Inhibition of plant acetyl-coenzyme a carboxylase by the herbicides sethoxydim and haloxyfop

Burton, J. D.; Gronwald, John W.; Somers, David A.; Connelly, James; Gengenbach, B. G.; Wyse, Donald L.

doi:10.1016/s0006-291x(87)80236-x

Cited by 173 publications

(112 citation statements)

References 14 publications

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“…It appears that the acyl component is at least partially responsible for this inhibition since free palmitate also inhibited enzymatic activity quite strongly. PalmitoylCoA was also reported to inhibit maize leaf acetyl-CoA carboxylase activity (15) (1,17), and yet 100 tM haloxyfop had no effect on C. cryptica acetyl-CoA carboxylase activity. The structure of the C. cryptica acetyl-CoA carboxylase active site apparently differs greatly from those of monocot acetyl-CoA carboxylases.…”

Section: Resultsmentioning

confidence: 98%

“…Since acetyl-CoA carboxylase has recently been shown to be the site of action of monocot-specific aryloxyphenoxypropionic acid and cyclohexanedione herbicides (1,16,21), it was of interest to determine the effects of these herbicides on the activity of purified C. cryptica acetyl-CoA carboxylase. The cyclohexanedione herbicide clethodim inhibited C. cryptica acetyl-CoA carboxylase activity in a dose-dependent man-…”

Section: Resultsmentioning

confidence: 99%

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Purification and Characterization of Acetyl-CoA Carboxylase from the Diatom Cyclotella cryptica

Roessler¹

1990

Plant Physiol.

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Acetyl-CoA carboxylase from the diatom Cyclotella cryptica has been purified to near homogeneity by the use of ammonium sulfate fractionation, gel filtration chromatography, and affinity chromatography with monomeric avidin-agarose. The specific activity of the final preparation was as high as 14.6 micromoles malonyl-CoA formed per milligram protein per minute, indicating a 600-fold purification. Native acetyl-CoA carboxylase has a molecular weight of approximately 740 kilodaltons and appears to be composed of four identical biotin-containing subunits. The enzyme has maximal activity at pH 8.2, but enzyme stability is greater at pH 6.5. Km values for MgATP, acetyl-CoA, and HC03 were determined to be 65, 233, and 750 micromolar, respectively. The purified enzyme is strongly inhibited by palmitoyl-CoA, and is inhibited to a lesser extent by malonyl-CoA, ADP, and phosphate. Pyruvate stimulates enzymatic activity to a slight extent.Acetyl-CoA carboxylase from Cyclotella cryptica is not inhibited by cyclohexanedione or aryloxyphenoxypropionic acid herbicides as strongly as monocot acetyl-CoA carboxylases; 50% and 0% inhibition was observed in the presence of 23 micromolar clethodim and 100 micromolar haloxyfop, respectively.

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Acetyl-CoA Carboxylase from the Diatom Cyclotella cryptica

Roessler¹

1990

Plant Physiol.

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“…In comparison to ACCase from the monocots wheat and ryegrass, ACCase from the broad-leaved species Pisum and Vicia is less sensitive to inhibition by the aryloxyphenoxypropionates and cyclohexanediones. It has been proposed that selective graminicidal action of the aryloxyphenoxypropionate and cyclohexanedione herbicides is a direct result of the differential sensitivities of ACCase from monocot and broadleaved plants to these herbicides (2,13,23,24).…”

Section: Accase From Species Tolerant To Diclofop-methylmentioning

confidence: 99%

“…Biotypes ofthe grass weed Lolium rigidum (annual ryegrass) with resistance to the selective postemergent graminicide diclofop-methyl' have been identified in all major cereal and ' Abbreviations: diclofop-methyl, methyl 2-[4-(2,4-dichlorophenoxy)phenoxy]propanoate; ACCase, acetyl-CoA carboxylase; alloxydim, 2-(l-alloxyaminobutylidene)-5,5-dimethyl-4-methoxycarbonylcyclohexane-1 ,3-dione; a.i., active ingredient; ALS, acetolactate synthase; chlorazifop-proponyl, 2 grain-legume cropping regions of mainland Australia (10,1,12,21). In all cases identified to date, resistance has developed following exposure to diclofop-methyl.…”

mentioning

confidence: 99%

“…The aryloxyphenoxypropionates diclofop-methyl, diclofop acid, haloxyfop acid, quizalofop acid, and fluazifop acid and the cyclohexanediones sethoxydim, alloxydim, and tralkoxydim inhibit ACCase (E.C. 6.4.1.2) (2,23,24,29) and, to a lesser extent, the pyruvate and a-ketoglutarate dehydrogenase complex (3). ACCase catalyses the acetyl CoA-, ATP-and HCO3 -dependent synthesis of malonyl CoA, a precursor required in the synthesis of lipids, fatty acids, and in several pathways of secondary metabolism.…”

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confidence: 99%

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Cross-Resistance to Herbicides in Annual Ryegrass (Lolium rigidum)

Matthews

Holtum²,

Liljegren³

et al. 1990

Plant Physiol.

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Acetyl‐CoA Carboxylase—a Graminicide Target Site

et al. 1997

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Acetyl‐CoA carboxylase catalyses the first committed step in fatty acid (and acyl lipid) formation. The enzyme has been shown to exert a high degree of flux control for lipid biosynthesis in leaves and, therefore, it is not surprising that chemicals which can inhibit it effectively are successful herbicides. These chemicals belong mainly to the cyclohexanedione and aryloxyphenoxypropionate classes and are graminicides. The reason for the selectivity of these herbicides towards grasses lies in the nature of the target site, acetyl‐CoA carboxylase. Recent advances in our knowledge of acetyl‐CoA carboxylases from sensitive and resistant plants has revealed some important facts. Dicotyledons, which are resistant, have a multi‐enzyme complex type of carboxylase in their chloroplasts while grasses have a multifunctional protein. Both divisions of plants have two isoforms of the enzyme, the second being in the cytosol. Detailed study of multifunctional forms of acetyl‐CoA carboxylases, which have different sensitivities to herbicides, suggests that herbicide resistance is correlated with cooperativity of herbicide binding to the native dimeric form of the carboxylase. © 1997 SCI.

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Inhibition of plant acetyl-coenzyme a carboxylase by the herbicides sethoxydim and haloxyfop

Cited by 173 publications

References 14 publications

Purification and Characterization of Acetyl-CoA Carboxylase from the Diatom Cyclotella cryptica

Purification and Characterization of Acetyl-CoA Carboxylase from the Diatom Cyclotella cryptica

Cross-Resistance to Herbicides in Annual Ryegrass (Lolium rigidum)

Acetyl‐CoA Carboxylase—a Graminicide Target Site

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