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Case Report: Myoclonic and tremulous movements associated with COQ8A-related coenzyme Q10 deficiency type 4. [PDF]
Front GenetWang D, Zhang G, Fang X, Liu F, Wang L.
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A targeted metabolomic method to detect epigenetically relevant metabolites. [PDF]
Mol MetabMiro-Blanch J +10 more
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New Insights on Mitochondria-Targeted Neurological Drugs. [PDF]
Biology (Basel)Lores-Arnaiz S.
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Profiles of paediatric patients experiencing stroke-like episodes associated with mitochondrial disease. [PDF]
Front NeurolMolla GK +17 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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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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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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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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