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A View at the Millennium: the Efficiency of Enzymatic Catalysis
Abstract
Binding TS in preference to S and increasing TDeltaS++by freezing out motions in E X S and E X TS have been accepted as the driving forces in enzymatic catalysis; however, the smaller value of DeltaG++ for a one-substrate enzymatic reaction, as compared to its nonenzymatic counterpart, is generally the result of a smaller value of DeltaH++. Ground-state conformers (E X NACs) are formed in enzymatic reactions that structurally resemble E X TS. E X NACs are in thermal equilibrium with all other E X S conformers and are turnstiles through which substrate molecules must pass to arrive at the lowest-energy TS. TS in E X TS may or may not be bound tighter than NAC in E X NAC.
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Citations
Cited by
Reetz, M. T. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201000826 · Cited by 538
Computer Simulations of Enzyme Catalysis: Methods, Progress, and Insights
Warshel, A. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.141807 · Cited by 503
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
QM/MM Methods for Biological Systems
Senn, H. M., & Thiel, W. (2006) · Topics in Current Chemistry · doi:10.1007/128_2006_084 · Cited by 428
The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction
Lahiri, S. D., Zhang, G., Dunaway-Mariano, D., & Allen, K. N. (2003) · Science · doi:10.1126/science.1082710 · Cited by 325
Metadata
- Authors
- Bruice, T. C.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-01-18
- Volume
- 35
- Issue
- 3
- Pages
- 139-148
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2950002563
- Cited by
- 276
- References
- 0
- FWCI
- 13.93
- Type
- journal article
- Language
- en
- Open access
- closed
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