人工酶与定向进化的前沿与挑战

doi:10.3981/j.issn.1000-7857.2020.08.012

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Abstract: The directed evolution is a method to obtain proteins with desired traits by mimicking the evolution process at the molecular level in a lab environment. It is an important method for protein design and engineering. Apart from the engineering natural proteins, the directed evolution can be used to construct artificial enzymes by modifying the existing enzymes to have new catalytic activities. This paper reviews the recent studies of the industrial biocatalysis, the nanozyme design and the photocatalysis, as well as the challenges and the problems in the field of the directed evolution and the artificial enzyme.

Key words： artificial enzyme directed evolution industrial biocatalysis nanozyme photocatalysis

Received: 27 November 2019

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	YU Yang
	WANG Jiangyun

Cite this article:

YU Yang,WANG Jiangyun. Frontiers and challenges of artificial enzyme and directed evolution[J]. Science & Technology Review, 2020, 38(8): 101-105.

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http://www.kjdb.org/EN/10.3981/j.issn.1000-7857.2020.08.012 OR http://www.kjdb.org/EN/Y2020/V38/I8/101

[1] Arnold F H. Innovation by evolution:Bringing new chemistry to life (Nobel Lecture)[J]. Angewandte Chemie (International Edition), 2019, 58(41):14420-14426.
[2] Zeymer C, Hilvert D. Directed evolution of protein catalysts[J]. Annual Review of Biochemistry, 2018, 87(1):131-157.
[3] Reetz M T. Directed evolution of artificial metalloenzymes:A universal means to tune the selectivity of transition metal catalysts?[J]. Accounts of Chemical Research, 2019, 52(2):336-344.
[4] 曲戈, 朱彤, 蒋迎迎, 等. 蛋白质工程:从定向进化到计算设计[J]. 生物工程学报, 2019, 35(10):1843-1856.
[5] Li R, Wijma H J, Song L, et al. Computational redesign of enzymes for regio-and enantioselective hydroamination[J]. Nature Chemical Biology, 2018, 14(7):664-670.
[6] Jiang B, Duan D, Gao L, et al. Standardized assays for determining the catalytic activity and kinetics of peroxidase-like nanozymes[J]. Nature Protocols, 2018, 13(7):1506-1520.
[7] Gao L, Zhuang J, Nie L, et al. Intrinsic peroxidase-like activity of ferromagnetic nanoparticles[J]. Nature Nanotechnology, 2007, 2(9):577-583.
[8] Wei H, Wang E. Nanomaterials with enzyme-like characteristics (nanozymes):Next-generation artificial enzymes[J]. Chemical Society Reviews, 2013, 42(14):6060-6093.
[9] Wang X, Gao X J, Qin L, et al. eg occupancy as an effective descriptor for the catalytic activity of perovskite oxide-based peroxidase mimics[J]. Nature Communications, 2019, 10(1):704.
[10] Wu J, Wang X, Wang Q, et al. Nanomaterials with enzyme-like characteristics (nanozymes):Next-generation artificial enzymes (II)[J]. Chemical Society Reviews, 2019, 48(4):1004-1076.
[11] Shih C F, Zhang T, Li J, et al. Powering the future with liquid sunshine[J]. Joule, 2018, 2(10):1925-1949.
[12] Liu X, Jiang L, Li J, et al. Significant expansion of fluorescent protein sensing ability through the genetic incorporation of superior photo-induced electron-transfer quenchers[J]. Journal of the American Chemical Society, 2014, 136(38):13094-13097.
[13] Liu X, Li J, Dong J, et al. Genetic incorporation of a metal-chelating amino acid as a probe for protein electron transfer[J]. Angewandte Chemie (International edition), 2012, 51(41):10261-10265.
[14] Liu X, Li J, Hu C, et al. Significant expansion of the fluorescent protein chromophore through the genetic incorporation of a metal-chelating unnatural amino acid[J]. Angewandte Chemie (International edition), 2013, 52(18):4805-4809.
[15] Lv X, Yu Y, Zhou M, et al. Ultrafast photoinduced electron transfer in green fluorescent protein bearing a genetically encoded electron acceptor[J]. Journal of the American Chemical Society, 2015, 137:7270-7273.
[16] Liu X, Kang F, Hu C, et al. A genetically encoded photosensitizer protein facilitates the rational design of a miniature photocatalytic CO₂-reducing enzyme[J]. Nature Chemistry, 2018, 10:1201-1206.