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Chemical Compound Review

CHEMBL1949896     [(2R,3S,4R,5R)-5-(6- aminopurin-9-yl)-4...

Synonyms: AC1L97OH
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Disease relevance of octanoyl-CoA


High impact information on octanoyl-CoA

  • No noticeable effect of Nagarse pretreatment was observed on the binding of octanoyl-CoA to mitochondria [3].
  • The medium-chain acyl CoA compound, octanoyl CoA, also did not affect benzo(a)pyrene hydroxylation in microsomes or liver [4].
  • Therefore, plant peroxisomes are capable of performing complete beta-oxidation of acyl-CoA chains, whereas mammalian peroxisomes can perform beta-oxidation of only those acyl-CoA chains that are larger than octanoyl-CoA (C8) [5].
  • The mode of binding of the ligand, octanoyl-CoA, shows that the omega-end of the acyl group binds in a hydrophobic tunnel formed by residues of the loop preceding helix H4 as well as by side-chains of the kinked helix H9 [6].
  • 1. The accessibility of the active site and malonyl-CoA-binding site of the enzyme from the cytosolic aspect of the membrane was investigated using preparations of octanoyl-CoA and malonyl-CoA immobilized on to agarose beads to render them impermeant through the outer membrane [7].

Biological context of octanoyl-CoA

  • The transient kinetics for the reductive half-reaction, oxidative half-reaction and the dissociation 'off-rate' (of the reaction product from the oxidized enzyme site) were all found to be affected by deletions of the 3'-phosphate group from octanoyl-CoA and butyryl-CoA substrates [8].
  • The rate of hydrolysis of octanoyl-CoA with increasing enzyme concentration appeared as a hyperbolic plot [9].
  • MLCT, compared with LCT, showed significantly lower body fat accumulation, higher 24-h energy expenditure and acyl-CoA dehydrogenase activity measured using octanoyl-CoA as a substrate, and similar lipogenic activity [10].

Anatomical context of octanoyl-CoA


Associations of octanoyl-CoA with other chemical compounds


Gene context of octanoyl-CoA

  • The recombinant wild type SCAD kcat/K(m) values for butyryl-hexanoyl-, and octanoyl-CoA were 220, 22, and 3.2 microM-1 min-1, respectively, while the Glu368Asp mutant gave kcat/K(m) of 81, 12, and 1.4 microM-1 min-1, respectively, for the same substrates [21].
  • A series of 8-alkylmercapto-FAD analogues containing increasingly bulky substituents bind tightly to apo-ETF and can be reduced to the dihydroflavin level by octanoyl-CoA in the presence of catalytic levels of the medium-chain acyl-CoA dehydrogenase [22].
  • The corresponding MCADH mutant, Thr255Glu (glu/glu-MCADH), is as active as MCADH with octanoyl-CoA; its activity/chain length profile is, however, much narrower [23].

Analytical, diagnostic and therapeutic context of octanoyl-CoA

  • Titrations of the medium-chain dehydrogenase with the 4-thia derivative resemble those obtained with octanoyl-CoA, except for the contribution of the strongly absorbing 4-thia-trans-2-octenoyl-CoA product [24].
  • In this study, capillary electrophoresis was used as an effective analytical technique to characterize rat liver peroxisomal acyl-CoA hydrolase reactivity using octanoyl-CoA as a substrate at different reaction conditions [9].


  1. Determination of selectivity and efficacy of fatty acid synthesis inhibitors. Kodali, S., Galgoci, A., Young, K., Painter, R., Silver, L.L., Herath, K.B., Singh, S.B., Cully, D., Barrett, J.F., Schmatz, D., Wang, J. J. Biol. Chem. (2005) [Pubmed]
  2. Enzymes of fatty acid beta-oxidation in developing brain. Reichmann, H., Maltese, W.A., DeVivo, D.C. J. Neurochem. (1988) [Pubmed]
  3. Malonyl-CoA binding site and the overt carnitine palmitoyltransferase activity reside on the opposite sides of the outer mitochondrial membrane. Murthy, M.S., Pande, S.V. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  4. Effect of fatty acids on formation, distribution, storage, and release of benzo(a)pyrene phenols and glucuronides in the isolated perfused rat liver. Zhong, Z., Gao, W., Kauffman, F.C., Thurman, R.G. Cancer Res. (1989) [Pubmed]
  5. A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. Hayashi, H., De Bellis, L., Ciurli, A., Kondo, M., Hayashi, M., Nishimura, M. J. Biol. Chem. (1999) [Pubmed]
  6. The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group. Partanen, S.T., Novikov, D.K., Popov, A.N., Mursula, A.M., Hiltunen, J.K., Wierenga, R.K. J. Mol. Biol. (2004) [Pubmed]
  7. Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane. Fraser, F., Corstorphine, C.G., Zammit, V.A. Biochem. J. (1997) [Pubmed]
  8. Functional role of a distal (3'-phosphate) group of CoA in the recombinant human liver medium-chain acyl-CoA dehydrogenase-catalysed reaction. Peterson, K.L., Srivastava, D.K. Biochem. J. (1997) [Pubmed]
  9. Capillary electrophoretic assay of acyl-CoA hydrolase activity. Panuganti, S.D., Moore, K.H. Journal of capillary electrophoresis. (2003) [Pubmed]
  10. Effect of randomly interesterified triacylglycerols containing medium- and long-chain fatty acids on energy expenditure and hepatic fatty acid metabolism in rats. Shinohara, H., Ogawa, A., Kasai, M., Aoyama, T. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  11. Acyl-CoA chain length affects the specificity of various carnitine palmitoyltransferases with respect to carnitine analogues. Possible application in the discrimination of different carnitine palmitoyltransferase activities. Murthy, M.S., Ramsay, R.R., Pande, S.V. Biochem. J. (1990) [Pubmed]
  12. Diagnosis of medium-chain acyl-CoA dehydrogenase deficiency in lymphocytes and liver by a gas chromatographic method: the effect of oral riboflavin supplementation. Duran, M., Cleutjens, C.B., Ketting, D., Dorland, L., de Klerk, J.B., van Sprang, F.J., Berger, R. Pediatr. Res. (1992) [Pubmed]
  13. Existence of acetyl-CoA-dependent chain elongation system in hepatic peroxisomes of rat: effects of clofibrate and di-(2-ethylhexyl)phthalate on the activity. Horie, S., Suzuki, T., Suga, T. Arch. Biochem. Biophys. (1989) [Pubmed]
  14. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. Kunau, W.H., Dommes, P. Eur. J. Biochem. (1978) [Pubmed]
  15. Medium chain acyl-CoA dehydrogenase deficiency: apparent Km and Vmax values for fibroblast acyl-CoA dehydrogenase towards octanoyl CoA in patient and control cell lines. Gregersen, N., Kølvraa, S. J. Inherit. Metab. Dis. (1984) [Pubmed]
  16. Rat liver peroxisomes catalyze the beta oxidation of fatty acids. Lazarow, P.B. J. Biol. Chem. (1978) [Pubmed]
  17. Alternate electron acceptors for medium-chain acyl-CoA dehydrogenase: use of ferricenium salts. Lehman, T.C., Thorpe, C. Biochemistry (1990) [Pubmed]
  18. Isolation and characterization of an acyl-CoA thioesterase from dark-grown Euglena gracilis. Larson, J.D., Kolattukudy, P.E. Arch. Biochem. Biophys. (1985) [Pubmed]
  19. Resonance Raman study on complexes of medium-chain acyl-CoA dehydrogenase. Nishina, Y., Sato, K., Shiga, K., Fujii, S., Kuroda, K., Miura, R. J. Biochem. (1992) [Pubmed]
  20. Protective role of adenine nucleotide translocase in O2-deficient hearts. Pande, S.V., Goswami, T., Parvin, R. Am. J. Physiol. (1984) [Pubmed]
  21. Functional role of the active site glutamate-368 in rat short chain acyl-CoA dehydrogenase. Battaile, K.P., Mohsen, A.W., Vockley, J. Biochemistry (1996) [Pubmed]
  22. Electron-transferring flavoprotein from pig kidney: flavin analogue studies. Gorelick, R.J., Thorpe, C. Biochemistry (1986) [Pubmed]
  23. Medium-long-chain chimeric human Acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain Acyl-CoA dehydrogenase. Nandy, A., Kieweg, V., Kräutle, F.G., Vock, P., Küchler, B., Bross, P., Kim, J.J., Rasched, I., Ghisla, S. Biochemistry (1996) [Pubmed]
  24. The reductive half-reaction in Acyl-CoA dehydrogenase from pig kidney: studies with thiaoctanoyl-CoA and oxaoctanoyl-CoA analogues. Lau, S.M., Brantley, R.K., Thorpe, C. Biochemistry (1988) [Pubmed]
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