Results 321 to 330 of about 86,728 (368)

The activation of acetyl CoA carboxylase by tricarboxylic acids

Advances in Enzyme Regulation, 1971
Summary Acetyl CoA carboxylases from animal tissues are capable of oscillating between catalytically-inactive protomeric and catalytically-active polymeric states, the level of carboxylase activity being determined by the position of the protomer-polymer equilibrium.
M D, Lane, J, Moss, E, Ryder, E, Stoll
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Regulation of Spinach Chloroplast Acetyl-CoA Carboxylase

Archives of Biochemistry and Biophysics, 1998
We have investigated several factors which influence acetyl-CoA carboxylase (ACCase) activity in lysed spinach chloroplasts. (1) When assayed after rapid lysis of light-incubated chloroplasts, ACCase activity was 2-fold higher than activity from dark-incubated chloroplasts.
S C, Hunter, J B, Ohlrogge
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Piperazine Oxadiazole Inhibitors of Acetyl-CoA Carboxylase

Journal of Medicinal Chemistry, 2013
Acetyl-CoA carboxylase (ACC) is a target of interest for the treatment of metabolic syndrome. Starting from a biphenyloxadiazole screening hit, a series of piperazine oxadiazole ACC inhibitors was developed. Initial pharmacokinetic liabilities of the piperazine oxadiazoles were overcome by blocking predicted sites of metabolism, resulting in compounds ...
Matthew P, Bourbeau, Aaron, Siegmund, John G, Allen, Hong, Shu, Christopher, Fotsch, Michael D, Bartberger, Ki-Won, Kim, Renee, Komorowski, Melissa, Graham, James, Busby, Minghan, Wang, James, Meyer, Yang, Xu, Kevin, Salyers, Mark, Fielden, Murielle M, Véniant, Wei, Gu   +16 more
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A study of acetyl CoA-carboxylase in adipose tissues

Zeitschrift für Ernährungswissenschaft, 1982
Acetyl-CoA-carboxylase activities were measured in adipose tissues of pigs during a breeding experiment for a low-fat line, and of rats and obese mice under different nutritional conditions. Acetyl-CoA-carboxylase behaves uniformly with the four major NADPH-generating dehydrogenases, like a block of lipogenic enzymes, and is found to be genetically ...
G, Sturm, G, Siebert
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Enzyme Studies on Isoforms of Acetyl-CoA Carboxylase

1997
Acetyl-CoA carboxylase is recognised generally as being a key enzyme in acyl lipid formation. In plants it has been shown to be important as a regulatory enzyme in light-driven lipid synthesis [1] and has a high flux control coefficient under such conditions [2]. Recently, characterisation of different isoforms of acetyl-CoA carboxylase from plants has
Price, L.J., Herbert, D., Alban, Claude, Job, D., Cole, D.J., Pallett, K.E., Harwood, J.L.   +6 more
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Regulation of acetyl-CoA carboxylase by ADP-ribosylation

Biochemistry, 1986
Because of certain similarities between acetyl-CoA carboxylase (ACC) and tubulin, and the recent demonstration of the ADP-ribosylation of tubulin by cholera toxin, we have investigated a potential role for ADP-ribosylation in the regulation of ACC activity.
L A, Witters, J M, McDermott
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Acetyl‐CoA Carboxylase—a Graminicide Target Site

Pesticide Science, 1997
Acetyl-CoA carboxylase catalyses the first committed step in fatty acid (and acyl lipid) formation. The enzyme has been shown to exert a high degree of flux control for lipid biosynthesis in leaves and, therefore, it is not surprising that chemicals which can inhibit it effectively are successful herbicides.
Derek Herbert, Kevin A. Walker, Lindsey J. Price, David J. Cole, Kenneth E. Pallett, Stuart M. Ridley, John L. Harwood   +6 more
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Control of acetyl-CoA carboxylase by covalent modification

Molecular and Cellular Biochemistry, 1979
In this review, various experiments which establish the occurrence of covalent modification mechanisms, both in vivo and in vitro, in the control of acetyl-CoA carboxylase have been presented. It is interesting to note that phosphorylation of the carboxylase results in disaggregation of the active species.
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Plant acetyl-CoA carboxylase

Biochemical Society Transactions, 1986
A, Hellyer, H E, Bambridge, A R, Slabas
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Acetyl-CoA Carboxylase Inhibitors

2002
Two important groups of herbicides, the cyclohexanediones (CHD) and aryloxyphenoxypropanoates (AOPP), inhibit the plastidic enzyme acetyl-CoA carboxylase (ACCase; E.C. 6.4.1.2). Representative compounds in these groups are shown in Fig. 1. A third class of inhibitor, based on a hybrid cyclic triketone structure, shows similar herbicidal activity ...
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