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Recent development in acetyl-CoA carboxylase inhibitors and their potential as novel drugs.
Future Medicinal Chemistry, 2020Acetyl-CoA carboxylase (ACC), a critical enzyme in the regulation of fatty acid synthesis and metabolism, has emerged as an attractive target for a plethora of emerging diseases, such as diabetes mellitus, nonalcoholic fatty liver disease, cancer ...
Xin Wu, Tonghui Huang
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Inhibitors of Mammalian Acetyl-CoA Carboxylase
Recent Patents on Cardiovascular Drug Discovery, 2007Inhibition of acetyl-CoA carboxylase (ACC), with its resultant inhibition of fatty acid synthesis and stimulation of fatty acid oxidation, has the potential to favorably affect, in a concerted manner, a multitude of the cardiometabolic risk factors associated with diabetes, obesity, and the metabolic syndrome.
Jeffrey W. Corbett, James H. Harwood
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Multi-subunit acetyl-CoA carboxylases
Progress in Lipid Research, 2002Acetyl-CoA carboxylase (ACC) catalyses the first committed step of fatty acid synthesis, the carboxylation of acetyl-CoA to malonyl-CoA. Two physically distinct types of enzymes are found in nature. Bacterial and most plant chloroplasts contain a multi-subunit ACC (MS-ACC) enzyme that is readily dissociated into its component proteins.
Grover L. Waldrop, John E. Cronan
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Resistance to acetyl-CoA carboxylase-inhibiting herbicides.
Pest Management Science, 2014Resistance to acetyl-CoA carboxylase herbicides is documented in at least 43 grass weeds and is particularly problematic in Lolium, Alopecurus and Avena species.
S. Kaundun
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Pest Management Science, 2017
BACKGROUND The occurrence of herbicide-resistant weed biotypes is increasing and this report of an acetyl-CoA carboxylase (ACCase) inhibitor-resistant Digitaria sanguinalis L. Scop. from southwestern Ontario is another example.
Martin Laforest+5 more
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BACKGROUND The occurrence of herbicide-resistant weed biotypes is increasing and this report of an acetyl-CoA carboxylase (ACCase) inhibitor-resistant Digitaria sanguinalis L. Scop. from southwestern Ontario is another example.
Martin Laforest+5 more
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Regulation and structure of the heteromeric acetyl-CoA carboxylase.
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2016The enzyme acetyl-CoA carboxylase (ACCase) catalyzes the committed step of the de novo fatty acid biosynthesis (FAS) pathway by converting acetyl-CoA to malonyl-CoA. Two forms of ACCase exist in nature, a homomeric and heteromic form. The heteromeric form of this enzyme requires four different subunits for activity: biotin carboxylase; biotin carboxyl ...
Matthew J Salie, J. Thelen
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Regulation of Acetyl-CoA Carboxylase
1983Publisher Summary This chapter discusses the regulation of acetyl-CoA carboxylase. Acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of acetyl-CoA in the formation of malonyl-CoA. Malonyl-CoA is then condensed to acetyl-CoA in the process of long-chain fatty acid synthesis.
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Inhibition of acetyl CoA carboxylase by GTPγS
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998Abstract The effect of nonhydrolyzable guanine nucleotides on mammalian acetyl CoA carboxylase (ACC) activity was examined. Using porous rat adipocytes and crude fat cell homogenates to study metabolic pathway flux, GMPPNP and/or GTP γ S inhibited [ 14 C] fatty acid formation by up to 95% when either [6- 14 C]glucose-6-phosphate or [1- 14 C]acetyl ...
Tracy L VanderBloomer+4 more
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The activation of acetyl CoA carboxylase by tricarboxylic acids
Advances in Enzyme Regulation, 1971Summary Acetyl CoA carboxylases from animal tissues are capable of oscillating between catalytically-inactive protomeric and catalytically-active polymeric states, the level of carboxylase activity being determined by the position of the protomer-polymer equilibrium.
Erwin Stoll+7 more
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Acetyl-CoA Carboxylase as Target for Herbicides
1989The cyclohexane-1,3-dione and aryloxyphenoxypropionic acid-type herbicides are used as selective grass herbicides in several economical important crop cultures. They are known to block de novo fatty acid synthesis in the chloroplasts of sensitive grasses (Poaceae).
Focke, Manfred+1 more
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