Interaction of Cyclohexanediones with Acetyl Coenzyme-A Carboxylase and an Artificial Target-Site Antibody Mimic: A Comparative Molecular Field Analysis

Webb, Steven R.; Durst, Gregory L.; Pernich, Daniel J.; Hall, J. Christopher

doi:10.1021/jf990568v

Cited by 10 publications

(12 citation statements)

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“…The molecules of APPs and CHDs consist of a hydrophobic carbon skeleton with polar substituents (developed formulas are available at www.weedscience.com). Their bioactivity is limited by rather strict structural requirements (Webb et al, 2000;Turner and Pernich, 2002). The structure-activity relationship and the mode of binding to ACCase are poorly understood for CHDs (Webb et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Their bioactivity is limited by rather strict structural requirements (Webb et al, 2000;Turner and Pernich, 2002). The structure-activity relationship and the mode of binding to ACCase are poorly understood for CHDs (Webb et al, 2000). Because residues 1,781 and 2,078 are involved in sensitivity to both APPs and CHDs, and because residues 2,027, 2,041, and 2,096 are involved in sensitivity to APPs only, it is clear that binding sites for both inhibitor classes are largely overlapping, but not Figure 3.…”

Section: Discussionmentioning

confidence: 99%

“…However, substantial variation in I 50 values are observed within the APP and CHD inhibitor classes, even within a given grass species (Tables II and III). This, and the heavy structural requirements for herbicidal activity observed for APPs and CHDs (Webb et al, 2000;Turner and Pernich, 2002), suggests that herbicide fitting into the cavity of the chloroplastic ACCase CT domain active site from grasses to reach their binding site(s) is extremely tight, and that some herbicide molecules fit better than others in the activesite cavity. Tight fitting is also likely the reason why such a subtle change as the Ile-1,781-Leu substitution, which may be considered as highly conservative, has a drastic effect upon the sensitivity of ACCase to the APPs fenoxaprop and diclofop and to the CHD cycloxydim, while it does not significantly alter sensitivity to the APPs clodinafop and haloxyfop, nor to the CHD clethodim (Zhang and Devine, 2000;Zagnitko et al, 2001;Christoffers et al, 2002;Délye et al, 2002aDélye et al, , 2002bDélye et al, , 2002c.…”

Section: Discussionmentioning

confidence: 99%

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Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

et al. 2005

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In grasses, residues homologous to residues Ile-1,781 and Ile-2,041 in the carboxyl-transferase (CT) domain of the chloroplastic acetyl-coenzyme A (CoA) carboxylase (ACCase) from the grass weed black-grass (Alopecurus myosuroides [Huds.]) are critical determinants for sensitivity to two classes of ACCase inhibitors, aryloxyphenoxypropionates (APPs) and cyclohexanediones. Using natural mutants of black-grass, we demonstrated through a molecular, biological, and biochemical approach that residues Trp-2,027, Asp-2,078, and Gly-2,096 are also involved in sensitivity to ACCase inhibitors. In addition, residues Trp-2,027 and Asp-2,078 are very likely involved in CT activity. Using three-dimensional modeling, we found that the side chains of the five residues are adjacent, located at the surface of the inside of the cavity of the CT active site, in the vicinity of the binding site for APPs. Residues 1,781 and 2,078 are involved in sensitivity to both APPs and cyclohexanediones, whereas residues 2,027, 2,041, and 2,096 are involved in sensitivity to APPs only. This suggests that the binding sites for these two classes of compounds are overlapping, although distinct. Comparison of three-dimensional models for black-grass wild-type and mutant CTs and for CTs from organisms with contrasted sensitivity to ACCase inhibitors suggested that inhibitors fitting into the cavity of the CT active site of the chloroplastic ACCase from grasses to reach their active sites may be tight. The three-dimensional shape of this cavity is thus likely of high importance for the efficacy of ACCase inhibitors.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

et al. 2005

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“…Para tener una mejor claridad sobre la capacidad que tiene un antioxidante para inhibir radicales libres, esta parte del trabajo se realizó utilizando el Software de Sistema de Modelamiento Molecular -HyperChem (Vérsion 6,01) (STATSOFT, 2000), determinando el Análisis Conformacional de Mínima Energía, reportado por Van Acker et al (1996);Vajragupta, Boonchoong, Wongkrajang (2000) y Webb et al (2000).…”

Section: C) Poder Antirradicalunclassified

Antocianinas, ácido ascórbico, polifenoles totales y actividad antioxidante, en la cáscara de camu-camu (Myrciaria dubia (H.B.K) McVaugh)

Villanueva-Tiburcio¹,

Condezo-Hoyos²,

Asquieri³

2010

Ciênc. Tecnol. Aliment.

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“…Even 3D structures of receptors are unclear, one can deduce the properties of receptors, design new chemicals and quantitatively estimate activities of chemicals by studying circumambient interaction force fields of bioactive molecules and quantifying bioactivities. CoMFA has been widely used in quantitative drugs and pesticides design [38,39] . In ecotoxicology, CoMFA has been mainly used to predict toxicity of organic pollutants, such as estrogenic activities of endocrine disrupting chemicals [40,41] .…”

Section: Principles and Methods Of (Q)sarsmentioning

confidence: 99%

Progress and perspectives of quantitative structure-activity relationships used for ecological risk assessment of toxic organic compounds

Chen

et al. 2008

Sci. China Ser. B-Chem.

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Structure-activity relationship (SAR) and quantitative structure-activity relationship (QSAR), collectively referred to as (Q)SARs, play an important role in ecological risk assessment (ERA) of organic chemicals. (Q)SARs can fill the data gap for physical-chemical, environmental behavioral and ecotoxicological parameters of organic compounds; they can decrease experimental expenses and reduce the extent of experimental testing (especially animal testing); they can also be used to assess the uncertainty of the experimental data. With the development for several decades, (Q)SARs in environmental sciences show three features: application orientation, multidisciplinary integration, and intelligence. Progress of (Q)SAR technology for ERA of toxic organic compounds, including endpoint selection and mathematic methods for establishing simple, transparent, easily interpretable and portable (Q)SAR models, is reviewed. The recent development on defining application domains and diagnosing outliers is summarized. Model characterization with respect to goodness-of-fit, stability and predictive power is specially presented. The purpose of the review is to promote the development of (Q)SARs orientated to ERA of organic chemicals.(Q)SARs, ecological risk assessment, application domain, stability, predictive power

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Interaction of Cyclohexanediones with Acetyl Coenzyme-A Carboxylase and an Artificial Target-Site Antibody Mimic: A Comparative Molecular Field Analysis

Cited by 10 publications

References 13 publications

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

Antocianinas, ácido ascórbico, polifenoles totales y actividad antioxidante, en la cáscara de camu-camu (Myrciaria dubia (H.B.K) McVaugh)

Progress and perspectives of quantitative structure-activity relationships used for ecological risk assessment of toxic organic compounds

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