The DOI matches its Crossref record; 143 of the 143 references it cites were found in a registry or an index.
Minimalist Active‐Site Redesign: Teaching Old Enzymes New Tricks
Abstract
Although nature evolves its catalysts over millions of years, enzyme engineers try to do it a bit faster. Enzyme active sites provide highly optimized microenvironments for the catalysis of biologically useful chemical transformations. Consequently, changes at these centers can have large effects on enzyme activity. The prediction and control of these effects provides a promising way to access new functions. The development of methods and strategies to explore the untapped catalytic potential of natural enzyme scaffolds has been pushed by the increasing demand for industrial biocatalysts. This Review describes the use of minimal modifications at enzyme active sites to expand their catalytic repertoires, including targeted mutagenesis and the addition of new reactive functionalities. Often, a novel activity can be obtained with only a single point mutation. The many successful examples of active‐site engineering through minimal mutations give useful insights into enzyme evolution and open new avenues in biocatalyst research.
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1 retracted
Computational Design of a Biologically Active Enzyme
Dwyer, M. A., Looger, L. L., & Hellinga, H. W. (2004) · Science · doi:10.1126/science.1098432 · Cited by 294
RetractedIndustrial biocatalysis today and tomorrow
Schmid, A., Dordick, J. S., Hauer, B., Kiener, A., Wubbolts, M., & Witholt, B. (2001) · Nature · doi:10.1038/35051736 · Cited by 2,405
Serine Protease Mechanism and Specificity
Hedstrom, L. (2002) · Chemical Reviews · doi:10.1021/cr000033x · Cited by 1,827
ENZYME RECRUITMENT IN EVOLUTION OF NEW FUNCTION
Jensen, R. A. (1976) · Annual Review of Microbiology · doi:10.1146/annurev.mi.30.100176.002205 · Cited by 1,101
Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations
Eliot, A. C., & Kirsch, J. F. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074021 · Cited by 950
The Isoenzymes of Glutathione Transferase
Mannervik, B. (1985) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470123034.ch5 · Cited by 948
The Depth of Chemical Time and the Power of Enzymes as Catalysts
Wolfenden, R., & Snider, M. J. (2001) · Accounts of Chemical Research · doi:10.1021/ar000058i · Cited by 930
Enzymes for chemical synthesis
Koeller, K. M., & Wong, C.-H. (2001) · Nature · doi:10.1038/35051706 · Cited by 894
Dispelling the Myths--Biocatalysis in Industrial Synthesis
Schoemaker, H. E., Mink, D., & Wubbolts, M. G. (2003) · Science · doi:10.1126/science.1079237 · Cited by 834
The 'evolvability' of promiscuous protein functions
Aharoni, A., Gaidukov, L., Khersonsky, O., Gould, S. M., Roodveldt, C., & Tawfik, D. S. (2005) · Nature Genetics · doi:10.1038/ng1482 · Cited by 832
Cited by
Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355
Enzyme promiscuity: evolutionary and mechanistic aspects
Khersonsky, O., Roodveldt, C., & Tawfik, D. S. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.011 · Cited by 641
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Protein Design by Directed Evolution
Jäckel, C., Kast, P., & Hilvert, D. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125832 · Cited by 409
Self-citationPierron, J., Malan, C., Creus, M., Gradinaru, J., Hafner, I., Ivanova, A., Sardo, A., & Ward, T. R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200703159 · Cited by 117
Metadata
- Authors
- Toscano, M. D., Woycechowsky, K. J., & Hilvert, D.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2007-04-23
- Volume
- 46
- Issue
- 18
- Pages
- 3212-3236
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2055212608
- Cited by
- 262
- References
- 143
- FWCI
- 9.10
- Type
- journal article
- Language
- en
- Open access
- closed
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