The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A Perspective on Enzyme Catalysis
Abstract
The seminal hypotheses proposed over the years for enzymatic catalysis are scrutinized. The historical record is explored from both biochemical and theoretical perspectives. Particular attention is given to the impact of molecular motions within the protein on the enzyme's catalytic properties. A case study for the enzyme dihydrofolate reductase provides evidence for coupled networks of predominantly conserved residues that influence the protein structure and motion. Such coupled networks have important implications for the origin and evolution of enzymes, as well as for protein engineering.
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Deu, E., Koch, K. A., & Kirsch, J. F. (2002) · Protein Science · doi:10.1110/ps.0200902 · Cited by 15
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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
Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity
Fisher, J. F., Meroueh, S. O., & Mobashery, S. (2005) · Chemical Reviews · doi:10.1021/cr030102i · Cited by 913
Conformational selection or induced fit: A flux description of reaction mechanism
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
Biomolecular Modeling: Goals, Problems, Perspectives
van Gunsteren, W. F., Bakowies, D., Baron, R., Chandrasekhar, I., Christen, M., Daura, X., Gee, P., Geerke, D. P., Glättli, A., Hünenberger, P. H., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200502655 · Cited by 561
Metadata
- Authors
- Benkovic, S. J., & Hammes-Schiffer, S.
- Venue
- Science
- Published
- 2003-08-29
- Volume
- 301
- Issue
- 5637
- Pages
- 1196-1202
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2160294964
- Cited by
- 1,262
- References
- 1
- FWCI
- 22.09
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
