1. Boosted activity by engineering the enzyme microenvironment in cascade reaction: A molecular understanding
- Author
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Haiyang Zhang, Jing Wang, Tianwei Tan, Xiao Xu, Deping Yin, and Yongqin Lv
- Subjects
Circular dichroism ,QH301-705.5 ,Biomedical Engineering ,Boosted activity ,Applied Microbiology and Biotechnology ,Article ,Cofactor ,Catalysis ,Cascade reaction ,Structural Biology ,Molecular dynamics simulation ,Genetics ,Biology (General) ,chemistry.chemical_classification ,Oxidase test ,biology ,Cytochrome c ,Engineering of microenvironment ,Enzyme assay ,Enzyme ,Molecular understanding ,chemistry ,Multienzyme ,Biophysics ,biology.protein ,Ionic polymers ,TP248.13-248.65 ,Biotechnology - Abstract
Engineering of enzyme microenvironment can surprisingly boost the apparent activity. However, the underlying regulation mechanism is not well-studied at a molecular level so far. Here, we present a modulation of two model enzymes of cytochrome c (Cty C) and d-amino acid oxidase (DAAO) with opposite pH-activity profiles using ionic polymers. The operational pH of poly (acrylic acid) modified Cyt C and polyallylamine modified DAAO was extended to 3–7 and 2–10 where the enzyme activity was larger than that at their optimum pH of 4.5 and 8.5 by 106% and 28%, respectively. The cascade reaction catalyzed by two modified enzymes reveals a 1.37-fold enhancement in catalytic efficiency compared with their native counterparts. The enzyme activity boosting is understood by performing the UV–vis/CD spectroscopy and molecular dynamics simulations in the atomistic level. The increased activity is ascribed to the favorable microenvironment in support of preserving enzyme native structures nearby cofactor under external perturbations.
- Published
- 2021
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