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Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase.

The Journal of biological chemistry, 1966
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Acetyl-coenzyme A synthetase (AMP forming)

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
V J, Starai, J C, Escalante-Semerena
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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.
Ajay W, Tumaney, John B, Ohlrogge, Mike, Pollard   +2 more
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Acetyl-coenzyme A hydrolase in blood

International Journal of Biochemistry, 1981
Abstract 1. 1. The existence of acetyl-coenzyme A hydrolase (AcCoA-H) in human blood has been demonstrated for the first time, with highest specific activity in RBCs and lowest in plasma. 2. 2. It has a pH optimum at 8.0. 3. 3. The RBC AcCoA-H inhibited but the plasma AcCoA-H is stimulated by 0.1–0.4 M NaCl.
L L, Hsu, J L, Claghorn
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Requirement of acetyl-coenzyme A carboxylase kinase for coenzyme A

Archives of Biochemistry and Biophysics, 1983
Phosphorylation and inactivation of acetyl-coenzyme A (CoA) carboxylase by acetyl-CoA carboxylase kinase in the presence of ATP and Mg2+ requires coenzyme A. Coenzyme A did not enhance the phosphorylation of alternative substrates of the carboxylase kinase such as protamine or histones.
B A, Lent, K H, Kim
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Efficient Synthesis of Radiolabeled Propionyl-Coenzyme A and Acetyl-Coenzyme A

Analytical Biochemistry, 1995
The efficient microscale synthesis of [1-14C]propionyl-CoA from commercially available sodium [1-14C]-propionate using 1,1'-carbonyldiimidazole in yields of nearly 70% is reported for the first time. A substantial improvement in the process for making [1-14C]acetyl-CoA from sodium [1-14C]acetate was also achieved.
V B, Rajgarhia, N D, Priestley, W R, Strohl   +2 more
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The origin of chloroplastic acetyl coenzyme A

Archives of Biochemistry and Biophysics, 1981
Abstract Pyruvic dehydrogenase activity has been examined in a number of highly purified leaf organelles. In spinach leaf cell, the major activity is in the mitochrondrion with low activity in isolated chloroplasts. The major source of CO2 derived from pyruvic acid metabolism in the isolated chloroplast is via the acetolactic synthase reaction ...
D J, Murphy, P K, Stumpf
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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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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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Malonate, Malonyl‐Coenzyme A, and Acetyl‐Coenzyme A in Developing Rat Brain

Journal of Neurochemistry, 1984
Abstract: Free malonate, malonyl‐coenzyme A (malonyl‐CoA), and acetyl‐CoA were assayed in rat brain at developmental ages from the 20th day of gestation to 60 days of postnatal life. The determination of malonate was based on its conversion to malonyl‐CoA and decarboxylation to acetyl‐CoA by enzyme extracts from Pseudo‐monas fluorescens. The resulting
E J, Mitzen, A H, Koeppen
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