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The metabolism of coenzyme A and control of its synthesis are reviewed. Pantothenate kinase is an important rate-controlling enzyme in the synthetic pathway of all tissues studied and appears to catalyze the flux-generating reaction of the pathway in cardiac muscle. This enzyme is strongly inhibited by coenzyme A and all of its acyl esters.
J D, Robishaw, J R, Neely
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CHEMICAL1 and enzymic2 studies from these two laboratories suggested that coenzyme A is best represented by formula (I) (cf. ref. 3). While the synthesis of various fragments of the molecule4 has lent considerable support to this structure, the enzymic and chemical evidence did not agree on one point.
J, BADDILEY +3 more
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Abstract An improved procedure for the chemical synthesis of coenzyme A by anhydride-anion exchange is described. A mixture of the 2′,5′- and 3′,5′-diphosphastes of adenosine is treated with diphenylphosphorochloridate to give P 1 -adenosine (2′3′-cyclic phosphate)-5′- P 2 -diphenylpyrophosphate quantitatively. This is then treated with pantethine
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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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