Results 181 to 190 of about 113,959,850 (208)
Capillary electrophoretic assay of human acetyl‐coenzyme A carboxylase 2
Electrophoresis, 2019 © 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim Human acetyl-coenzyme A carboxylase 2 catalyzes the carboxylation of acetyl coenzyme A to form malonyl coenzyme A, along with the conversion of magnesium-adenosine triphosphate complex to magnesium ...
S Douglass Gilman
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Effect of salicylates on acetyl coenzyme a carboxylase
Biochemical Pharmacology, 1979Abstract The effects of salicylates on rat and chicken liver acetyl-CoA carboxylase were investigated. Acetyl salicylate (2.5 mM) mimicked the activating effect of citrate on rat liver carboxylase if included during the preincubation period. The dissociated inactive form of chicken liver carboxylase could be reconstituted into the partially active ...
U, Dular, K, Dakshinamurti
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Acetyl-coenzyme A carboxylase in maize leaves
Archives of Biochemistry and Biophysics, 1981Abstract Purified chloroplasts from mesophyll and bundle sheath cells of maize leaves have been shown to be the location of acetyl-CoA carboxylase. In disrupted chloroplasts the enzyme was recovered in the stromal fraction, along with protein-bound biotin; acetyl-CoA carboxylase activity did not require a membrane component.
B J, Nikolau, J C, Hawke, C R, Slack
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REGULATION OF MAMMALIAN ACETYL-COENZYME A CARBOXYLASE
Annual Review of Nutrition, 1997▪ Abstract Long-chain fatty acids are involved in all aspects of cellular structure and function. For controlling amounts of fatty acids, cells are endowed with two acetyl-coenzyme A carboxylase (ACC) systems. ACC-α is the rate-limiting enzyme in the biogenesis of long-chain fatty acids, and ACC-β is believed to control mitochondrial fatty acid ...
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Acetyl-coenzyme A carboxylase mRNA metabolism in the rat liver
Metabolism, 1992The acetyl-coenzyme A carboxylase (ACC) gene contains two promoters (PI and PII), both of which are active in the liver. Various physiological stimuli affect one, or both of the promoters of the ACC gene, and result in the generation of two classes of ACC mRNAs which differ in the composition of their 5' untranslated regions (5' UTR).
F, López-Casillas +2 more
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Maize Acetyl-CoEnzyme a Carboxylase Genes
1995Acetyl-coenzyme A carboxylase (ACCase) carboxylates acetyl-coenzyme A to malonyl-coenzyme A which serves as an intermediate metabolite for several diverse pathways in plant metabolism including synthesis of fatty acids, flavonoids, pigments and waxes. Plants likely have more than one ACCase isoform — one in the plastid for fatty acid synthesis and at ...
Burle Gengenbach +5 more
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Acetyl Coenzyme A Carboxylase: Filamentous Nature of the Animal Enzymes
Science, 1969Acetyl coenzyme A carboxylases purified from several animal tissues exist as enzymatically active polymeric filaments of high molecular weight and have similar electron microscopic, hydrodynamic, and catalytic properties. These filaments reversibly dissociate into inactive protomers of uniform size.
A K, Kleinschmidt, J, Moss, D M, Lane
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5 Acetyl-Coenzyme A Carboxylase
1987Publisher Summary This chapter summarizes the regulation of the specific activity of acetyl-CoA carboxylase from animal tissues, especially by phosphorylation. Acetyl-CoA carboxylase derived from both avian and mammalian sources has been shown to be activated under conditions that promote the aggregation of the dimers of the enzyme into linear ...
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Purification and characterization of maize leaf acetyl-coenzyme a carboxylase
Archives of Biochemistry and Biophysics, 1984Maize leaf acetyl-CoA carboxylase was purified from whole tissue homogenates by precipitation with polyethylene glycol and ammonium sulfate, and gel filtration. Recoveries were approximately 5% with 100-fold increases in specific activity. The molecular weight of the native enzyme is estimated at 500,000 from the elution volume of a calibrated Ultrogel
B J, Nikolau, J C, Hawke
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Crystal Structure of the Carboxyltransferase Domain of Acetyl-Coenzyme A Carboxylase
Science, 2003Acetyl–coenzyme A carboxylases (ACCs) are required for the biosynthesis and oxidation of long-chain fatty acids. They are targets for therapeutics against obesity and diabetes, and several herbicides function by inhibiting their carboxyltransferase (CT) domain.
Hailong, Zhang +3 more
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