Coenzyme A activation of acetyl-CoA carboxylase.
نویسندگان
چکیده
منابع مشابه
Regulation of acetyl-coA carboxylase: properties of coA activation of acetyl-coA carboxylase.
Acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] is activated by physiological concentrations of CoA. The CoA concentration dependency of this activation is sigmoidal; below 60 microM there is little or no activation, but the activation observed between 60 and 120 microM indicates that small changes in the concentration of CoA can cause significant changes in ...
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medium containing [” Plphosphate, the distribution of 32P-labelled acetyl-CoA carboxylase in the fractions can be investigated and it has been found that a greater proportion of the phosphorylated enzyme is present in the polymeric form after exposure of the intact tissue to insulin. Present studies are concerned with investigating whether this polymeric active form is phosphorylated to a great...
متن کاملLiver acetyl CoA carboxylase: insight into the mechanism of activation by tricarboxylic acids and acetyl CoA.
Recent investigations in this laboratory have shownl 2 that the isocitrate(or citrate-) activated form of liver acetyl CoA carboxylase (E.C. 6.4.1.2) is a large protein structure having a molecular weight of about four million. Electron microscopic examination of the carboxylase in the presence of isocitrate reveals' that it has a filamentous structure with dimensions of SG-100 A by up to 5000 ...
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The mechanism underlying the ability of insulin to acutely activate acetyl-CoA carboxylase [acetyl-CoA: carbon-dioxide ligase (ADP-forming), EC 6.4.1.2; AcCoA-Case] has been examined in Fao Reuber hepatoma cells. Insulin promotes the rapid activation of AcCoACase, as measured in cell lysates, and this stimulation persists to the same degree after isolation of AcCoACase by avidin-Sepharose chrom...
متن کاملCharacterization of Maize Acetyl-Coenzyme A Carboxylase.
Maize (Zea mays L.) leaf acetyl-CoA carboxylase (ACCase) was purified about 500-fold by ammonium sulfate fractionation and gel filtration and blue Sepharose affinity and anion-exchange chromatography. Most ACCase activity (85%) recovered from the anion-exchange column was found in a highly purified fraction (specific activity 5.5 [mu]mol acid-stable product min-1 mg-1) that consisted primarily ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)69776-0