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Chemical Compound Review

coenzyme A     [(2R,3S,4R,5R)-5-(6- aminopurin-9-yl)-4...

Synonyms: Zeel, CoA-SH, Depot-Zeel, S-propanoate, coenzymes A, ...
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Disease relevance of coenzyme A


High impact information on coenzyme A

  • Lack of regulation of enzyme activity by free CoASH suggests that PTE-Ia and PTE-Ic regulate intraperoxisomal levels of acyl-CoA, and they may have a function in termination of beta-oxidation of fatty acids of different chain lengths [6].
  • The uptake of fatty acid in the presence of non-limiting amounts of ATP and CoASH was dependent on the amount of endogenous fatty acyl-CoA synthetase either retained within vesicles during isolation or trapped within vesicles after isolation by freeze-thawing [7].
  • When CoASH and ATP were present there was also a linear accumulation of acyl-CoA thioesters (plus derived polar lipids), with no measurable lag phase (<30 s), indicating that the FFA pool supplying LACS rapidly reached steady state [8].
  • PTE-2 activity is inhibited by free CoASH, suggesting that intraperoxisomal free CoASH levels regulate the activity of this enzyme [9].
  • To prevent CoASH sequestration and to facilitate excretion of chain-shortened carboxylic acids, acyl-CoA thioesterases, which catalyze the hydrolysis of acyl-CoAs to the free acid and CoASH, may play important roles [9].

Chemical compound and disease context of coenzyme A

  • The key step of the pathway, the dehydration of (R)-lactate required acetyl phosphate and CoASH under anaerobic conditions [10].
  • In Escherichia coli K-12 cells, the addition of reagents to inhibit the respiratory system led to a rapid decrease in the amount of acetyl-CoA with a concomitant increase in the amount of CoASH, whereas the addition of cerulenin, a specific inhibitor of fatty acid synthase, triggered the intracellular accumulation of malonyl-CoA [4].
  • As carnitine conjugation is thought to be the only detoxification metabolic route in canine muscle, under certain circumstances such as carnitine deficiency, the risk of exposure with toxic pivaloyl CoA might increase and the CoASH pool in canine muscle might be exhausted, resulting in toxicity in canine muscle [11].

Biological context of coenzyme A


Anatomical context of coenzyme A


Associations of coenzyme A with other chemical compounds

  • An azido-125I-CoA photolabel was synthesized from N-(3-iodo-[125I]4-azidophenylpropionamido)cysteinyl- 5-(2'thiopyridyl) cysteine ([125I]ACTP) and CoASH, separated by chromatography on a silica gel TLC, and identified by autoradiography [21].
  • Lysyl-tRNA synthetase aminoacylates CoA-SH with lysine, leucine, threonine, alanine, valine, and isoleucine [15].
  • For comparison, the equilibrium constant for the reaction CoASH + GSSG in equilibrium CoASSG + GSH was found to be 3.1 at pH 8 [22].
  • HoPan triggered significant changes in hepatic gene expression that substantially increased the thioesterases, which liberate CoASH from acyl-CoA, and increased pyruvate dehydrogenase kinase 1, which prevents the conversion of CoASH to acetyl-CoA [23].
  • These results identify the metabolic rearrangements that maintain the CoASH pool which is critical to mitochondrial functions, including gluconeogenesis, fatty acid oxidation, and the tricarboxylic acid and urea cycles [23].

Gene context of coenzyme A

  • The apo-PCP fragment was covalently modified to phosphopantetheinylated holo-PCP by pure Lys5 and CoASH with a Km of 1 microM and kcat of 3 min-1 for both the PCP and CoASH substrates [24].
  • In this study, mechanistic aspects of the AANAT-catalyzed alkyl transfer reaction were explored by employing CoASH and a series of N-haloacetyltryptamines that were also evaluated for their AANAT acetyltransferase inhibitory activities [25].
  • Neither oleoyl CoA, oleic acid, nor CoASH altered overall I-FABP rotational correlation time [26].
  • Further, ligands such as fatty acids, fatty acyl CoAs, and/or CoASH differentially modulate the I-FABP and L-FABP dynamics, and the ligand binding sites of these proteins differ in their ability to order the ligands [26].
  • Brain acyl-CoA hydrolase (BACH) hydrolyzes long-chain acyl-CoAs to free fatty acids and CoA-SH [27].

Analytical, diagnostic and therapeutic context of coenzyme A


  1. Escherichia coli alpha-ketoglutarate dehydrogenase complex. Steginsky, C.A., Frey, P.A. J. Biol. Chem. (1984) [Pubmed]
  2. Loading peptidyl-coenzyme A onto peptidyl carrier proteins: a novel approach in characterizing macrocyclization by thioesterase domains. Sieber, S.A., Walsh, C.T., Marahiel, M.A. J. Am. Chem. Soc. (2003) [Pubmed]
  3. Effects of fasting on tissue contents of coenzyme A and related intermediates in rats. Jenniskens, F.A., Jopperi-Davis, K.S., Walters, L.C., Schorr, E.N., Rogers, L.K., Welty, S.E., Smith, C.V. Pediatr. Res. (2002) [Pubmed]
  4. Changes in the size and composition of intracellular pools of nonesterified coenzyme A and coenzyme A thioesters in aerobic and facultatively anaerobic bacteria. Chohnan, S., Furukawa, H., Fujio, T., Nishihara, H., Takamura, Y. Appl. Environ. Microbiol. (1997) [Pubmed]
  5. CoASH and CoASSG levels in lungs of hyperoxic rats as potential biomarkers of intramitochondrial oxidant stresses. O'Donovan, D.J., Rogers, L.K., Kelley, D.K., Welty, S.E., Ramsay, P.L., Smith, C.V. Pediatr. Res. (2002) [Pubmed]
  6. Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases. Westin, M.A., Alexson, S.E., Hunt, M.C. J. Biol. Chem. (2004) [Pubmed]
  7. Biochemical demonstration of the involvement of fatty acyl-CoA synthetase in fatty acid translocation across the plasma membrane. Schmelter, T., Trigatti, B.L., Gerber, G.E., Mangroo, D. J. Biol. Chem. (2004) [Pubmed]
  8. On the export of fatty acids from the chloroplast. Koo, A.J., Ohlrogge, J.B., Pollard, M. J. Biol. Chem. (2004) [Pubmed]
  9. Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. Hunt, M.C., Solaas, K., Kase, B.F., Alexson, S.E. J. Biol. Chem. (2002) [Pubmed]
  10. On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum. Schweiger, G., Buckel, W. FEBS Lett. (1984) [Pubmed]
  11. Possible mechanism for species difference on the toxicity of pivalic acid between dogs and rats. Yamaguchi, T., Nakajima, Y., Nakamura, Y. Toxicol. Appl. Pharmacol. (2006) [Pubmed]
  12. Regulation of pantothenate kinase by coenzyme A and its thioesters. Vallari, D.S., Jackowski, S., Rock, C.O. J. Biol. Chem. (1987) [Pubmed]
  13. The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase. Huhtinen, K., O'Byrne, J., Lindquist, P.J., Contreras, J.A., Alexson, S.E. J. Biol. Chem. (2002) [Pubmed]
  14. Dynamic 13C NMR analysis of oxidative metabolism in the in vivo canine myocardium. Robitaille, P.M., Rath, D.P., Abduljalil, A.M., O'Donnell, J.M., Jiang, Z., Zhang, H., Hamlin, R.L. J. Biol. Chem. (1993) [Pubmed]
  15. Amino acid selectivity in the aminoacylation of coenzyme A and RNA minihelices by aminoacyl-tRNA synthetases. Jakubowski, H. J. Biol. Chem. (2000) [Pubmed]
  16. Epothilone biosynthesis: assembly of the methylthiazolylcarboxy starter unit on the EpoB subunit. Chen, H., O'Connor, S., Cane, D.E., Walsh, C.T. Chem. Biol. (2001) [Pubmed]
  17. Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart. Evidence that the dominant cardiac CPT I isoform is identical to the skeletal muscle enzyme. Weis, B.C., Cowan, A.T., Brown, N., Foster, D.W., McGarry, J.D. J. Biol. Chem. (1994) [Pubmed]
  18. Bile acid: CoASH ligases from guinea pig and porcine liver microsomes. Purification and characterization. Vessey, D.A., Benfatto, A.M., Kempner, E.S. J. Biol. Chem. (1987) [Pubmed]
  19. Formation of a free acyl adenylate during the activation of 2-propylpentanoic acid. Valproyl-AMP: a novel cellular metabolite of valproic acid. Mao, L.F., Millington, D.S., Schulz, H. J. Biol. Chem. (1992) [Pubmed]
  20. Myocardial accumulation of iodinated beta-methyl-branched fatty acid analogue, iodine-125-15-(p-iodophenyl)-3-(R,S)methylpentadecanoic acid (BMIPP), in relation to ATP concentration. Fujibayashi, Y., Yonekura, Y., Takemura, Y., Wada, K., Matsumoto, K., Tamaki, N., Yamamoto, K., Konishi, J., Yokoyama, A. J. Nucl. Med. (1990) [Pubmed]
  21. Specific labeling of beef heart mitochondrial ADP/ATP carrier with N-(3-iodo-4-azidophenylpropionamido)cysteinyl- 5-(2'-thiopyridyl)cysteine-coenzyme A (ACT-CoA), a newly synthesized 125I-coenzyme A derivative photolabel. Ruoho, A.E., Woldegiorgis, G., Kobayashi, C., Shrago, E. J. Biol. Chem. (1989) [Pubmed]
  22. Biological disulfides: the third messenger? Modulation of phosphofructokinase activity by thiol/disulfide exchange. Gilbert, H.F. J. Biol. Chem. (1982) [Pubmed]
  23. Chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme a homeostasis. Zhang, Y.M., Chohnan, S., Virga, K.G., Stevens, R.D., Ilkayeva, O.R., Wenner, B.R., Bain, J.R., Newgard, C.B., Lee, R.E., Rock, C.O., Jackowski, S. Chem. Biol. (2007) [Pubmed]
  24. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Ehmann, D.E., Gehring, A.M., Walsh, C.T. Biochemistry (1999) [Pubmed]
  25. Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase. Zheng, W., Scheibner, K.A., Ho, A.K., Cole, P.A. Chem. Biol. (2001) [Pubmed]
  26. Time-resolved fluorescence of intestinal and liver fatty acid binding proteins: role of fatty acyl CoA and fatty acid. Frolov, A., Schroeder, F. Biochemistry (1997) [Pubmed]
  27. Localization of a long-chain acyl-CoA hydrolase in spermatogenic cells in mice. Takagi, M., Ohtomo, T., Hiratsuka, K., Kuramochi, Y., Suga, T., Yamada, J. Arch. Biochem. Biophys. (2006) [Pubmed]
  28. A role for malonyl-CoA in glucose-stimulated insulin secretion from clonal pancreatic beta-cells. Corkey, B.E., Glennon, M.C., Chen, K.S., Deeney, J.T., Matschinsky, F.M., Prentki, M. J. Biol. Chem. (1989) [Pubmed]
  29. Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method. Ferdinandusse, S., Denis, S., van Berkel, E., Dacremont, G., Wanders, R.J. J. Lipid Res. (2000) [Pubmed]
  30. Lipid-metabolizing enzymes, CoASH and long-chain acyl-CoA in rat liver after treatment with tiadenol, nicotinic acid and niadenate. Bakke, O.M., Berge, R.K. Biochem. Pharmacol. (1982) [Pubmed]
  31. The charge heterogeneity of the mitochondrial acetyl-CoA acetyltransferase from rat liver. Huth, W. Eur. J. Biochem. (1981) [Pubmed]
  32. Hepatocytes mediate coenzyme A transfer to specific carbohydrate-derivatized surfaces. Weisz, O.A., Schnaar, R.L. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
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