Results 201 to 210 of about 129,225 (257)
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Nature, 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.
J, BADDILEY +3 more
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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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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.
J D, Robishaw, J R, Neely
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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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Coenzyme A: to make it or uptake it?
Nature Reviews Molecular Cell Biology, 2016The consensus has been that intracellular coenzyme A (CoA) is obtained exclusively by de novo biosynthesis via a universal, conserved five-step pathway in the cell cytosol. However, old and new evidence suggest that cells (and some microorganisms) have several strategies to obtain CoA, with 4'-phosphopantetheine (P-PantSH; the fourth intermediate in ...
Sibon, Ody C. M., Strauss, Erick
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Biochimica et Biophysica Acta (BBA) - General Subjects, 1961
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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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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Coenzymes I: Organic Coenzymes
2007Most 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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Biochimie, 2002
Coenzymes are small organic molecules that supply a varied set of reactive groups to protein enzymes, thereby diversifying catalysis beyond the chemistries of amino acid sidechains. As RNA structures begin with a more limited chemical diversity than proteins, it seems likely that RNA enzymes would also use functional groups from other molecules to ...
Vasant R, Jadhav, Michael, Yarus
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Coenzymes are small organic molecules that supply a varied set of reactive groups to protein enzymes, thereby diversifying catalysis beyond the chemistries of amino acid sidechains. As RNA structures begin with a more limited chemical diversity than proteins, it seems likely that RNA enzymes would also use functional groups from other molecules to ...
Vasant R, Jadhav, Michael, Yarus
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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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Synthesis of arachidonoyl coenzyme A and docosahexaenoyl coenzyme A in retina
Current Eye Research, 1984The synthesis of 14C-labeled arachidonoyl coenzyme A (CoA) and docosahexaenoyl CoA was studied in the human, bovine, rat and frog retina. The synthesis of arachidonoyl CoA was two- to fourfold higher than that of docosahexaenoyl CoA in the retinal membranes examined.
T S, Reddy, N G, Bazan
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Coenzymes II: Metallic Coenzymes
2007The 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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