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Chemical Compound Review

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

Synonyms:
 
 
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Disease relevance of Lauroyl-coenzyme A

 

High impact information on Lauroyl-coenzyme A

  • Laureate is converted to its CoA form in peroxisomes by the action of lauroyl-CoA synthetase [4].
  • Effects on function were measured by the extent of binding of the ligand dodecanoyl-CoA using isothermal titration calorimetry, and effects on protein stability were measured with chemical denaturation followed by intrinsic tryptophan and tyrosine fluorescence [5].
  • Binding of dodecanoyl-CoA to ACBP was studied at various temperatures and was characterized by a weak temperature dependence on delta G zero and a strong enthalpy-entropy compensation [6].
  • RESULTS: Acyl-CoA thioesterase activity was found in human fibroblasts with all saturated acyl-CoAs from C4-CoA to C18-CoA, with highest activity detected with lauroyl-CoA and myristoyl-CoA (C12-CoA and C14-CoA) [7].
  • Although [Glu304]MCADH has approximately the same rate of substrate reduction with dodecanoyl-CoA and the same V(max) as human MCADH with the best substrate for the latter, octanoyl-CoA, the K(m) in the mutant MCADH is fourfold higher, which generates a correspondingly lower catalytic efficiency [8].
 

Biological context of Lauroyl-coenzyme A

  • This treatment resulted in inductions of catalase, lauroyl-CoA oxidase (which catalyzes the first step in peroxisomal beta-oxidation) and of cytochrome P-450IVA (specialized for omega- and omega-1 hydroxylation of fatty acids) [9].
 

Anatomical context of Lauroyl-coenzyme A

 

Associations of Lauroyl-coenzyme A with other chemical compounds

  • Peroxisomes were found to contain 7% of the liver's palmitoyl-CoA synthetase activity and 6% of its lauroyl-CoA synthetase activity, but no demonstrable octanoyl-CoA synthetase activity [11].
  • The V(max)/K(m) versus chain-length profile of the mutant shows a maximum with dodecanoyl-CoA which differs markedly from that of human MCADH, which has maximal efficiency with octanoyl-CoA [8].
  • Lauric acid is the most suitable substrate for these enzymes, and the product of lauroyl CoA was identified with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) [12].

References

  1. Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. Musayev, F., Sachdeva, S., Scarsdale, J.N., Reynolds, K.A., Wright, H.T. J. Mol. Biol. (2005) [Pubmed]
  2. Perfluorooctanoate, perflourooctanesulfonate, and N-ethyl perfluorooctanesulfonamido ethanol; peroxisome proliferation and mitochondrial biogenesis. Berthiaume, J., Wallace, K.B. Toxicol. Lett. (2002) [Pubmed]
  3. Synergistic induction of acyl-CoA oxidase activity, an indicator of peroxisome proliferation, by arachidonic acid and retinoic acid in Morris hepatoma 7800C1 cells. Sohlenius, A.K., Wigren, J., Bäckström, K., Andersson, K., DePierre, J.W. Biochim. Biophys. Acta (1995) [Pubmed]
  4. Peroxisomal membrane protein Pmp47 is essential in the metabolism of middle-chain fatty acid in yeast peroxisomes and Is associated with peroxisome proliferation. Nakagawa, T., Imanaka, T., Morita, M., Ishiguro, K., Yurimoto, H., Yamashita, A., Kato, N., Sakai, Y. J. Biol. Chem. (2000) [Pubmed]
  5. Conserved residues and their role in the structure, function, and stability of acyl-coenzyme A binding protein. Kragelund, B.B., Poulsen, K., Andersen, K.V., Baldursson, T., Krøll, J.B., Neergård, T.B., Jepsen, J., Roepstorff, P., Kristiansen, K., Poulsen, F.M., Knudsen, J. Biochemistry (1999) [Pubmed]
  6. Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry. Faergeman, N.J., Sigurskjold, B.W., Kragelund, B.B., Andersen, K.V., Knudsen, J. Biochemistry (1996) [Pubmed]
  7. Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts. Hunt, M.C., Ruiter, J., Mooyer, P., van Roermond, C.W., Ofman, R., Ijlst, L., Wanders, R.J. Eur. J. Clin. Invest. (2005) [Pubmed]
  8. Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme. Kieweg, V., Kräutle, F.G., Nandy, A., Engst, S., Vock, P., Abdel-Ghany, A.G., Bross, P., Gregersen, N., Rasched, I., Strauss, A., Ghisla, S. Eur. J. Biochem. (1997) [Pubmed]
  9. Effects of perfluorooctanoic acid--a potent peroxisome proliferator in rat--on Morris hepatoma 7800C1 cells, a rat cell line. Sohlenius, A.K., Andersson, K., Bergstrand, A., Spydevold, O., De Pierre, J.W. Biochim. Biophys. Acta (1994) [Pubmed]
  10. Peroxisomal and mitochondrial beta-oxidation of monocarboxylyl-CoA, omega-hydroxymonocarboxylyl-CoA and dicarboxylyl-CoA esters in tissues from untreated and clofibrate-treated rats. Vamecq, J., Draye, J.P. J. Biochem. (1989) [Pubmed]
  11. Acyl-CoA synthetase in rat liver peroxisomes. Computer-assisted analysis of cell fractionation experiments. Krisans, S.K., Mortensen, R.M., Lazarow, P.B. J. Biol. Chem. (1980) [Pubmed]
  12. Enzymatic and genetic characterization of firefly luciferase and Drosophila CG6178 as a fatty acyl-CoA synthetase. Oba, Y., Sato, M., Ojika, M., Inouye, S. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
 
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