The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop
Open accessAbstract
Acetyl-CoA carboxylases (ACCs) are crucial for the metabolism of fatty acids, making these enzymes important targets for the development of therapeutics against obesity, diabetes, and other diseases. The carboxyltransferase (CT) domain of ACC is the site of action of commercial herbicides, such as haloxyfop, diclofop, and sethoxydim. We have determined the crystal structures at up to 2.5-Å resolution of the CT domain of yeast ACC in complex with the herbicide haloxyfop or diclofop. The inhibitors are bound in the active site, at the interface of the dimer of the CT domain. Unexpectedly, inhibitor binding requires large conformational changes for several residues in this interface, which create a highly conserved hydrophobic pocket that extends deeply into the core of the dimer. Two residues that affect herbicide sensitivity are located in this binding site, and mutation of these residues disrupts the structure of the domain. Other residues in the binding site are strictly conserved among the CT domains.
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Obesity and the Environment: Where Do We Go from Here?
Hill, J. O., Wyatt, H. R., Reed, G. W., & Peters, J. C. (2003) · Science · doi:10.1126/science.1079857 · Cited by 2,180
The Mitochondrial Carnitine Palmitoyltransferase System — From Concept to Molecular Analysis
McGarry, J. D., & Brown, N. F. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00001.x · Cited by 1,616
Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2
Abu-Elheiga, L., Matzuk, M. M., Abo-Hashema, K. A. H., & Wakil, S. J. (2001) · Science · doi:10.1126/science.1056843 · Cited by 903
A war on obesity, not the obese.
Friedman, J. M. (2003) · Science · doi:10.1126/science.1079856 · Cited by 375
Cited by
Successful fluorine-containing herbicide agrochemicals
Fujiwara, T., & O’Hagan, D. (2014) · Journal of Fluorine Chemistry · doi:10.1016/j.jfluchem.2014.06.014 · Cited by 894
Key role for a glutathione transferase in multiple-herbicide resistance in grass weeds
Cummins, I., Wortley, D. J., Sabbadin, F., He, Z., Coxon, C. R., Straker, H. E., Sellars, J. D., Knight, K., Edwards, L., Hughes, D., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221179110 · Cited by 371
Harriman, G., Greenwood, J., Bhat, S., Huang, X., Wang, R., Paul, D., Tong, L., Saha, A. K., Westlin, W. F., Kapeller, R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520686113 · Cited by 287
Self-citationAcetyl-coenzyme A carboxylases: versatile targets for drug discovery
Tong, L., & Harwood, H. J. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21077 · Cited by 207
Self-citationEffect of Agricultural Chemicals and Organic Amendments on Biological Control Fungi
Pakdaman Sardrood, B., & Mohammadi Goltapeh, E. (2018) · Sustainable Agriculture Reviews · doi:10.1007/978-3-319-94232-2_5 · Cited by 13
Metadata
- Authors
- Zhang, H., Tweel, B., & Tong, L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-04-12
- Volume
- 101
- Issue
- 16
- Pages
- 5910-5915
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1967273388
- Cited by
- 165
- References
- 4
- FWCI
- 3.96
- Type
- journal article
- Language
- en
- Open access
- green
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