Results 261 to 270 of about 56,101 (298)
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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
openaire   +3 more sources

The Bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl‐CoA carboxylase

Molecular Microbiology, 2015
Biosynthesis of fatty acids is one of the most fundamental biochemical pathways in nature. In bacteria and plant chloroplasts, the committed and rate‐limiting step in fatty acid biosynthesis is catalyzed by a multi‐subunit form of the acetyl‐CoA ...
E. C. Gerhardt   +6 more
semanticscholar   +1 more source

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
openaire   +3 more sources

The acetyl-CoA carboxylase enzyme: a target for cancer therapy?

Expert Review of Anticancer Therapy, 2015
As a rate-limiting enzyme, the acetyl-CoA carboxylase (ACC) is essential for fatty acid synthesis. Traditionally, the ACC has been a target of metabolic syndrome and obesity. Recent research has demonstrated that malignant tumors have a high energy flow,
Chao Wang   +5 more
semanticscholar   +1 more source

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.   +6 more
openaire   +3 more sources

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

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

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
openaire   +3 more sources

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.
Joan M. McDermott, Lee A. Witters
openaire   +3 more sources

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