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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 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
exaly   +3 more sources

Acetyl coenzyme A biosynthesis in the chloroplast

Planta, 1982
Acetyl coenzyme A (CoA) biosynthesis in spinach chloroplasts has been investigated by following the incorporation of bicarbonate and acetate into fatty acids under a variety of conditions. Both substrates were readily incorporated into fatty acids in a light-dependent manner by intact photosynthesising chloroplasts, but when the concentrations of these
Denis J Murphy, Murphy Denis J, Walker D A   +2 more
exaly   +3 more sources

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 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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Effect of salicylates on acetyl coenzyme a carboxylase

Biochemical Pharmacology, 1979
Abstract The effects of salicylates on rat and chicken liver acetyl-CoA carboxylase were investigated. Acetyl salicylate (2.5 mM) mimicked the activating effect of citrate on rat liver carboxylase if included during the preincubation period. The dissociated inactive form of chicken liver carboxylase could be reconstituted into the partially active ...
U, Dular, K, Dakshinamurti
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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
J, Lumbers, C J, Threlfall, H B, Stoner
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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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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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