Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase

Biochemistry

Volumn 44, Issue 7, 2005, Pages 2330-2338

  McCourt, Jennifer A ^a   Pang, Siew Siew ^a,b   Guddat, Luke W ^a   Duggleby, Ronald G ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b NOVARTIS INSTITUTE FOR TROPICAL DISEASES   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; ENZYME INHIBITION; ENZYMES; HERBICIDES; MUTAGENESIS; PLANTS (BOTANY);

ACETOHYDROXYACID SYNTHASE; MUTATIONS; SULFOMETURAN METHYL; SULFONYLUREA HERBICIDES;

UREA;

ACETOLACTATE SYNTHASE; CHLORSULFURON; COCARBOXYLASE; ENAMINE; FLAVINE ADENINE NUCLEOTIDE; HERBICIDE; METSULFURON METHYL; SULFOMETURON METHYL; SULFONYLUREA DERIVATIVE; TRIBENURON METHYL;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENE MUTATION; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

ACETOLACTATE SYNTHASE; ARYLSULFONATES; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FLAVIN-ADENINE DINUCLEOTIDE; HERBICIDES; MITOCHONDRIA; MOLECULAR CONFORMATION; PYRIMIDINES; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY; SULFONAMIDES; SULFONYLUREA COMPOUNDS; THIAMINE PYROPHOSPHATE; TRIAZINES;

EID: 14044273048     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047980a     Document Type: Article

References (32)

1. Sauers, R. F., and Levitt, G. (1984) Sulfonylureas: New high potency herbicides, in Pesticide Synthesis Through Rational Approaches (Magee, P. S., Kohn, G. K., and Menn, J. J., Eds.) pp 21-28, American Chemical Society, Washington, DC.
2. LaRossa, R. A., and Schloss, J. V. (1984) The sulfonylurea herbicide sulfometuron methyl is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium, J. Biol. Chem. 259, 8753-8757.
3. Ray, T. B. (1984) Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis of plants, Plant Physiol. 75, 827-831.
4. Duggleby, R. G., and Pang, S. S. (2000) Acetohydroxyacid synthase, J. Biochem. Mol. Biol. 33, 1-36.
5. Pang, S. S., Duggleby, R. G., and Guddat, L. W. (2002) Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors, J. Mol. Biol. 317, 249-262.
6. Pang, S. S., Guddat, L. W., and Duggleby, R. G. (2003) Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase, J. Biol. Chem. 278, 7639-7644.
7. Duggleby, R. G., Pang, S. S., Yu, H., and Guddat, L. W. (2003) Systematic characterization of mutations in yeast acetohydroxyacid synthase; Interpretation of herbicide-resistance data, Eur. J. Biochem. 270, 2895-2904.
8. Stornier, F. C., and Umbarger, H. E. (1964) The requirement for flavin adenine dinucleotide in the formation of acetolactate by Salmonella typhimurium extracts, Biochem. Biophys. Res. Commun. 17, 587-592.
9. Stornier, F. C. (1968) The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. II. Evidence that it is not a flavoprotein, J. Biol. Chem. 243, 3740-3741.
10. Chang, Y.-Y., and Cronan, J. E., Jr. (1988) Common ancestry of Escherichia coli pyruvate oxidase and the acetohydroxy acid synthases of the branched-chain amino acid biosynthetic pathway, J. Bacteriol. 170, 3937-3945.
11. Schloss, J. V., Ciskanik, L. M., and Van Dyk, D. E. (1988) Origin of the herbicide binding site of acetolactate synthase, Nature 331, 360-362.
12. Muller, Y. A., Schumacher, G., Rudolph, R., and Schulz, G. E. (1994) The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum, J. Mol. Biol. 237, 315-335.
13. Pang, S. S., Duggleby, R. G., Schowen, R. L., and Guddat, L. W. (2004) The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate, J. Biol. Chem. 279, 2242-2253.
14. Schloss, J. V., and Aulabaugh, A. (1988) Acetolactate synthase and ketol-acid reductoisomerase: A search for a reason and a reason for a search, in Biosynthesis of Branched Chain Amino Acids (Barak, Z., Chipman, D. M., and Schloss, J. V., Eds.) pp 329-356, VCH Press, Weinheim, Germany.
15. McCourt, J. A. (2004) Structural and mechanistic studies on acetohydroxyacid synthase and related enzymes, Ph.D. Thesis, The University of Queensland, Brisbane, Australia.
16. Tittmann, K., Schröder, K., Golbik, R., McCourt, J., Kaplun, A., Duggleby, R. G., Barak, Z., Chipman, D., and Hübner, G. (2004) Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of α-hydroxyethylthiamin diphosphate in a "nonredox" flavoenzyme, Biochemistry 43, 8652-8661.
17. Muller, Y. A., and Schulz, G. E. (1993) Structure of the thiamin-and-flavin-dependent enzyme pyruvate oxidase, Science 259, 965-967.
18. Pang, S. S., and Duggleby, R. G. (1999) Expression, purification, characterization and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase, Biochemistry 38, 5222-5231.
19. Lee, Y.-T., and Duggleby, R. G. (2002) Regulatory interactions in Arabidopsis thaliana acetohydroxyacid synthase, FEBS Lett. 512, 180-184.
20. Smith, P. K., Krohn, R. I., Hermanson, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeko, N. M., Olsen, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid, Anal. Biochem. 150, 76-85.
21. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
22. Navaza, J. (1994) AMoRe: An automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
23. Brünger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., et al. (1998) Crystallography and NMR system (CNS): A new software system for macromolecular structure determination, Acta Crystallogr. D54, 905-921.
24. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
25. Evans, S. V. (1993) SETOR: Hardware lighted three-dimensional solid model representations of macromolecules, J. Mol. Graphics 11, 134-138.
26. Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl Crystallogr. 24, 946-950.
27. Merritt, E. A., and Bacon, D. J. (1997) RASTER3D: Photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
28. Abell, L. M., and Schloss, J. V. (1991) Oxygenase side reactions of acetolactate synthase and other carbanion-forming enzymes, Biochemistry 30, 7883-7887.
29. Dobritzsch, D., König, S., Schneider, G., and Lu, G. (1998) High-resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases, J. Biol. Chem. 273, 20196-20204.
30. Falco, S. C., McDevitt, R. E., Chui, C-F., Hartnett, M. E., Knowlton, S., Mauvais, C. J., Smith, J. K., and Mazur, B. J. (1989) Engineering herbicide-resistant acetolactate synthase, Dev. Ind. Microbiol, 30, 187-194.
31. Engel, S., Vyamensky, M., Vinogradov, M., Berkovich, D., Barllan, A., Qimron, U., Rosiansky, Y., Barak, Z., and Chipman, D. (2004) Role of a conserved arginine in the mechanism of acetohydroxyacid synthase, J. Biol. Chem. 279, 24803-24812.
32. Chang, A. K., and Duggleby, R. G. (1998) Herbicide-resistant forms of Arabidopsis thaliana acetohydroxyacid synthase: Characterization of the catalytic properties and sensitivity to inhibitors of four defined mutants, Biochem. J. 333, 765-777.