HERBICIDES THAT INHIBIT ACETOLACTATE SYNTHASE

doi:10.15302/J-FASE-2021420

Front. Agr. Sci. Eng.

2022, Vol. 9

Issue (1) : 155-160 https://doi.org/10.15302/J-FASE-2021420

PERSPECTIVE

HERBICIDES THAT INHIBIT ACETOLACTATE SYNTHASE

Thierry LONHIENNE, Mario Daniel GARCIA, Yu Shang LOW, Luke W. GUDDAT(

)

School of Chemistry and Molecular Bioscience, The University of Queensland, Queensland 4072, Australia

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Corresponding Author(s): Luke W. GUDDAT

Just Accepted Date: 24 August 2021 Online First Date: 14 September 2021 Issue Date: 17 January 2022

Cite this article:

Thierry LONHIENNE,Mario Daniel GARCIA,Yu Shang LOW, et al. HERBICIDES THAT INHIBIT ACETOLACTATE SYNTHASE[J]. Front. Agr. Sci. Eng. , 2022, 9(1): 155-160.

URL:

https://academic.hep.com.cn/fase/EN/10.15302/J-FASE-2021420
https://academic.hep.com.cn/fase/EN/Y2022/V9/I1/155

Fig.1 Chemical reactions for ALS and structures of ALS-inhibiting herbicides. (a) The chemical reactions of ALS. (b) The five different chemical classes of ALS-inhibiting herbicide, imidazolinones (IMIs) in pink, pyrimidinyl benzoates (PBs) in brown, a selection of sulfonylureas (SUs) in black, triazolopyrimidines (TPs) in blue, and the sulfonylamino-carbonyl-triazolinones (SCTs) in purple.

Fig.2 Cryo-EM and crystal structures of Arabidopsis thaliana ALS. (a) The complex between the CSUs (blue) and the RSUs (white) as determined by cryo-EM. (b) Close up of the interaction between the CSUs and RSUs. FAD, ThDP, Q-loop and valine are in yellow, green, red and blue, respectively. (c, d) Crystal structure of the complex between the CSU of A. thaliana ALS and the herbicide, penoxsulam. Penoxsulam is shown as a ball and stick model in with magenta carbon atoms. (c) The interface between the two CSU subunits (green and blue) is shown as a surface. Herbicide resistance sites are in red. (d) Details of the herbicide binding site. FAD, ThDP and peracetate are shown as stick models. The herbicide resistance sites are labeled and highlighted in red.

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