Results 271 to 280 of about 56,101 (298)

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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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, K A Walker, Kenneth E. Pallett, Lindsey J Price, S.M. Ridley, John L. Harwood, David J. Cole   +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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Soybean Chloroplast Acetyl-CoA Carboxylase

1997
Acetyl-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, S. V. Reverdatto, Niels C. Nielsen, Niels C. Nielsen   +3 more
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Plant acetyl-CoA carboxylase

Biochemical Society Transactions, 1986
A. R. Slabas, H. E. Bambridge, A. Hellyer   +2 more
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Coenzyme repression of acetyl-CoA carboxylase by (+)-biotin

Archives of Biochemistry and Biophysics, 1969
Abstract 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

1990
One 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, 1966
Terrance G. Cooper, C.R. Benedict
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Acetyl‐CoA Carboxylase Inhibitor GS‐0976 for 12 Weeks Reduces Hepatic De Novo Lipogenesis and Steatosis in Patients With Nonalcoholic Steatohepatitis

Clinical Gastroenterology and Hepatology, 2018
E. Lawitz, A. Coste, F. Poordad, N. Alkhouri, N. Loo, B. McColgan, J. Tarrant, Tuan Nguyen, Ling Han, C. Chung, A. Ray, J. Mchutchison, M. Subramanian, R. Myers, M. Middleton, C. Sirlin, R. Loomba, Edna Nyangau, M. Fitch, Kelvin W. Li, M. Hellerstein   +20 more
semanticscholar   +1 more source

Purification and crystallization of acetyl CoA carboxylase

Life Sciences, 1967
Shosaku Numa, Barbara Riedel, Tamotsu Goto, Erika Ringelmann   +3 more
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