The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A Mechanism of Drug Action Revealed by Structural Studies of Enoyl Reductase
Abstract
Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2′ hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.
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Cites
inhA , a Gene Encoding a Target for Isoniazid and Ethionamide in Mycobacterium tuberculosis
Banerjee, A., Dubnau, E., Quemard, A., Balasubramanian, V., Um, K. S., Wilson, T., Collins, D., de Lisle, G., & Jacobs, W. R. (1994) · Science · doi:10.1126/science.8284673 · Cited by 1,389
Cited by
THE STRUCTURAL BIOLOGY OF TYPE II FATTY ACID BIOSYNTHESIS
White, S. W., Zheng, J., Zhang, Y.-M., & Rock, C. O. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133524 · Cited by 832
Antituberculosis drugs: Ten years of research
Janin, Y. L. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.01.030 · Cited by 485
Bacterial Fatty Acid Biosynthesis: Targets for Antibacterial Drug Discovery
Campbell, J. W., & Cronan, J. E. (2001) · Annual Review of Microbiology · doi:10.1146/annurev.micro.55.1.305 · Cited by 479
Therapeutic Potential of Boron-Containing Compounds
Baker, S. J., Ding, C. Z., Akama, T., Zhang, Y.-K., Hernandez, V., & Xia, Y. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.71 · Cited by 373
Lipid biosynthesis as a target for antibacterial agents
Heath, R. J., White, S. W., & Rock, C. O. (2001) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00012-1 · Cited by 344
Metadata
- Authors
- Baldock, C., Rafferty, J. B., Sedelnikova, S. E., Baker, P. J., Stuitje, A. R., Slabas, A. R., Hawkes, T. R., & Rice, D. W.
- Venue
- Science
- Published
- 1996-12-20
- Volume
- 274
- Issue
- 5295
- Pages
- 2107-2110
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2006941404
- Cited by
- 239
- References
- 1
- FWCI
- 9.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- Baldock, C., Rafferty, J. B., Sedelnikova, S. E., Baker, P. J., Stuitje, A. R., Slabas, A. R., Hawkes, T. R., & Rice, D. W. (1996). A Mechanism of Drug Action Revealed by Structural Studies of Enoyl Reductase. Science. https://doi.org/10.1126/science.274.5295.2107
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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