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Acetyl-CoA Carboxylase Inhibitors
2002Two 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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Enzyme Studies on Isoforms of Acetyl-CoA Carboxylase
1997Acetyl-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. +6 more
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Regulation of acetyl-CoA carboxylase by ADP-ribosylation
Biochemistry, 1986Because 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.
Joan M. McDermott, Lee A. Witters
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Acetyl‐CoA Carboxylase—a Graminicide Target Site
Pesticide Science, 1997Acetyl-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 +6 more
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Control of acetyl-CoA carboxylase by covalent modification
Molecular and Cellular Biochemistry, 1979In 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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Soybean Chloroplast Acetyl-CoA Carboxylase
1997Acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) catalyzes an ATP-dependent conversion of acetyl-CoA to malonyl-CoA, which is a regulated step in de novo synthesis of fatty acids that takes place in chloroplasts. In soybean, the chloroplast ACCase is apparently a multiprotein, prokaryotic type of complex [1], that is thought to consist of 4 subunits: biotin
Vadim Beilinson +3 more
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Coenzyme repression of acetyl-CoA carboxylase by (+)-biotin
Archives of Biochemistry and Biophysics, 1969Abstract Cell-free sonicated suspensions of L. plantarum were found to have acetyl-CoA carboxylase activity. The product of the reaction, which required ATP, acetyl-CoA and MnCl2 for maximum activity, was identified as malonyl-CoA. Avidin completely inhibited the reaction; the avidin effect was reversed by (+)-biotin.
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Mechanisms of regulation of acetyl-CoA carboxylase
1990One of the major physiological responses to insulin secretion is the activation of lipogenesis in target tissues (principally fat and liver). As acetyl-CoA carboxylase (ACC) is the rate limiting enzyme in fatty acid synthesis, the mechanisms involved in the short term regulation of this enzyme represent a pertinent model system for determining elements
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The participation of acetyl-CoA in pyruvate carboxylase
Biochemical and Biophysical Research Communications, 1966Terrance G. Cooper, C.R. Benedict
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