Results 191 to 200 of about 29,839 (226)

ATP-citrate lyase: A mini-review

Biochemical and Biophysical Research Communications, 2012
ATP-citrate lyase (ACLY) is a cytosolic enzyme that catalyzes generation of acetyl-CoA from citrate. Acetyl-CoA is a vital building block for the endogenous biosynthesis of fatty acids and cholesterol and is involved in isoprenoid-based protein modifications.
Melanie, Chypre, Nousheen, Zaidi, Karine, Smans   +2 more
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2-Hydroxy-N-arylbenzenesulfonamides as ATP-citrate lyase inhibitors

Bioorganic & Medicinal Chemistry Letters, 2007
A novel series of 2-hydroxy-N-arylbenzenesulfonamides were identified to be ATP-citrate lyase (ACL) inhibitors with compound 9 displaying potent in vitro activity (IC(50)=0.13 microM). Chronic oral dosing of compound 9 in high-fat fed mice lowered plasma cholesterol, triglyceride, and glucose, as well as inhibited weight gain.
James J, Li, Haixia, Wang, Joseph A, Tino, Jeffrey A, Robl, Timothy F, Herpin, R Michael, Lawrence, Scott, Biller, Haris, Jamil, Randy, Ponticiello, Luping, Chen, Ching-hsuen, Chu, Neil, Flynn, Dong, Cheng, Rulin, Zhao, Bangchi, Chen, Dora, Schnur, Mary T, Obermeier, Vito, Sasseville, Ramesh, Padmanabha, Kristen, Pike, Thomas, Harrity   +20 more
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Association of ATP citrate lyase with mitochondria

Biochemical and Biophysical Research Communications, 1980
Abstract (1) The association of ATP citrate lyase with mitochondria was studied with isolated rat hepatocytes and mitochondria. (2) When hepatocytes were treated with digitonin, about 25% of the lyase activity was released like a mitochondrial enzyme.
A M, Janski, N W, Cornell
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ATP citrate lyase in cholinergic nerve endings

Neurochemical Research, 1982
The activity of ATP-citrate lyase in homogenates of five selected rat brain regions varied from 2.93 to 6.90 nmol/min/mg of protein in the following order: cerebellum less than hippocampus less than parietal cortex less than striatum less than medulla oblongata and that of the choline acetyltransferase from 0.15 to 2.08 nmol/min/mg of protein in ...
A, Szutowicz, M, Stepień, H, Bielarczyk, J, Kabata, W, Lysiak   +4 more
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Comparison of phospho- and dephospho-ATP citrate lyase

Archives of Biochemistry and Biophysics, 1980
Abstract The dephospho- form of rat liver citrate lyase has been prepared by treating purified [32P]-ATP citrate lyase with a partially purified phosphatase. A comparison of the properties of the phospho- and dephosphoenzyme has been performed. The pH optima were the same for both forms of the enzyme in four different buffer systems although the ...
N S, Ranganathan, P A, Srere, T C, Linn
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[27] ATP citrate lyase (citrate-cleavage enzyme)

1969
Publisher Summary The chapter discusses three different methods by which ATP citrate lyase is assayed by determining the amount of acetyl-CoA or oxaloacetate formed. These methods are: The hydroxamate method: The acetyl-CoA formed is trapped as acetylhydroxamate and the latter is determined by the color produced with FeCl 3 .
Yoshiro Takeda, Fujio Suzuki, Hideo Inoue   +2 more
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Phospho-oligosaccharide dependent phosphorylation of ATP citrate lyase

Advances in Enzyme Regulation, 1990
The effect of insulin on ATP citrate lyase phosphorylation has been shown to be mimicked by a phospho-oligosaccharide in intact adipocytes. We demonstrate that the addition of phospho-oligosaccharide to intact adipocytes enhances the phosphorylation of ATP citrate lyase in the same tryptic peptide as insulin does.
J, Puerta, J M, Mato, S, Alemany
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ATP-citrate lyase activity in fungal extracts

Antonie van Leeuwenhoek, 1973
ATP-citrate lyase activity has been demonstrated in crude extracts from several species ofMortierella. This filamentous fungus characteristically stores lipid in the mycelium. The enzyme catalyses an ATP-dependent cleavage of citrate in the presence of CoA to oxaloacetic acid and acetylCoA.
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Characterization of ATP citrate lyase from Chlorobium limicola

Journal of Bacteriology, 1982
ATP citrate lyase (EC 4.1.3.8) from Chlorobium limicola was partially purified. It was established that the consumption of substrates and the formation of products proceeded stoichiometrically and that citrate cleavage was of the si-type. ADP and oxaloacetate inhibited enzyme activity. Oxaloacetate also inhibited the growth of C. limicola.
G, Antranikian, C, Herzberg, G, Gottschalk   +2 more
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Binding of hydroxycitrate to human ATP-citrate lyase

Acta Crystallographica Section D Structural Biology, 2017
Hydroxycitrate from the fruit ofGarcinia cambogia[i.e.(2S,3S)-2-hydroxycitrate] is the best-known inhibitor of ATP-citrate lyase. Well diffracting crystals showing how the inhibitor binds to human ATP-citrate lyase were grown by modifying the protein. The protein was modified by introducing cleavage sites forTobacco etch virusprotease on either side of
Jinhong, Hu, Aruna, Komakula, Marie E, Fraser   +2 more
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