Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.4.1.2 (acetyl-CoA carboxylase)
 2,876 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Partially purified acetyl-CoA carboxylase was covalently bound to a Sepharose 4B matrix. Although aggregation was thus prevented, the enzymic activity was stimulated by citrate and isocitrate.
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PMID:Activation of immobilized acetyl-Coenzyme A carboxylase. 2 39

2-Methylcitrate was tested in vitro on enzymes which interact with citrate and isocitrate. It was found to inhibit citrate synthase, aconitase, the NAD+- and NADP+-linked isocitrate dehydrogenase. This inhibition was competitive in nature except in the case of aconitase, and the Ki for all the enzymes was in the range of 1.5-7.6 mM. Phosphofructokinase was also inhibited by 2-methylcitrate with 50% inhibition achieved at 1 mM. ATP-citrate lyase and acetyl-CoA carboxylase were not inhibited by this compound. 2-Methylcitrate was not a substrate for ATP-citrate lyase. Acetyl-CoA carboxylase was activated by 2-methylcitrate with a Ka of 2.8 mM. The apparent Km (3.3 mM) for 2-methylcitrate for the mitochondrial citrate transporter was about 10-fold higher than the apparent Km (0.26 mM) for citrate. The tricarboxylase carrier can also be inhibited by low concentrations (0.2 mM) of 2-methylcitrate when the concentration of citrate is close to the apparent Km. Accumulation of 2-methylcitrate inside the mitochondrion, therefore, might lead to inhibition of enzymes in the citric acid cycle and thereby contribute to the ketogenesis and hypoglycemia seen under these conditions.
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PMID:Effect of 2-methylcitrate on citrate metabolism: implications for the management of patients with propionic acidemia and methylmalonic aciduria. 12 73

Acetyl-coenzyme A carboxylase from Euglena gracilis strain Z was isolated as a component of a multienzyme complex which includes phosphoenolpyruvate carboxylase and malate dehydrogenase. The multienzyme complex was shown to exist in crude extracts and was purified to a homogeneous protein with a molecular weight of 360,000 by gel filtration. The ratio of the activities of the constituent enzymes was acetyl-CoA carboxylase:phosphoenolpyruvate carboxylase:malate dehydrogenase, 1:25:500. The complex is proposed to operate in conjunction with malic enzyme, which is present in Euglena, to facilitate the formation of substrates, malonyl-CoA, and NADPH, for fatty acid biosynthesis. The interaction of the enzymes may represent a means of control of acetyl-CoA carboxylase activity in organisms which do not possess an enzyme subject to allosteric regulation. The acetyl-CoA carboxylase activity from Euglena is unaffected by citrate and isocitrate.
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PMID:A multienzyme complex for CO2 fixation. 23 76

9-Oxononanoic acid, which is one of the major products of the autoxidation of linoleic acid, was administered orally to rats and its effect on hepatic lipid metabolism was investigated. The de novo synthesis of fatty acids was strongly reduced 30 h after the administration of 100 mg of 9-oxononanoic acid as compared to that in the saline-administered group. Activity of acetyl-CoA carboxylase decreased by 60% and the activity of carnitine palmitoyltransferase increased by 35% in the test group. The level of triacylglycerols in serum was low and the level of free fatty acids remained unchanged. Thus, the administration of 9-oxononanoic acid decreased hepatic lipogenesis. It is generally believed that the reduction in lipogenesis is facilitated by a decrease in the NADPH level. The ratio of NADPH/NADP in the test group, however, became high as compared to that in the control group, and the activities of glucose 6-phosphate and isocitrate dehydrogenases increased. On the other hand, the levels of CoA derivatives, especially long-chain acyl-CoA, were higher in the test group than in the control. Therefore, the reduction of hepatic lipogenesis in the 9-oxononanoic acid group could be attributed to the inhibition of acetyl-CoA carboxylase by the accumulated long-chain acyl-CoA.
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PMID:Effect of orally administered 9-oxononanoic acid on lipogenesis in rat liver. 289 34

Fatty acid-biosynthetic activity in rat liver cytosol fractions is much greater when the bivalent cation in the assay system is Mn(2+) than when it is Mg(2+). This difference between bivalent cations can be abolished if the cytosol fractions are preincubated with isocitrate and the bivalent cation for 30min before assay of fatty acid-biosynthetic activity. In a search for the biochemical basis of this phenomenon, the following differences between Mg(2+) and Mn(2+) were established: (1) Mn(2+) promotes acetyl-CoA carboxylase activity of the protomeric form of the enzyme under conditions in which Mg(2+) does not; (2) Mn(2+)+ATP have little inhibitory effect on the polymerization of acetyl-CoA carboxylase whereas Mg(2+)+ATP are markedly inhibitory; (3) under conditions in which utilization of malonyl-CoA in condensation reactions is prevented, the steady-state concentration of malonyl-CoA formed by a cytosol fraction is much greater with Mn(2+) than with Mg(2+). The role that each of these specific differences between Mn(2+) and Mg(2+) might play in causing liver cytosol preparations to have greater fatty acid-biosynthetic activity in the presence of Mn(2+) is discussed.
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PMID:Differences between manganese and magnesium ions with regard to fatty acid biosynthesis, acetyl-coenzyme A carboxylase activity and malonyl-coenzyme A decarboxylation. 547 65

During the formation of two layers of adipose tissue in the pig's body, starting from the 80th day after birth, samples were obtained by biopsy and analyzed for gross constituents and enzymes concerned with fatty-acid biosynthesis. These two layers differ in total lipid and water content and demonstrate more subtle differences amongst DNA, protein, collagen and sodium concentrations when comparisons are made in regard to age, sex, and breeding selection for low-fat animals. Acetyl-CoA carboxylase, malic enzyme and glucose-6-phosphate dehydrogenase are more active in the inner layer, while 6-phosphogluconate and isocitrate dehydrogenases are distinguishable in the two layers of adipose tissue as well if age, sex, and breeding line are taken into consideration. The data form the basis for a more detailed study of lipogenic potentials in adipose tissue (next paper).
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PMID:Biochemical characterization of the layers of subcutaneous adipose tissue in the pig body. 612 11