The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Evolution of a highly active and enantiospecific metalloenzyme from short peptides
Open accessAbstract
Evolution trains a from-scratch catalyst: Metal-bound peptides can catalyze simple reactions such as ester hydrolysis and may have been the starting point for the evolution of modern enzymes. Studer et al. selected progressively more-proficient variants of a small protein derived from a computationally designed zinc-binding peptide. The resulting enzyme could perform the trained reaction at rates typical for naturally evolved enzymes and serendipitously developed a strong preference for a single enantiomer of the substrate. A structure of the final catalyst highlights how small, progressive changes can remodel both catalytic residues and protein architecture in unpredictable ways. Science , this issue p. 1285
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Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Leaver-Fay (2011) · doi:10.1016/b978-0-12-381270-4.00019-6 · Cited by 1,904
Linking Crystallographic Model and Data Quality
Karplus, P. A., & Diederichs, K. (2012) · Science · doi:10.1126/science.1218231 · Cited by 1,781
The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters
Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S., & Milo, R. (2011) · Biochemistry · doi:10.1021/bi2002289 · Cited by 1,050
Evolution of the Structure of Ferredoxin Based on Living Relics of Primitive Amino Acid Sequences
Eck, R. V., & Dayhoff, M. O. (1966) · Science · doi:10.1126/science.152.3720.363 · Cited by 471
Cited by
Directed Evolution: Methodologies and Applications
Wang, Y., Xue, P., Cao, M., Yu, T., Lane, S. T., & Zhao, H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00260 · Cited by 719
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Embracing Nature’s Catalysts: A Viewpoint on the Future of Biocatalysis
Hauer, B. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c01708 · Cited by 284
Artificial Metalloenzymes: Challenges and Opportunities
Davis, H. J., & Ward, T. R. (2019) · ACS Central Science · doi:10.1021/acscentsci.9b00397 · Cited by 283
Advances in ultrahigh-throughput screening for directed enzyme evolution
Markel, U., Essani, K. D., Besirlioglu, V., Schiffels, J., Streit, W. R., & Schwaneberg, U. (2020) · Chemical Society Reviews · doi:10.1039/c8cs00981c · Cited by 258
Metadata
- Authors
- Studer, S., Hansen, D. A., Pianowski, Z. L., Mittl, P. R. E., Debon, A., Guffy, S. L., Der, B. S., Kuhlman, B., & Hilvert, D.
- Venue
- Science
- Published
- 2018-12-14
- Volume
- 362
- Issue
- 6420
- Pages
- 1285-1288
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2905286816
- Cited by
- 171
- References
- 5
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- green
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