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Gene Review

ECs2514  -  long-chain-fatty-acid--CoA ligase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs2514

  • From the E. coli transformant, AcsA was purified to homogeneity and characterized [1].
  • The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family [2].
  • Surprisingly, the sequence of the encoded protein was significantly more similar to that of an acyl-CoA synthetase of the distantly related bacterium, Thermus thermophilus, than to that of the membrane-bound acyl-acyl carrier protein synthetase of E. coli, an enzyme that catalyzes the same reaction from a more closely related organism [2].
  • However, the deduced amino acid sequence of ferA did show 31% identity with pimeloyl-CoA synthetase of Pseudomonas mendocina 35, which has been classified as a new superfamily of acyl-CoA synthetase (ADP forming) with succinyl-CoA synthetase (L. B. Sánchez, M. Y. Galperin, and M. Müller, J. Biol. Chem. 275:5794-5803, 2000) [3].

High impact information on ECs2514


Chemical compound and disease context of ECs2514


Biological context of ECs2514


Anatomical context of ECs2514


Associations of ECs2514 with chemical compounds

  • The activities of aldoxime dehydratase, NHase, and amidase were detected together with that of acyl-CoA synthetase under the culture conditions used [1].
  • 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 [5].
  • Affinity labeling fatty acyl-CoA synthetase with 9-p-azidophenoxy nonanoic acid and the identification of the fatty acid-binding site [14].
  • The predominant route originates with the activation of fatty acids by acyl-CoA synthetase followed by the distribution of the acyl moieties into all phospholipid classes via the sn-glycerol-3-phosphate acyltransferase reaction [15].
  • The remaining portions of octanoic acids isolated from the incubation mixtures were converted to their CoA esters by the action of acyl-CoA synthetase, and they were dehydrogenated by treatment with acyl-CoA oxidase, which had previously been shown to catalyze the anti-elimination of the pro-2R and pro-3R hydrogen atoms of acyl-CoA [16].

Analytical, diagnostic and therapeutic context of ECs2514


  1. Nitrile pathway involving acyl-CoA synthetase: overall metabolic gene organization and purification and characterization of the enzyme. Hashimoto, Y., Hosaka, H., Oinuma, K., Goda, M., Higashibata, H., Kobayashi, M. J. Biol. Chem. (2005) [Pubmed]
  2. The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family. Jiang, Y., Chan, C.H., Cronan, J.E. Biochemistry (2006) [Pubmed]
  3. Cloning and characterization of the ferulic acid catabolic genes of Sphingomonas paucimobilis SYK-6. Masai, E., Harada, K., Peng, X., Kitayama, H., Katayama, Y., Fukuda, M. Appl. Environ. Microbiol. (2002) [Pubmed]
  4. A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis. Kang, M.J., Fujino, T., Sasano, H., Minekura, H., Yabuki, N., Nagura, H., Iijima, H., Yamamoto, T.T. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. 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]
  6. Fatty acid uptake in Escherichia coli: regulation by recruitment of fatty acyl-CoA synthetase to the plasma membrane. Mangroo, D., Gerber, G.E. Biochem. Cell Biol. (1993) [Pubmed]
  7. Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. Black, P.N., DiRusso, C.C., Metzger, A.K., Heimert, T.L. J. Biol. Chem. (1992) [Pubmed]
  8. Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. Black, P.N., Zhang, Q., Weimar, J.D., DiRusso, C.C. J. Biol. Chem. (1997) [Pubmed]
  9. Use of Escherichia coli strains containing fad mutations plus a triple plasmid expression system to study the import of myristate, its activation by Saccharomyces cerevisiae acyl-CoA synthetase, and its utilization by S. cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Knoll, L.J., Gordon, J.I. J. Biol. Chem. (1993) [Pubmed]
  10. Isolation and Characterization of an Alcohol Dehydrogenase Gene from the Octylphenol Polyethoxylate Degrader Pseudomonas putida S-5. Tasaki, Y., Yoshikawa, H., Tamura, H. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  11. Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation. Fulda, M., Shockey, J., Werber, M., Wolter, F.P., Heinz, E. Plant J. (2002) [Pubmed]
  12. Expression of rat liver long-chain acyl-CoA synthetase and characterization of its role in the metabolism of R-ibuprofen and other fatty acid-like xenobiotics. Bruggera, R., Reichel, C., Garcia Alia, B., Brune, K., Yamamoto, T., Tegeder, I., Geisslinger, G., Geissinger, G. Biochem. Pharmacol. (2001) [Pubmed]
  13. Role of acylCoA binding protein in acylCoA transport, metabolism and cell signaling. Knudsen, J., Jensen, M.V., Hansen, J.K., Faergeman, N.J., Neergaard, T.B., Gaigg, B. Mol. Cell. Biochem. (1999) [Pubmed]
  14. Affinity labeling fatty acyl-CoA synthetase with 9-p-azidophenoxy nonanoic acid and the identification of the fatty acid-binding site. Black, P.N., DiRusso, C.C., Sherin, D., MacColl, R., Knudsen, J., Weimar, J.D. J. Biol. Chem. (2000) [Pubmed]
  15. Pathways for the incorporation of exogenous fatty acids into phosphatidylethanolamine in Escherichia coli. Rock, C.O., Jackowski, S. J. Biol. Chem. (1985) [Pubmed]
  16. Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli. Mizugaki, M., Nishimaki, T., Shiraishi, T., Kawaguchi, A., Okuda, S., Yamanaka, H. J. Biochem. (1982) [Pubmed]
  17. Further purification, characterization and salt activation of acyl-CoA synthetase from Escherichia coli. Kameda, K., Suzuki, L.K., Imai, Y. Biochim. Biophys. Acta (1985) [Pubmed]
  18. Isolation and characterization of the multiple charge isoforms of acyl-CoA synthetase from Escherichia coli. Kameda, K., Imai, Y. Biochim. Biophys. Acta (1985) [Pubmed]
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