Kinetic characterization, stereoselectivity, and species selectivity of the inhibition of plant acetyl-CoA carboxylase by the aryloxyphenoxypropionic acid grass herbicides

Rendina, Alan R.; Felts, Judy M.; Beaudoin, Jacqueline D.; Craig-Kennard, Adrienne; Look, Larry L.; Paraskos, Stacie L.; Hagenah, Jeffrey A.

doi:10.1016/0003-9861(88)90387-6

Cited by 78 publications

(46 citation statements)

References 22 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%

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%

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

Roessler¹

1990

Plant Physiol.

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“…72 Earlier kinetic analyses with the aryloxyphenoxypropionates and the cyclohexandiones showed noncompetitive inhibition with respect to acetyl-CoA. 82 All of the crystal structures revealed that the herbicides share three common anchoring points. The first two are the peptidic NH groups of Ala 1627 and Ile 1735 that interact with oxygens on the inhibitors.…”

Section: Inhibitors Of Carboxyltransferasementioning

confidence: 99%

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

2012

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Biotin is the major cofactor involved in carbon dioxide metabolism. Indeed, biotindependent enzymes are ubiquitous in nature and are involved in a myriad of metabolic processes including fatty acid synthesis and gluconeogenesis. The cofactor, itself, is composed of a ureido ring, a tetrahydrothiophene ring, and a valeric acid side chain. It is the ureido ring that functions as the CO 2 carrier. A complete understanding of biotin-dependent enzymes is critically important for translational research in light of the fact that some of these enzymes serve as targets for antiobesity agents, antibiotics, and herbicides. Prior to 1990, however, there was a dearth of information regarding the molecular architectures of biotin-dependent enzymes. In recent years there has been an explosion in the number of three-dimensional structures reported for these proteins. Here we review our current understanding of the structures and functions of biotindependent enzymes. In addition, we provide a critical analysis of what these structures have and have not revealed about biotin-dependent catalysis.

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“…Briefly, ACCase activity was measured by coupling the production of ADP to the oxidation of NADH by PK and LDH (Rendina et al, 1988). The reaction was measured by following the change in Absorbance at 340 nm for 3 min at 30 0 C.…”

Section: Ac Case Assaymentioning

confidence: 99%

Analysis of Acetyl Co-A Carboxylase Activity in Marine Diatoms Isolated from Vellar Estuary, Southest Coast of India

Lawrence¹,

Suresh²,

Anantharaman³

2017

Int.J.Curr.Microbiol.App.Sci

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Kinetic characterization, stereoselectivity, and species selectivity of the inhibition of plant acetyl-CoA carboxylase by the aryloxyphenoxypropionic acid grass herbicides

Cited by 78 publications

References 22 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

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

Analysis of Acetyl Co-A Carboxylase Activity in Marine Diatoms Isolated from Vellar Estuary, Southest Coast of India

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Kinetic characterization, stereoselectivity, and species selectivity of the inhibition of plant acetyl-CoA carboxylase by the aryloxyphenoxypropionic acid grass herbicides

Cited by 78 publications

References 22 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

The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

Analysis of Acetyl Co-A Carboxylase Activity in Marine Diatoms Isolated from Vellar Estuary, Southest Coast of India

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The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms