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Acetyl-coenzyme A synthetase (AMP forming) [PDF]

Cellular and Molecular Life Sciences, 2004
Acetyl-coenzyme A synthetase (AMP forming; Acs) is an enzyme whose activity is central to the metabolism of prokaryotic and eukaryotic cells. The physiological role of this enzyme is to activate acetate to acetyl-coenzyme A (Ac-CoA). The importance of Acs has been recognized for decades, since it provides the cell the two-carbon metabolite used in many
Jorge C. Escalante-Semerena, Vincent J. Starai   +1 more
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Novel mutations and expression changes of acetyl‐coenzyme A carboxylase are associated with spirotetramat resistance in Aphis gossypii Glover

Insect molecular biology (Print), 2017
Acetyl‐coenzyme A carboxylase (ACC) catalyses the carboxylation of acetyl‐coenzyme A (acetyl‐CoA) to produce malonyl‐CoA during the de novo synthesis of fatty acids. Spirotetramat, an inhibitor of ACC, is widely used to control a range of sucking insects,
Y. Pan, E. Zhu, X. Gao, R. Nauen, J. Xi, T. Peng, X. Wei, C. Zheng, Q. Shang   +8 more
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Measurement of acetyl coenzyme A in rat liver

Analytical Biochemistry, 1969
Abstract The estimation of acetyl CoA in rat liver samples by enzymic methods has been investigated with particular reference to the techniques used for obtaining the samples. In the assay it was found necessary to measure the NADH 2 produced in the coupled enzyme reaction fluorometrically and to add internal standards of acetyl CoA to the cuvet at
H.B. Stoner, Josephine Lumbers, C.J. Threlfall   +2 more
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Acetyl coenzyme A concentrations in plant tissues

Journal of Plant Physiology, 2004
Despite the importance of acetyl coenzyme A in many facets of metabolism and the availability of methods for estimation of its concentration, data for acetyl-CoA concentrations in plant tissues have been very scarce. A method using reversed phase HPLC for the quantitative estimation of acetyl-CoA was applied to a variety of plant tissues.
John B. Ohlrogge, Mike Pollard, Ajay W. Tumaney   +2 more
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On the biosynthesis of acetyl coenzyme a in the brain

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1965
Abstract 1. 1. A method for the investigation of the enzymic formation of acetyl-CoA from [1- 14 C]acetate, CoA ATP has been worked out. 2. 2. The formation of acetyl-CoA from acetate, CoA ATP in brain homogenates is mainly catalyzed by acetyl-CoA synthetase (acetate: CoA ligase (AMP), EC 6.2.1.1). 3. 3.
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Acetyl-coenzyme A carboxylase in maize leaves

Archives of Biochemistry and Biophysics, 1981
Abstract Purified chloroplasts from mesophyll and bundle sheath cells of maize leaves have been shown to be the location of acetyl-CoA carboxylase. In disrupted chloroplasts the enzyme was recovered in the stromal fraction, along with protein-bound biotin; acetyl-CoA carboxylase activity did not require a membrane component.
B.J. Nikolau, J.C. Hawke, C.R. Slack
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Coenzyme A and acetylation in various experimental obesities

American Journal of Physiology-Legacy Content, 1962
Coenzyme A concentration and in vivo acetylation of sulfanilamide were determined in genetically obese-hyperglycemic mice, their lean littermates, littermates made obese by injection of gold thioglucose, yellow-obese mice, and Swiss mice. Metabolically obese mice show an increased total liver and kidney coenzyme A content.
Jean Mayer, Marilyn M. Thompson
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5 Acetyl-Coenzyme A Carboxylase

1987
Publisher Summary This chapter summarizes the regulation of the specific activity of acetyl-CoA carboxylase from animal tissues, especially by phosphorylation. Acetyl-CoA carboxylase derived from both avian and mammalian sources has been shown to be activated under conditions that promote the aggregation of the dimers of the enzyme into linear ...
Richard M. Denton, Roger W. Brownsey
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Fermentative Pyruvate and Acetyl-Coenzyme A Metabolism

EcoSal Plus, 2004
Pyruvate and acetyl-CoA form the backbone of central metabolism. The nonoxidative cleavage of pyruvate to acetyl-CoA and formate by the glycyl radical enzyme pyruvate formate lyase is one of the signature reactions of mixed-acid fermentation in enterobacteria.
R. Gary Sawers, David P. Clark
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[8] Micromethod for the measurement of acetyl phosphate and acetyl coenzyme A

1986
The method described here utilizes two enzymes involved with acetyl-CoA and acetyl phosphate metabolism in bacteria to measure these compounds. Basically, the acetyl-CoA and acetyl phosphate in perchloric acid extracts are converted to ATP, in the presence of [3H]ADP of high specific activity, using the enzymes phosphotransacetylase (PTA) and acetate ...
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