Acetyl‐CoA Carboxylase Inhibitors

Wenger, Jean; Niderman, Thierry; Mathews, Chris

doi:10.1002/9783527644179.ch11

Cited by 35 publications

(40 citation statements)

References 63 publications

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“…ACCase herbicides inhibit de novo fatty acid synthesis in sensitive grass weeds leading to rapid necrosis and plant death . The compounds can be divided into three classes, namely aryloxyphenoxypropionates (FOPs), cyclohexanediones (DIMs) and phenylpyrazolin (DEN), based on their chemical structures . Currently, ten FOPs, nine DIMs and one DEN herbicide are commercially available for controlling both grass weeds and volunteer crops.…”

Section: Accase Target and Herbicidesmentioning

confidence: 99%

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Resistance to acetyl‐CoA carboxylase‐inhibiting herbicides

Kaundun

2014

Pest Management Science

200

222

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Resistance to acetyl-CoA carboxylase herbicides is documented in at least 43 grass weeds and is particularly problematic in Lolium, Alopecurus and Avena species. Genetic studies have shown that resistance generally evolves independently and can be conferred by target-site mutations at ACCase codon positions 1781, 1999, 2027, 2041, 2078, 2088 and 2096. The level of resistance depends on the herbicides, recommended field rates, weed species, plant growth stages, specific amino acid changes and the number of gene copies and mutant ACCase alleles. Non-target-site resistance, or in essence metabolic resistance, is prevalent, multigenic and favoured under low-dose selection. Metabolic resistance can be specific but also broad, affecting other modes of action. Some target-site and metabolic-resistant biotypes are characterised by a fitness penalty. However, the significance for resistance regression in the absence of ACCase herbicides is yet to be determined over a practical timeframe. More recently, a fitness benefit has been reported in some populations containing the I1781L mutation in terms of vegetative and reproductive outputs and delayed germination. Several DNA-based methods have been developed to detect known ACCase resistance mutations, unlike metabolic resistance, as the genes remain elusive to date. Therefore, confirmation of resistance is still carried out via whole-plant herbicide bioassays. A growing number of monocotyledonous crops have been engineered to resist ACCase herbicides, thus increasing the options for grass weed control. While the science of ACCase herbicide resistance has progressed significantly over the past 10 years, several avenues provided in the present review remain to be explored for a better understanding of resistance to this important mode of action.

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Section: Accase Target and Herbicidesmentioning

confidence: 99%

“…Broadleaf species on the other hand are innately less sensitive owing to major differences in plastidic isoforms between grass and dicotyledonous species . A more comprehensive review of the ACCase target and herbicides can be found in several earlier publications …”

Section: Accase Target and Herbicidesmentioning

confidence: 99%

Resistance to acetyl‐CoA carboxylase‐inhibiting herbicides

Kaundun

2014

Pest Management Science

200

222

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“…It is a well-established molecular target site for commercially successful herbicides, including the aryloxyphenoxypropionates (FOPs), the cyclohexanediones (DIMs), and the more recently introduced pinoxaden (Devine, 2002, Wenger et al, 2012. Localization of herbicide-resistant mutations as well as structural studies have shown that the herbicidal ACC inhibitor classes bind to the carboxyltransferase (CT) domain of the multidomain ACC isoform in the plastids of grasses (Yu et al, 2007;Liu et al, 2007;Kaundun et al, 2013;Yu et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

The cyclic keto-enol insecticide spirotetramat inhibits insect and spider mite acetyl-CoA carboxylases by interfering with the carboxyltransferase partial reaction

Lümmen

Khajehali

Luther

et al. 2014

Insect Biochemistry and Molecular Biology

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Acetyl-CoA carboxylase (ACC) catalyzes the committed and rate-limiting step in fatty acid biosynthesis. The two partial reactions, carboxylation of biotin followed by carboxyl transfer to the acceptor acetyl-CoA, are performed by two separate domains in animal ACCs. The cyclic keto-enol insecticides and acaricides have been proposed to inhibit insect ACCs. In this communication, we show that the enol derivative of the cylic keto-enol insecticide spirotetramat inhibited ACCs partially purified from the insect species Myzus persicae and Spodoptera frugiperda, as well as the spider mite (Tetranychus urticae) ACC which was expressed in insect cells using a recombinant baculovirus. Steady-state kinetic analysis revealed competitive inhibition with respect to the carboxyl acceptor, acetyl-CoA, indicating that spirotetramat-enol bound to the carboxyltransferase domain of ACC. Interestingly, inhibition with respect to the biotin carboxylase substrate ATP was uncompetitive, which may indicate that the keto-enol binding site was formed following long-range conformational change triggered by ATP binding. Amino acid residues in the carboxyltransferase domains of plant ACCs are important for binding of established herbicidal inhibitors. Mutating the spider mite ACC at the homologous positions, for example L1736 to either isoleucine or alanine, and A1739 to either valine or serine, did not affect the inhibition of the spider mite ACC by spirotetramat-enol. These results indicated different binding modes of the keto-enols and the herbicidal chemical families.

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“…Because the acetyl‐CoA‐carboxylase (ACCase) also plays a fundamental role in fatty acid metabolism by catalysing the carboxylation of acetyl‐CoA in plants, it is also a target of interest for weed control …”

Section: Proherbicides For Weed Controlmentioning

confidence: 99%

Propesticides and their use as agrochemicals

2015

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The synthesis of propesticides is an important concept in design of modern agrochemicals with optimal efficacy, environmental safety, user friendliness and economic variability. Based on increasing knowledge of the biochemistry and genetics of major pest insects, weeds and agricultural pathogens, the search for selectivity has become an ever more important part of pesticide development and can be achieved by appropriate structural modifications of the active ingredient. Propesticides affect the absorption, distribution, metabolism and excretion parameters, which can lead to biological superiority of these modified active ingredients over their non-derivatised analogues. Various selected commercial propesticides testify to the successful utilisation of this concept in the design of agrochemicals. This review describes comprehensively the successful utilisation of propesticides and their role in syntheses of modern agrochemicals, exemplified by selected commercial products coming from different agrochemical areas.

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Acetyl‐CoA Carboxylase Inhibitors

Cited by 35 publications

References 63 publications

Resistance to acetyl‐CoA carboxylase‐inhibiting herbicides

Resistance to acetyl‐CoA carboxylase‐inhibiting herbicides

The cyclic keto-enol insecticide spirotetramat inhibits insect and spider mite acetyl-CoA carboxylases by interfering with the carboxyltransferase partial reaction

Propesticides and their use as agrochemicals

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