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Mechanism of the synergistic action of oxythiamine and ketoconazole against the yeast Malassezia pachydermatis. [PDF]
Czerniecka M, Więcko A, Tylicki A.
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Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase.
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Acetyl-coenzyme A hydrolase in blood
International Journal of Biochemistry, 1981Abstract 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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Acetyl-coenzyme A synthetase (AMP forming)
Cellular and Molecular Life Sciences, 2004Acetyl-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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Requirement of acetyl-coenzyme A carboxylase kinase for coenzyme A
Archives of Biochemistry and Biophysics, 1983Phosphorylation 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, 1995The 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 +2 more
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Acetyl coenzyme A concentrations in plant tissues
Journal of Plant Physiology, 2004Despite 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 +2 more
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The origin of chloroplastic acetyl coenzyme A
Archives of Biochemistry and Biophysics, 1981Abstract 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, 1981Abstract 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, 2004Pyruvate 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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