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Gene Review

ECs1469  -  3-oxoacyl-ACP synthase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs1469


High impact information on ECs1469

  • The mutant strain carries an in-frame deletion of the KAS III active site region and was isolated by gene replacement using a medium supplemented with a source of saturated and unsaturated long-chain fatty acids [1].
  • Based on the amino acid sequence of tryptic digests of purified spinach KAS III, degenerate polymerase chain reaction (PCR) primers were designed and used to amplify a 612-bp fragment from first-strand cDNA of spinach leaf RNA [2].
  • Working with KAS IIIs from Cuphea seeds we obtained kinetic evidence that KAS III catalysis follows a Ping-Pong mechanism and that these enzymes have substrate-binding sites for acetyl-CoA and malonyl-ACP [3].
  • Incubations with chloroplasts and direct assay of the individual condensing enzymes showed that all three compounds inhibited the pea FAS condensing enzymes in the order KAS II > KAS I > KAS III [4].
  • Finally, alanine scanning revealed the involvement of Arg(150) and Arg(306) in KAS III catalysis [3].

Chemical compound and disease context of ECs1469


Biological context of ECs1469


Anatomical context of ECs1469

  • Bacterial KAS III was expressed in a seed- and developmentally specific manner in B. napus in either cytoplasm or plastid [6].

Associations of ECs1469 with chemical compounds

  • Its enzymological characteristics were similar to those of two other plant KAS III enzymes except for its inhibition by thiolactomycin [9].

Analytical, diagnostic and therapeutic context of ECs1469


  1. Beta-ketoacyl-acyl carrier protein synthase III (FabH) is essential for bacterial fatty acid synthesis. Lai, C.Y., Cronan, J.E. J. Biol. Chem. (2003) [Pubmed]
  2. 3-Ketoacyl-acyl carrier protein synthase III from spinach (Spinacia oleracea) is not similar to other condensing enzymes of fatty acid synthase. Tai, H., Jaworski, J.G. Plant Physiol. (1993) [Pubmed]
  3. Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme. Abbadi, A., Brummel, M., Schütt, B.S., Slabaugh, M.B., Schuch, R., Spener, F. Biochem. J. (2000) [Pubmed]
  4. Novel inhibitors of the condensing enzymes of the type II fatty acid synthase of pea (Pisum sativum). Jones, A.L., Herbert, D., Rutter, A.J., Dancer, J.E., Harwood, J.L. Biochem. J. (2000) [Pubmed]
  5. Molecular cloning and functional expression of Perilla frutescens 3-ketoacyl-(acyl carrier protein) synthase III. Hwang, S.K., Hwang, Y.S. Mol. Cells (2000) [Pubmed]
  6. Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase III. Verwoert, I.I., van der Linden, K.H., Walsh, M.C., Nijkamp, H.J., Stuitje, A.R. Plant Mol. Biol. (1995) [Pubmed]
  7. Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Qiu, X., Choudhry, A.E., Janson, C.A., Grooms, M., Daines, R.A., Lonsdale, J.T., Khandekar, S.S. Protein Sci. (2005) [Pubmed]
  8. Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Olsen, J.G., Kadziola, A., von Wettstein-Knowles, P., Siggaard-Andersen, M., Larsen, S. Structure (Camb.) (2001) [Pubmed]
  9. Beta-ketoacyl-acyl carrier protein synthase III from pea (Pisum sativum L.): properties, inhibition by a novel thiolactomycin analogue and isolation of a cDNA clone encoding the enzyme. Jones, A.L., Gane, A.M., Herbert, D., Willey, D.L., Rutter, A.J., Kille, P., Dancer, J.E., Harwood, J.L. Planta (2003) [Pubmed]
  10. Expression, purification, and crystallization of the Escherichia coli selenomethionyl beta-ketoacyl-acyl carrier protein synthase III. Khandekar, S.S., Konstantinidis, A.K., Silverman, C., Janson, C.A., McNulty, D.E., Nwagwu, S., Van Aller, G.S., Doyle, M.L., Kane, J.F., Qiu, X., Lonsdale, J. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  11. Crystallization of Escherichia coli beta-ketoacyl-ACP synthase III and the use of a dry flash-cooling technique for data collection. Janson, C.A., Konstantinidis, A.K., Lonsdale, J.T., Qiu, X. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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