Results 151 to 160 of about 13,638 (176)
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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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Dephosphorylation and activation of chicken liver acetyl‐coenzyme‐A carboxylase
European Journal of Biochemistry, 1983Studies were made on the dephosphorylation and activation of chicken liver acetyl‐coenzyme‐A carboxylase. The enzyme isolated by avidin‐Sepharose affinity chromatography in the presence of protein phosphatase inhibitors contained 4.9 ± 0.2 mol of alkali‐labile phosphate/mol subunit and had a specific activity of 3.5 ± 0.4 units/mg protein. The purified
K, Wada, T, Tanabe
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Acetyl coenzyme A carboxylase in species of Triticum of different ploidy
Planta, 1990The cellular amounts and cellular activities of acetyl CoA carboxylase (ACC; EC 6.4.1.2.) were determined in the first leaves of diploid, tetraploid and hexaploid species of Triticum (wheat). Per leaf the ACC activities were very similar in T. monococcum (2 χ), T. dicoccum (4 χ) and T. aestivum (6 χ). The ACC activity per chloroplast also showed little
J C, Hawke, R M, Leech
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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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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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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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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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Age‐Related Changes in Rat Hepatic Acetyl‐Coenzyme A Carboxylase
Proceedings of the Society for Experimental Biology and Medicine, 2000Abstract. Acetyl‐CoA carboxylase (ACC) catalyzes the rate‐limiting step in the synthesis of long‐chain fatty acids. Since aging influences adiposity, we studied the activity of ACC and its mRNA content in livers of 4‐, 12‐, and 24‐month‐old male Fischer 344 rats.
K G, Thampy, M J, Haas, A D, Mooradian
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Mechanisms of resistance to acetyl‐coenzyme A carboxylase inhibitors: a review
Pesticide Science, 1997Resistance to acetyl-coenzyme A carboxylase (ACCase) inhibitors has developed in at least 10 grass weed species in recent years. In most instances, resistance is conferred by an ACCase alteration in the resistant biotypes that reduces sensitivity to aryloxyphenoxypropionate (AOPP) and cyclohexanedione (CHD) herbicides.
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Acetyl coenzyme A carboxylase.
Current topics in cellular regulation, 1975M D, Lane, J, Moss, S E, Polakis
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