The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Artificial selenoenzymes: Designed and redesigned
Abstract
Enzymes, highly evolved machinery developed by nature, catalyse reactions with formidable efficiency and specificity under mild conditions. Considerable efforts have been devoted for several decades on the development of enzyme-like catalysts with tailored properties by rationally manipulating natural and artificially synthesized host molecules. One of the great challenges is to design artificial systems with catalytic efficiencies and specificities rivalling natural components. Although most of the designed artificial enzymes present mild rate promotion, the high efficiency and specificity rivalling natural ones by artificially designed system appears. In this tutorial review, we recount the methods and strategies of design and redesign of artificial selenoenzymes on synthesized and natural hosts, with emphasis on construction of the active sites of antioxidative glutathione peroxidase (GPx) by the concept of synergy between recognition and catalysis (66 references).
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Cites
Glutathione Peroxidase, V. The kinetic mechanism
Flohé, L., Loschen, G., Günzler, W. A., & Eichele, E. (1972) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1972.353.1.987 · Cited by 340
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Wei, H., & Wang, E. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35486e · Cited by 3,779
Wang, Y., Wang, X., & Antonietti, M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201101182 · Cited by 3,364
Selenium-Containing Polymers: Promising Biomaterials for Controlled Release and Enzyme Mimics
Xu, H., Cao, W., & Zhang, X. (2013) · Accounts of Chemical Research · doi:10.1021/ar4000339 · Cited by 586
Design of therapeutic biomaterials to control inflammation
Tu, Z., Zhong, Y., Hu, H., Shao, D., Haag, R., Schirner, M., Lee, J., Sullenger, B., & Leong, K. W. (2022) · Nature Reviews Materials · doi:10.1038/s41578-022-00426-z · Cited by 513
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Metadata
- Authors
- Huang, X., Liu, X., Luo, Q., Liu, J., & Shen, J.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2011
- Volume
- 40
- Issue
- 3
- Pages
- 1171-1184
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2044525084
- Cited by
- 181
- References
- 1
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- closed
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- Huang, X., Liu, X., Luo, Q., Liu, J., & Shen, J. (2011). Artificial selenoenzymes: Designed and redesigned. Chem. Soc. Rev. https://doi.org/10.1039/c0cs00046a
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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