用GOx制造酶生物燃料电池的大量研究已经完成,然而获得的结果并不是最理想的。这项研究旨在提高GOx的Km值,以增加其作为酶燃料电池材料的潜力。516位的组氨酸是活性位点的残基,在葡萄糖氧化过程中起重要作用。在本研究中,我们用硅片对H516进行了两次突变,得到了突变体R516和D516。突变导致两个突变体的对接区域发生变化,并导致与H516D的对接亲和力发生变化,从而导致更高的Km值。这表明H516残基在葡萄糖氧化酶的功能中起着重要的作用,突变为天冬氨酸可以改善葡萄糖氧化酶酶促燃料电池。
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In Silico Analysis of Glucose Oxidase H516r and H516d Mutations for an Enzymatic Fuel Cell
Glucose oxidase (GOx) is an oxido-reductase enzyme that catalyzes glucose into hydrogen peroxide and glucono delta-lactone (GDL). GOx has the potential to be used in the medical field. Numerous research concerning the usage of GOx to create enzymatic biofuel cells have been done, nevertheless the results obtained have not been optimal. This research aims to increase the Km values of GOx in order to increase its potential as a material for an enzymatic fuel cell. The amino acid histidine in position 516 is a residue in the active site that plays an important part in the process of glucose oxidation. In this research we mutated H516 by in silico twice resulting in the mutants R516 and D516. The mutations resulted in a change of the docking area for both mutants and in the docking affinity for H516D resulting in higher Km values. This shows that the H516 residue plays an important part in the functions of glucose oxidase and mutation into aspartate could improve glucose oxidase based enzymatic fuel cells.
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来源期刊
CiteScore
0.80
自引率
0.00%
发文量
15
审稿时长
24 weeks
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