Inhibition of acetyl-coenzyme A carboxylase by two classes of grass-selective herbicides

Rendina, Alan R.; Craig-Kennard, Adrienne; Beaudoin, Jacqueline D.; Breen, Mary K.

doi:10.1021/jf00095a029

Cited by 87 publications

(71 citation statements)

References 21 publications

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“…[3][4][5] This enzyme is of two types in the cell, the prokaryotic type and the eukaryotic type. The above groups of herbicides, in vitro, inhibit ACCase of the eukaryotic type, but do not inhibit that of the prokaryotic type.…”

mentioning

confidence: 99%

Determination of Acetyl-CoA and Malonyl-CoA in Germinating Rice Seeds Using the LC-MS/MS Technique

Hayashi

Satoh

2006

Bioscience, Biotechnology, and Biochemistry

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A highly sensitive and selective analytical method was developed to determine levels of acetyl-CoA and malonyl-CoA in plant tissues. The analytical method includes a convenient extraction method for plant samples and a new LC-MS/MS technique utilizing an ion pair reagent. These acyl-CoAs, present in germinating rice seeds, were then determined by the method developed. It was found that the concentrations of both acetyl-CoA and malonyl-CoA increased with time during the germination of rice seeds and also increased at the elevated cultivation temperatures among tested. These results reflect the development of enzymes that produce these acyl-CoAs in germinating rice seeds.

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mentioning

confidence: 99%

Determination of Acetyl-CoA and Malonyl-CoA in Germinating Rice Seeds Using the LC-MS/MS Technique

Hayashi

Satoh

2006

Bioscience, Biotechnology, and Biochemistry

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“…These chemicals inhibit the CT activity, thus blocking the transfer of the carboxyl group to acetyl-CoA (Rendina et al, 1990;Burton et al, 1991). Multisubunit-type ACCases and cytosolic, multidomain-type ACCases are insensitive and significantly less sensitive, respectively, to CHDs and APPs than chloroplastic, multidomain-type ACCase (Egli et al, 1993;Alban et al, 1994).…”

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confidence: 99%

An Isoleucine Residue within the Carboxyl-Transferase Domain of Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione Inhibitors

et al. 2003

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A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive Alopecurus myosuroides (Huds.). No resistant plant contained an Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in resistant plants. Phylogenetic analysis of the sequences revealed that Asn-2,041 ACCase alleles derived from several distinct origins. Allele-specific polymerase chain reaction associated the presence of Asn-2,041 with seedling resistance to APPs but not to CHDs. ACCase enzyme assays confirmed that Asn-2,041 ACCase activity was moderately resistant to CHDs but highly resistant to APPs. Thus, the Ile-2,041-Asn substitution, which is located outside a domain previously shown to control sensitivity to APPs and CHDs in wheat (Triticum aestivum), is a direct cause of resistance to APPs only. In known multidomain ACCases, the position corresponding to the Ile/Asn-2,041 residue in A. myosuroides is occupied by an Ile or a Val residue. In Lolium rigidum (Gaud.), we found Ile-Asn and Ile-Val substitutions. The Ile-Val change did not confer resistance to the APP clodinafop, whereas the Ile-Asn change did. The position and the particular substitution at this position are of importance for sensitivity to APPs.

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“…M. tuberculosis AccD6 inhibition assay. Ten commercially available herbicides, reported as ACC ligands (23), were selected for their evaluation as possible M. tuberculosis ACC inhibitors. The compounds tested were clodinafop, cyhalofop, haloxyfop, fluazifop, and diclofop (from the FOP family) and sethoxydim, alloxydim, cycloxydim, tepraloxydim, and tralkoxydim (from the DIM family).…”

Section: Methodsmentioning

confidence: 99%

Structure, Activity, and Inhibition of the Carboxyltransferase β-Subunit of Acetyl Coenzyme A Carboxylase (AccD6) from Mycobacterium tuberculosis

Reddy

Breda

Bruning

et al. 2014

Antimicrob Agents Chemother

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Inhibition of acetyl-coenzyme A carboxylase by two classes of grass-selective herbicides

Cited by 87 publications

References 21 publications

Determination of Acetyl-CoA and Malonyl-CoA in Germinating Rice Seeds Using the LC-MS/MS Technique

Determination of Acetyl-CoA and Malonyl-CoA in Germinating Rice Seeds Using the LC-MS/MS Technique

An Isoleucine Residue within the Carboxyl-Transferase Domain of Multidomain Acetyl-Coenzyme A Carboxylase Is a Major Determinant of Sensitivity to Aryloxyphenoxypropionate But Not to Cyclohexanedione Inhibitors

Structure, Activity, and Inhibition of the Carboxyltransferase β-Subunit of Acetyl Coenzyme A Carboxylase (AccD6) from Mycobacterium tuberculosis

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