Hostname: page-component-84b7d79bbc-tsvsl Total loading time: 0 Render date: 2024-07-29T21:34:26.536Z Has data issue: false hasContentIssue false
  • English
  • Français

Evaluating anthranilate synthase as a herbicide target

Published online by Cambridge University Press:  12 June 2017

Daniel L. Siehl ,
Mani V. Subramanian ,
Eric W. Walters ,
Jonathan H. Blanding ,
Thierry Niderman  and
Christian Weinmann
Daniel L. Siehl*
Affiliation:
Novartis Crop Protection, 975 California Avenue, Palo Alto, CA 94304-1104
Mani V. Subramanian
Affiliation:
Novartis Crop Protection, Paro Alto, CA 943041104
Eric W. Walters
Affiliation:
Novartis Crop Protection, Paro Alto, CA 943041104
Jonathan H. Blanding
Affiliation:
Novartis Crop Protection, Paro Alto, CA 943041104
Thierry Niderman
Affiliation:
Novartis Crop Protection, R-1040. P7A, Basel, Switzerland CH-4002
Christian Weinmann
Affiliation:
Novartis Crop Protection, R-1040. P7A, Basel, Switzerland CH-4002
*
dan.siehl@cp.novartis.com.
Get access Rights & Permissions [Opens in a new window]

Abstract

Attempts to discover new active ingredients and target sites within the aromatic pathway have resulted in the synthesis of potent enzyme inhibitors, but no herbicides. As an aid in identifying a new target for inhibitor design and screening, we have determined the mode of action of a compound (6-methyl anthranilate) that exhibits noncommercial levels of herbicidal activity. Our evidence suggests that 6-methyl anthranilate is converted in vivo, by traversing the tryptophan biosynthetic sequence, to 4-methyl tryptophan, which inhibits anthranilate synthase. Inhibitors synthesized by design and those found by target-based screening converged on analogs of tryptophan and anthranilate. None, however, was more herbicidal than 6-methyl anthranilate.

Keywords

Anthranilate synthase6-methyl anthranilateherbicide targetaromatic biosynthesis
Type
Symposium
Information
Weed Science , Volume 45 , Issue 5 , October 1997 , pp. 628 - 633
Copyright
Copyright © 1997 by the Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Literature Cited

Alberg, D. G., Lauhon, C. T., Nyfeler, R., Fässler, A., and Bartlett, P. A. 1992. Inhibition of EPSP synthase by analogues of the tetrahedral intermediate and of EPSP. J. Am. Chem. Soc. 114: 3535–3546.Google Scholar
Baille, A. C., Corbett, J. R., Dowsett, J. R., and McCloskey, P. 1972. Inhibitors of shikimate dehydrogenase as potential herbicides. Pestic. Sci. 3: 113–120.Google Scholar
Bartlett, P. A., Nakagawa, Y., Johnson, C. R., Reich, S. H., and Luis, A. 1988. Chorismate mutase inhibitors: synthesis and evaluation of some potential transition-state analogues. J. Org. Chem. 53: 3195–3210.Google Scholar
Bugg, T.D.H., Abell, C., and Coggins, J. R. 1988a. Specificity of E. coli shikimate dehydrogenase towards analogues of 3-dehydroshikimic acid. Tetrahedron Lett. 29: 6779–6782.CrossRefGoogle Scholar
Bugg, T.D.H., Abell, C., and Coggins, J. R. 1988b. Affinity labelling of E. coli dehydroquinase. Tetrahedron Lett. 29: 6783–6786.Google Scholar
Caligiuri, M. G. and Bauerle, R. 1991. Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhymurium . J. Biol. Chem. 266: 8328–8335.Google Scholar
Clarke, T., Stewart, J. D., and Ganem, B. 1990. Transition-state analogue inhibitors of chorismate mutase. Tetrahedron 46: 731–748.Google Scholar
Last, R. and Fink, G. 1988. Tryptophan-requiring mutants of the plant Arabidopsis thaliana , Science 240: 305–310.Google Scholar
Montchamp, J-L., Pieler, L. T., and Frost, J. W. 1992. Diastereoselection and in vivo inhibition of 3-dehydroquinate synthase. J. Am. Chem. Soc. 114: 4453–4459.CrossRefGoogle Scholar
Morollo, A. A., Finn, M. G., and Bauerle, R. 1993. Isolation and structure determination of 2-amino-2-deoxyisochorismate: an intermediate in the biosynthesis of anthranilate. J. Am. Chem. Soc. 115: 816–817.CrossRefGoogle Scholar
Normanly, J., Cohen, J. D., and Fink, G. R. 1993. Arabidopsis thaliana auxotrophs reveal a tryptophan-independent biosynthetic pathway for indole-3-acetic acid. Proc. Natl. Acad. Sci. 90: 10355–10359.Google Scholar
Pompliano, D. L., Reimer, L. M., Myrvold, S., and Frost, J. W. 1989. Probing metabolic perturbations in plants with chemical inhibition of dehydroquinate synthase. J. Am. Chem. Soc. 111: 1866–1871.Google Scholar
Poulsen, C., Bongaerts, R.J.M., and Verpoorte, R. 1993. Purification and characterization of anthranilate synthase from Catharanthus roseus . Eur. J. Biochem. 212: 431–440.Google Scholar
Prisbylla, M. P., Onisko, B. C., Shribbs, J. M., Adams, D. O., Liu, Y., Ellis, M. K., Hawkes, T. R., and Mutter, L. C. 1993. The novel mechanism of action of the herbicidal triketones. in Proc. Brighton Crop Prot. Conf.—Weeds. London: British Crop Protection Council, pp. 731–738.Google Scholar
Schulz, A., Ort, O., Beyer, P., and Kleinig, H. 1993. SC-0051, a 2-benzolcyclohexane-1,3-dione bleaching herbicide, is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase. FEBS Lett. 318: 162–166.Google Scholar
Siehl, D. L. 1992. Considerations in selecting a target site for herbicide design. in Singh, B. K., Flores, H. E., and Shannon, J. C., eds. Biosynthesis and Molecular Regulation of Amino Acids in Plants. Rockville, MD: American Society of Plant Physiologists, pp. 146–162.Google Scholar
Siehl, D. L. 1997. Inhibitors of EPSP synthase, glutamine synthetase and histidine synthesis. in Roe, R. M. and Burton, J., eds. Herbicide Activity: Toxicology, Biochemistry and Molecular Biology. Amsterdam: I.O.S. Press, pp. 67–125.Google Scholar
Subramanian, M. V., Brunn, S. A., Bernasconi, P., Patel, B. C., and Reagan, J. D. 1997. Revisiting auxin transport inhibition as a mode of action for herbicides. Weed Sci. 45: 621–627.Google Scholar
Thomas, G. M. 1984. Herbicidal activity of 6-methylanthranilate and analogues. J. Agric. Food Chem. 32: 747–749.CrossRefGoogle Scholar
Veerasekaran, P., Kirkwood, R. C., and Parnell, E. W. 1981. Studies of the mechanism of action of asulam in plants: effect of asulam on the biosynthesis of folic acid. Pestic. Sci. 12: 330–338.CrossRefGoogle Scholar
Wittenbach, V.A., Aulabaugh, A., and Schloss, J. V. 1991. Examples of extraneous site inhibitors and reaction intermediate analogues: acetolactate synthase and ketol-acid reductoisomerase. in Frehse, H., ed. Pesticide Chemistry: Advances in International Research, Development and Legislation. Weinheim, Germany: VCH, pp. 151–160.Google Scholar