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Structure of Coenzyme A [PDF]

open access: possibleNature, 1953
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.
E. M. Thain   +3 more
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Coenzyme A metabolism

American Journal of Physiology-Endocrinology and Metabolism, 1985
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.
Janet D. Robishaw, J. R. Neely
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Coenzymes I: Organic Coenzymes

2007
Most enzymatic reactions proceed with chemical changes that cannot be brought about by the side chains of amino acid residues. These enzymes function in cooperation with coenzymes and cofactors, which lend physicochemical potentialities not found in amino acids.
Perry A. Frey, Adrian D. Hegeman
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Coenzymes II: Metallic Coenzymes

2007
The original coenzymes were small organic molecules that activated enzymes and participated directly in catalyzing enzymatic reactions. Most of them were derived from vitamins and were known as biologically “activated” forms of vitamins such as niacin, riboflavin, thiamine, and pyridoxal.
Perry A. Frey, Adrian D. Hegeman
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