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Gene Review

aceA  -  isocitrate lyase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4007, JW3975, icl
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Disease relevance of aceA


High impact information on aceA


Chemical compound and disease context of aceA


Biological context of aceA

  • DNA sequence analysis of the cloned gene and N-terminal protein sequencing of the cloned and wild-type enzymes revealed an entire aceA gene which encodes a 429-amino-acid residue polypeptide whose C-terminus is histidine [1].
  • Isocitrate lyase and malate synthase were readily identified by autoradiography after the products of the operon clone were labeled by the maxicell procedure and then resolved by electrophoresis [11].
  • Moreover, the main metabolic pathways and carbon flow operating during cell biotransformation was that controlled by the ICDH/ICL ratio, which decreased from 8.0 to 2.5, and the phosphotransferase/ACS ratio, which increased from 2.1 to 5.2, after a NaCl pulse fivefold the steady-state level [12].
  • The fully sequenced open reading frame encodes 436 amino acids with a deduced M(r) of 47.5 kDa, consistent with the observed M(r) (49-67.5 kDa) of most ICL enzymes reported so far [2].
  • Downstream of aceA, a gene essential for thiamine biosynthesis was identified [13].

Anatomical context of aceA

  • The M. tuberculosis model reproduced the observation that deletion of one of the two isocitrate lyase genes has little effect on bacterial growth in macrophages, but deletion of both genes leads to the elimination of the bacilli from the lungs [14].

Associations of aceA with chemical compounds

  • Therefore it seems unlikely that the glyoxylate cycle serves primarily a gluconeogenic role in starved (detached) cotyledons, in contrast to post-germinative and senescing cotyledons where PCK, ICL and MS are coordinately synthesised [15].
  • While exogenous sucrose greatly represses expression of icl and ms genes in dark-incubated cotyledons, it has a smaller effect on the level of PCK mRNA [15].
  • Itaconate, a succinate analog which inhibited both forms of isocitrate lyase in crude extracts, did not affect the growth of Y. pestis under conditions where little isocitrate lyase activity was detected [3].
  • Only marginal similarity was observed between this open reading frame (ORF) (termed icl) and a second distinct ORF (named aceA) which exhibits a low similarity to other isocitrate lyases [16].
  • Overexpression of aceA in C. glutamicum resulted in specific activities of 0.1 and 7.4 U/mg of protein in minimal medium containing glucose and acetate, respectively [13].

Regulatory relationships of aceA

  • Transcriptional analysis revealed that aceA and aceB are expressed as a 5-kb polycistronic transcript from a promoter upstream of aceA [17].

Other interactions of aceA


Analytical, diagnostic and therapeutic context of aceA


  1. Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli. Matsuoka, M., McFadden, B.A. J. Bacteriol. (1988) [Pubmed]
  2. Cloning, heterologous expression and purification of an isocitrate lyase from Streptomyces clavuligerus NRRL 3585. Soh, B.S., Loke, P., Sim, T.S. Biochim. Biophys. Acta (2001) [Pubmed]
  3. Glyoxylate bypass enzymes in Yersinia species and multiple forms of isocitrate lyase in Yersinia pestis. Hillier, S., Charnetzky, W.T. J. Bacteriol. (1981) [Pubmed]
  4. Expression and biochemical characterisation of recombinant AceA, a bacterial alpha-mannosyltransferase. Geremia, R.A., Roux, M., Ferreiro, D.U., Dauphin-Dubois, R., Lellouch, A.C., Ielpi, L. Mol. Gen. Genet. (1999) [Pubmed]
  5. Isocitrate lyase of the facultative intracellular pathogen Rhodococcus equi. Kelly, B.G., Wall, D.M., Boland, C.A., Meijer, W.G. Microbiology (Reading, Engl.) (2002) [Pubmed]
  6. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. Smith, C.V., Huang, C.C., Miczak, A., Russell, D.G., Sacchettini, J.C., Höner zu Bentrup, K. J. Biol. Chem. (2003) [Pubmed]
  7. Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli. Robertson, E.F., Hoyt, J.C., Reeves, H.C. J. Biol. Chem. (1988) [Pubmed]
  8. Role of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli. Ogawa, T., Murakami, K., Mori, H., Ishii, N., Tomita, M., Yoshin, M. J. Bacteriol. (2007) [Pubmed]
  9. Phosphorylation of isocitrate dehydrogenase in Escherichia coli mutants with a non-functional glyoxylate cycle. Reeves, H.C., Malloy, P.J. FEBS Lett. (1983) [Pubmed]
  10. Alkylation of isocitrate lyase from Escherichia coli by 3-bromopyruvate. Ko, Y.H., McFadden, B.A. Arch. Biochem. Biophys. (1990) [Pubmed]
  11. Glyoxylate bypass operon of Escherichia coli: cloning and determination of the functional map. Chung, T., Klumpp, D.J., LaPorte, D.C. J. Bacteriol. (1988) [Pubmed]
  12. Salt stress effects on the central and carnitine metabolisms of Escherichia coli. Cánovas, M., Bernal, V., Sevilla, A., Iborra, J.L. Biotechnol. Bioeng. (2007) [Pubmed]
  13. 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]
  14. Kinetic modeling of tricarboxylic acid cycle and glyoxylate bypass in Mycobacterium tuberculosis, and its application to assessment of drug targets. Singh, V.K., Ghosh, I. Theoretical biology & medical modelling [electronic resource]. (2006) [Pubmed]
  15. Molecular cloning of cucumber phosphoenolpyruvate carboxykinase and developmental regulation of gene expression. Kim, D.J., Smith, S.M. Plant Mol. Biol. (1994) [Pubmed]
  16. 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]
  17. Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa. Rae, J.L., Cutfield, J.F., Lamont, I.L. J. Bacteriol. (1997) [Pubmed]
  18. Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase. Klumpp, D.J., Plank, D.W., Bowdin, L.J., Stueland, C.S., Chung, T., LaPorte, D.C. J. Bacteriol. (1988) [Pubmed]
  19. Elevated levels of glyoxylate shunt enzymes in Escherichia coli strains constitutive for fatty acid degradation. Maloy, S.R., Bohlander, M., Nunn, W.D. J. Bacteriol. (1980) [Pubmed]
  20. Chemostat culture characterization of Escherichia coli mutant strains metabolically engineered for aerobic succinate production: a study of the modified metabolic network based on metabolite profile, enzyme activity, and gene expression profile. Lin, H., Bennett, G.N., San, K.Y. Metab. Eng. (2005) [Pubmed]
  21. Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308. Robertson, A.G., Nimmo, H.G. Biochem. J. (1995) [Pubmed]
  22. The absence of glyoxylate cycle enzymes in rodent and embryonic chick liver. Holmes, R.P. Biochim. Biophys. Acta (1993) [Pubmed]
  23. Identification of the histidine residue in Escherichia coli isocitrate lyase that reacts with diethylpyrocarbonate. Rua, J., Robertson, A.G., Nimmo, H.G. Biochim. Biophys. Acta (1992) [Pubmed]
  24. Purification of isocitrate lyase from Escherichia coli and watermelon using fast protein liquid chromatography. Conder, M.J., Ko, Y.H., McFadden, B.A. Prep. Biochem. (1988) [Pubmed]
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