The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Enzymatic Catalysis and Transition-State Theory: Transition-state analogs show that catalysis is due to tighter binding of transition states than of substrates.
Abstract
The application of transition-state theory to enzymatic catalysis provides an approach to understanding enzymatic catalysis in terms of the factors that determine the strength of binding of ligands to proteins. The prediction that the transition state should bind to the enzyme much more tightly than the substrate is supported by the experimental results with stable analogs of transition states. Transition-state analogs have great potential for use in understanding enzymatic catalysis and in inhibiting enzymes. Because of their potency and specificity as enzyme inhibitors, some of them may become very useful chemotherapeutic agents.
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Citations
Cites
A Correlation of Reaction Rates
Hammond, G. S. (1955) · Journal of the American Chemical Society · doi:10.1021/ja01607a027 · Cited by 3,559
Page, M. I., & Jencks, W. P. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.8.1678 · Cited by 1,014
Pseudo-rotation in the hydrolysis of phosphate esters
Westheimer, F. H. (1968) · Accounts of Chemical Research · doi:10.1021/ar50003a002 · Cited by 772
Crystallographic studies of the activity of hen egg-white lysozyme
Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Phillips, D. C., & Sarma, V. R. (1967) · Proceedings of the Royal Society of London. Series B. Biological Sciences · doi:10.1098/rspb.1967.0035 · Cited by 656
Cold Spring Harbor Symposia on Quantitative Biology
(1934) · Science · doi:10.1126/science.79.2061.584 · Cited by 609
Analog approaches to the structure of the transition state in enzyme reactions
Wolfenden, R. (1972) · Accounts of Chemical Research · doi:10.1021/ar50049a002 · Cited by 602
P1,P5-Di(adenosine-5′)pentaphosphate, a Potent Multisubstrate Inhibitor of Adenylate Kinase
Lienhard, G. E., & Secemski, I. I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44380-9 · Cited by 521
Self-citationTransition State Analogues for Enzyme Catalysis
WOLFENDEN, R. (1969) · Nature · doi:10.1038/223704a0 · Cited by 389
Reynolds, S. J., Yates, D., & Pogson, C. I. (1971) · Biochemical Journal · doi:10.1042/bj1220285 · Cited by 128
7 Chymotrypsin-Chemical Properties and Catalysis
Kraut, J. (1971) · The Enzymes · doi:10.1016/s1874-6047(08)60398-4 · Cited by 99
Cited by
Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect
Jencks, W. P. (1975) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470122884.ch4 · Cited by 854
MECHANISTIC ASPECTS OF ENZYMATIC CATALYSIS: Lessons from Comparison of RNA and Protein Enzymes
Narlikar, G. J., & Herschlag, D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.19 · Cited by 262
Lad, C., Williams, N. H., & Wolfenden, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0631607100 · Cited by 260
Brath, U., & Akke, M. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.047 · Cited by 36
Metadata
- Authors
- Lienhard, G. E.
- Venue
- Science
- Published
- 1973-04-13
- Volume
- 180
- Issue
- 4082
- Pages
- 149-154
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1995841839
- Cited by
- 503
- References
- 14
- FWCI
- 33.22
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lienhard, G. E. (1973). Enzymatic Catalysis and Transition-State Theory: Transition-state analogs show that catalysis is due to tighter binding of transition states than of substrates. Science. https://doi.org/10.1126/science.180.4082.149
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
