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Regulation of Acetyl-CoA Carboxylase

1983
Publisher Summary This chapter discusses the regulation of acetyl-CoA carboxylase. Acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of acetyl-CoA in the formation of malonyl-CoA. Malonyl-CoA is then condensed to acetyl-CoA in the process of long-chain fatty acid synthesis.
openaire   +3 more sources

Inhibition of acetyl CoA carboxylase by GTPγS

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
Abstract The effect of nonhydrolyzable guanine nucleotides on mammalian acetyl CoA carboxylase (ACC) activity was examined. Using porous rat adipocytes and crude fat cell homogenates to study metabolic pathway flux, GMPPNP and/or GTP γ S inhibited [ 14 C] fatty acid formation by up to 95% when either [6- 14 C]glucose-6-phosphate or [1- 14 C]acetyl ...
Tracy L VanderBloomer   +4 more
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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.
Erwin Stoll   +7 more
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Acetyl-CoA Carboxylase as Target for Herbicides

1989
The cyclohexane-1,3-dione and aryloxyphenoxypropionic acid-type herbicides are used as selective grass herbicides in several economical important crop cultures. They are known to block de novo fatty acid synthesis in the chloroplasts of sensitive grasses (Poaceae).
Focke, Manfred   +1 more
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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.
John B. Ohlrogge, Sarah C. Hunter
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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 ...
Kevin Salyers   +16 more
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Phosphorylation-activity relationships of AMPK and acetyl-CoA carboxylase in muscle.

Journal of applied physiology, 2002
AMP-activated protein kinase (AMPK) is activated during muscle contraction in response to the increase in AMP and decrease in phosphocreatine (PCr). Once activated, AMPK has been proposed to phosphorylate a number of targets, resulting in increases in ...
S. Park   +5 more
semanticscholar   +1 more source

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. Siebert, G. Siebert, Gerlinde Sturm
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Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase.

European Journal of Biochemistry, 1988
We have examined the sites phosphorylated on acetyl-CoA carboxylase by three protein kinases which have been shown to inactivate the enzyme, i.e. cyclic-AMP-dependent protein kinase, acetyl-CoA carboxylase kinase-2 (ACK2, purified from rat mammary gland)
M. Munday   +3 more
semanticscholar   +1 more source

AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation.

American Journal of Physiology. Endocrinology and Metabolism, 2000
AMP-activated protein kinase (AMPK) is a metabolic stress-sensing protein kinase responsible for coordinating metabolism and energy demand. In rodents, exercise accelerates fatty acid metabolism, enhances glucose uptake, and stimulates nitric oxide (NO ...
Zhi-ping Chen   +5 more
semanticscholar   +1 more source

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