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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.
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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.
Janet 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.
Janet D. Robishaw, J. R. Neely
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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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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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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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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 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 Jadhav, Michael Yarus
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, 2012
Coenzymes are organic substances that participate like substrates in enzymatic reactions; however, unlike normal products the coenzymes are regenerated in subsequent reactions. Many, but not all coenzymes are vitamin derivatives. Vitamins are the dietary micronutrients that are required to produce these coenzymes.
H. Fromm, M. Hargrove
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Coenzymes are organic substances that participate like substrates in enzymatic reactions; however, unlike normal products the coenzymes are regenerated in subsequent reactions. Many, but not all coenzymes are vitamin derivatives. Vitamins are the dietary micronutrients that are required to produce these coenzymes.
H. Fromm, M. Hargrove
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Organometallic chemistry of b(12) coenzymes.
Metal ions in life sciences, 2009When coenzyme B(12) was identified as organometallic derivative of vitamin B(12), metal-carbon bonds were revealed to be relevant in life processes. Vitamin B(12), the "antipernicious anaemia factor" required for human health, was isolated earlier as a ...
B. Kräutler
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1965
Publisher Summary This chapter provides an overview of coenzymes and prosthetic groups. The terms coenzyme and prosthetic group are frequently used synonymously. Naturally, it is often difficult to decide what is easily dissociable and what is not, for there is a complete range of possibilities.
P. Karlson, Charles H. Doering
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Publisher Summary This chapter provides an overview of coenzymes and prosthetic groups. The terms coenzyme and prosthetic group are frequently used synonymously. Naturally, it is often difficult to decide what is easily dissociable and what is not, for there is a complete range of possibilities.
P. Karlson, Charles H. Doering
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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.
Bruce A. Lent, Ki-Han Kim
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