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Gene Review

ECs4933  -  isocitrate lyase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs4933


High impact information on ECs4933

  • Highly differential labeling of serine residues 319 and 321 in the absence of substrates suggests their importance in the action of isocitrate lyase [1].
  • The role of isocitrate lyase (ICL) in the glyoxylate cycle and its necessity for persistence and virulence of Mycobacterium tuberculosis has been well described [2].
  • Furthermore, we present evidence that in both M. avium and M. tuberculosis the production and activity of the isocitrate lyase is enhanced under minimal growth conditions when supplemented with acetate or palmitate [4].
  • Its physiological role in S. cerevisiae is probably to transport cytoplasmic succinate, derived from isocitrate by the action of isocitrate lyase in the cytosol, into the mitochondrial matrix in exchange for fumarate [5].
  • In crude extracts of C. glutamicum, the specific activities of isocitrate lyase were found to be 0.01 U/mg of protein after growth on glucose and 2.8 U/mg of protein after growth on acetate, indicating tight regulation [3].

Chemical compound and disease context of ECs4933


Biological context of ECs4933


Associations of ECs4933 with chemical compounds

  • Isocitrate lyase is a key enzyme in the glyoxylate cycle and is essential as an anapleurotic enzyme for growth on acetate and certain fatty acids as carbon source [4].
  • The results showed that during batch fermentation isocitrate lyase activity and isocitrate concentration were higher in BL21 than in JM109, while pyruvate concentration was higher in JM109 [11].
  • The interaction of 3-phosphoglycerate and other substrate analogs with the glyoxylate- and succinate-binding sites of isocitrate lyase [6].


  1. Vanadate-dependent photomodification of serine 319 and 321 in the active site of isocitrate lyase from Escherichia coli. Ko, Y.H., Cremo, C.R., McFadden, B.A. J. Biol. Chem. (1992) [Pubmed]
  2. Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis. Gould, T.A., van de Langemheen, H., Muñoz-Elías, E.J., McKinney, J.D., Sacchettini, J.C. Mol. Microbiol. (2006) [Pubmed]
  3. Characterization of the isocitrate lyase gene from Corynebacterium glutamicum and biochemical analysis of the enzyme. Reinscheid, D.J., Eikmanns, B.J., Sahm, H. J. Bacteriol. (1994) [Pubmed]
  4. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. Höner Zu Bentrup, K., Miczak, A., Swenson, D.L., Russell, D.G. J. Bacteriol. (1999) [Pubmed]
  5. Identification of the yeast ACR1 gene product as a succinate-fumarate transporter essential for growth on ethanol or acetate. Palmieri, L., Lasorsa, F.M., De Palma, A., Palmieri, F., Runswick, M.J., Walker, J.E. FEBS Lett. (1997) [Pubmed]
  6. The interaction of 3-phosphoglycerate and other substrate analogs with the glyoxylate- and succinate-binding sites of isocitrate lyase. Ko, Y.H., Vanni, P., McFadden, B.A. Arch. Biochem. Biophys. (1989) [Pubmed]
  7. In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. Hoyt, J.C., Reeves, H.C. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  8. The upstream region of the isocitrate lyase gene (UPR-ICL) of Candida tropicalis induces gene expression in both Saccharomyces cerevisiae and Escherichia coli by acetate via two distinct promoters. Atomi, H., Umemura, K., Higashijima, T., Kanai, T., Yotsumoto, Y., Teranishi, Y., Ueda, M., Tanaka, A. Arch. Microbiol. (1995) [Pubmed]
  9. Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+). Simanshu, D.K., Satheshkumar, P.S., Savithri, H.S., Murthy, M.R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  10. Link between primary and secondary metabolism in the biotransformation of trimethylammonium compounds by escherichia coli. Cánovas, M., Bernal, V., Torroglosa, T., Ramirez, J.L., Iborra, J.L. Biotechnol. Bioeng. (2003) [Pubmed]
  11. Proposed mechanism of acetate accumulation in two recombinant Escherichia coli strains during high density fermentation. van de Walle, M., Shiloach, J. Biotechnol. Bioeng. (1998) [Pubmed]
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