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Network of coupled promoting motions in enzyme catalysis
Open accessAbstract
A network of coupled promoting motions in the enzyme dihydrofolate reductase is identified and characterized. The present identification is based on genomic analysis for sequence conservation, kinetic measurements of multiple mutations, and mixed quantum/classical molecular dynamics simulations of hydride transfer. The motions in this network span time scales of femtoseconds to milliseconds and are found on the exterior of the enzyme as well as in the active site. This type of network has broad implications for an expanded role of the protein fold in catalysis as well as ancillaries such as the engineering of altered protein function and the action of drugs distal to the active site.
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Citations
Cited by
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Hammes, G. G., Chang, Y.-C., & Oas, T. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907195106 · Cited by 577
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Generalized correlation for biomolecular dynamics
Lange, O. F., & Grubmüller, H. (2006) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20784 · Cited by 455
Metadata
- Authors
- Agarwal, P. K., Billeter, S. R., Rajagopalan, P. T. R., Benkovic, S. J., & Hammes-Schiffer, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-02-26
- Volume
- 99
- Issue
- 5
- Pages
- 2794-2799
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2139036153
- Cited by
- 460
- References
- 0
- FWCI
- 8.75
- Type
- journal article
- Language
- en
- Open access
- green
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- Agarwal, P. K., Billeter, S. R., Rajagopalan, P. T. R., Benkovic, S. J., & Hammes-Schiffer, S. (2002). Network of coupled promoting motions in enzyme catalysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.052005999
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