Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.2.1.13 (acetyl-CoA synthetase)
 451 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of choline acetyltransferase and ATP-citrate lyase were significantly correlated (r = 0.995) in fractions of small and large synaptosomes isolated from rat hippocampus and cerebellum. The activities of these two enzymes did not correlate with those of pyruvate dehydrogenase, carnitine acetyltransferase, citrate synthase, acetyl-CoA synthetase, lactate dehydrogenase, or with the rate of high-affinity glutamate uptake in the synaptosomal fractions. The results provide additional evidence linking ATP-citrate lyase to the cholinergic system in the brain.
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PMID:ATP-citrate lyase and other enzymes of acetyl-CoA metabolism in fractions of small and large synaptosomes from rat brain hippocampus and cerebellum. 613 19

The influence of phenylacetate, phenylbutyrate, and phenylacetyl-CoA on the activity of choline acetyltransferase and S-acetyl-CoA synthetase was investigated in vitro. Phenylacetyl-CoA was found to be a very potent inhibitor of choline acetyltransferase, competitive for acetyl-CoA with Ki of 3.1 X 10(-7)M. In contrast, millimolar concentrations of phenylacetate and phenylbutyrate were required to inhibit the activity of the enzyme. Activity of S-acetyl-CoA synthetase was affected only slightly by the three agents in concentrations of 10(-3)-10(-2)M. At this time, results are interpreted to suggest that in phenylketonuria, phenylacetate exerts its neurotoxic action through its metabolic product, phenylacetyl-CoA, which could severely decrease the availability of acetyl-CoA.
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PMID:On the possible mechanism of phenylacetate neurotoxicity: inhibition of choline acetyltransferase by phenylacetyl-CoA. 614 28

Rat liver cytoplasmic acetyl-CoA synthetase was partially purified (purification factor = 23, yield = 30%). The apparent Kms for acetate, coenzyme A, ATP and MgCl2 were determined and found to be 52.5 microM, 50.5 microM, 570 microM and 1.5 mM, respectively. The partially-purified enzyme showed a low affinity for short-chain carbon substrates other than acetate. The properties of the partially-purified enzyme were compared with those of enzymes from other sources.
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PMID:Partial purification of rat liver cytoplasmic acetyl-CoA synthetase; characterization of some properties. 614 83

The effect of hypolipidemic drugs, WY14643 and DH990, on plant lipid metabolism has been studied. The total incorporation of [14C]acetate into lipids was inhibited by addition of both drugs to aged potato (Solanum tuberosum) tuber discs, spinach (Spinacia oleracea) leaves, and spinach chloroplasts, while the incorporation in Chlorella vulgaris cells was affected only by DH990. Moreover, DH990 inhibited the incorporation of 14C-labeled fatty acids into phosphatidylcholine and phosphatidylethanolamine of potato discs, and decreased the incorporation into phosphatidylglycerol of Chlorella cells. DH990 inhibited the formation of polyunsaturated fatty acids in potato discs, Chlorella cells, and spinach leaves, whereas WY14643 had no effect on the formation of these fatty acids. Stearoyl-ACP desaturase from safflower (Carthamus tinctorius) seeds was very sensitive to both drugs, especially DH990, which completely blocked the activity at 2 mM levels. When safflower lysophospholipid acyltransferases were solubilized by detergent treatment, only DH990 inhibited the incorporation of [14C]oleoyl-CoA into lysophosphatidylcholine or lysophosphatidylethanolamine. Both drugs inhibited fatty acid synthesis from [14C]malonyl-CoA in the microsomal fraction from safflower seeds, but only DH990 inhibited FAS activity in the soluble fraction; both drugs inhibited severely the formation of stearic acid. Both acetyl-CoA carboxylase and acetyl-CoA synthetase were sensitive to both drugs.
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PMID:The effect of hypolipidemic drugs on plant lipid metabolism. 648 26

Saccharin analogues were observed to be potent antihyperlipidemic agents at 20 mg/kg/day in rodents, significantly reducing both serum cholesterol and triglyceride levels in both normal and atherogenic mice. The saccharin analogues suppressed in vitro and in vivo liver enzymatic activity of acetyl-CoA synthetase, citrate lyase, and mitochondrial citrate exchange leading to a reduction of available cytoplasmic acetyl-CoA, which is required for the synthesis of cholesterol and fatty acids. Liver acetyl-CoA carboxylase, phosphatidate phosphohydralase, and glycerol-3-phosphate acyl transferase activities were markedly reduced by the saccharin analogues. Suppression of these enzymes would lead to a reduction of triglyceride synthesis. The saccharin analogues accelerated bile excretion of cholesterol metabolites and increased the fecal excretion of the cholesterol, triglycerides, neutral lipids, and phospholipids. The liver and plasma lipoprotein lipid content (including cholesterol, triglycerides, and neutral lipids) was markedly reduced by the saccharin analogues, whereas phospholipid content was elevated. The reduction of lipid content of serum chylomicron, very low-density, low-density, and high-density lipoprotein fractions by the saccharin analogues indicates that these agents may be useful in controlling hyperlipidemic diseases where specific lipoprotein fractions are elevated.
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PMID:Antihyperlipidemic activity of saccharin analogues in rodents. 664 71

Candida tropicalis, a representative alkane- and higher fatty acid-utilizing yeast, can grow on propionate used as sole carbon and energy source. Initial pH of the medium markedly affected the growth of the yeast on propionate. In propionate-grown cells, several enzymes associated with peroxisomes and/or participating in propionate metabolism were induced in connection with the appearance of the characteristic peroxisomes. Acetate-grown cells of this yeast had only few peroxisomes, while alkane-grown cells contained conspicuous numbers of the organelles. As compared with alkane-grown cells, some specific features were observed in peroxisomes and enzymes associated with the organelles of propionate-grown cells: The shape of peroxisomes was large but the number was small; unlike localization of catalase in peroxisomes of alkane-grown cells, the enzyme of propionate-grown cells was mainly localized in cytoplasm; as for carnitine acetyltransferase localized almost equally in peroxisomes and mitochondria in alkane-grown cells, propionate-grown cells contained mainly the mitochondrial type enzyme. A propionate-activating enzyme, which was different from acetyl-CoA synthetase, was also induced in cytoplasm of propionate-grown cells. The role of carnitine acetyltransferase and the propionate-activating enzyme in propionate metabolism is discussed in comparison with the role of carnitine acetyltransferase and acetyl-CoA synthetase in acetate metabolism.
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PMID:Induction and subcellular localization of enzymes participating in propionate metabolism in Candida tropicalis. 666 Sep 94

The mode of action of carnitine on the growth of the yeast Torulopsis bovina ATCC 26014 was investigated. When 0.5-5 microM L-carnitine was added to the medium, the growth rate doubled for both aerobic and anaerobic cultures. Cells grown in the absence of carnitine contain 0.4 nmol of L-carnitine/g, wet weight, but with 5 microM L-carnitine in the media, cells contain 1400 nmol of carnitine/g, wet weight, by the end of exponential growth. When [1-14C]acetyl-L-carnitine was added to growth media, almost all of the radioactivity became cell-associated. Most of the 14C was incorporated into cell protein although considerable 14C was recovered in the fatty acid fraction of saponified cells. Analyses of the amino acids derived from radiolabeled protein showed that the acetyl[14C] of acetylcarnitine was in glutamate, arginine, proline, leucine, and lysine. In contrast, [1-14C]acetate labeled leucine and lysine. Isopycnic density gradient analysis demonstrated that carnitine acetyltransferase was primarily associated with mitochondria, while acetyl-CoA synthetase and acetyl-CoA hydrolase were cytosolic. Isolated mitochondria incorporated [14C]acetylcarnitine radioactivity into citrate and 2-oxoglutarate. The data are consistent with carnitine facilitating the transfer of acetyl groups from the cytosol into mitochondria for synthesis of citrate and its metabolites. These results demonstrate a role for carnitine in biosyntheses in the yeast T. bovina.
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PMID:A biosynthetic role for carnitine in the yeast Torulopsis bovina. 668 27

Two short-chain fatty acyl-CoA synthetases were extracted from the photosynthetic bacterium, Rhodopseudomonas sphaeroides, and partially purified by column chromatography on Sephacryl S-200 and DEAE-cellulose. One enzyme activated propionate, valerate, acrylate, butyrate, and acetate, and was designated as propionyl-CoA synthetase, since the highest activity and lowest Km value (0.6 mM) were observed with propionate. The other enzyme activated acetate, propionate and acrylate. It showed the highest activity and lowest Km value (0.37 mM) for acetate, and was identified as acetyl-CoA synthetase [EC 6.2.1.1].
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PMID:Short-chain acyl-coenzyme A synthetases in Rhodopseudomonas sphaeroides. 697 35

1. The mean volume of adipocytes, the rates of fatty acid and acylglycerol glycerol synthesis from various precursors (in vitro), the rates of oxidation of acetate and glucose (in vitro) and the activities of lipoprotein lipase and various lipogenic enzymes were determined for perirenal adipose tissue from foetal lambs during the last month of gestation. 2. The fall in the rate of growth of perirenal adipose tissue during the last month of gestation is associated with a diminished capacity for fatty acid synthesis and lipoprotein lipase activity, but no change in the rate of acylglycerol glycerol synthesis was observed. There was no fall in the activities of cytosolic acetyl-CoA synthetase or the NADP-linked dehydrogenases, suggesting that the decrease in the rate of fatty acid synthesis was due to an impairment at the level of acetyl-CoA carboxylase or fatty acid synthetase. 3. The rate of fatty acid synthesis from acetate was greater than that from glucose. The rate of fatty acid synthesis from glucose per adipocyte of foetal lambs was similar to that of young sheep. The characteristic metabolism of adipose tissue of the adult sheep is thus present in the foetus, despite the relatively large amounts of glucose in the foetal 'diet'.
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PMID:Aspects of adipose-tissue metabolism in foetal lambs. 703 12

Some naturally occurring pseudoguaianolides and germacranolides as well as synthetic related compounds were observed to be antihyperlipidemic agents in mice. Several of these compounds at a dose of 20 mg/kg/day resulted in lowering of serum cholesterol by approximately 30% and of serum triglycerides by approximately 25%. Thiol-bearing enzymes of lipid synthesis, i.e., acetyl-CoA, citrate-lyase, acetyl-CoA synthetase, and beta-hydroxy-beta-methylglutaryl-CoA reductase, were inhibited by these agents in vitro, supporting the premise that these agents alkylate thiol nucleophiles by a Michael-type addition. The alpha-methylene-gamma-lactone moiety, the beta-unsubstituted cyclopentenone ring, and the alpha-epoxycyclopentanone system of these compounds appeared to be responsible for the lowering of serum lipids.
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PMID:Antihyperlipidemic activity of sesquiterpene lactones and related compounds. 720 85


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