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Gene Review

ACO2  -  aconitase 2, mitochondrial

Bos taurus

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Disease relevance of ACO2


High impact information on ACO2

  • This domain packs against the remainder of the protein to form a tunnel leading to the aconitase active site, potentially for substrate channeling [1].
  • The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex [3].
  • When (+)-erythro-2-fluorocitrate is added to aconitase, the release of fluoride is stoichiometric with total substrate added, and HPLC analysis of the products indicates the formation of oxalosuccinate, and its derivative alpha-ketoglutarate [3].
  • This enzyme is isolated largely in its active [4Fe-4S] form and has a turnover number similar to that of mitochondrial aconitase [4].
  • However, there is a second aconitase, found only in the cytosol of mammalian tissues, that might serve as an IRE-BP [4].

Biological context of ACO2

  • Somatic cell mapping of the mitochondrial aconitase gene (ACO2) to bovine chromosome 5 [5].
  • At least 23 residues from all four domains of aconitase contribute to the active site [6].
  • The crystal structures of mitochondrial aconitase with isocitrate and nitroisocitrate bound have been solved and refined to R factors of 0.179 and 0.161, respectively, for all observed data in the range 8.0-2.1 A [6].
  • The trapping of exons for bovine ACO2 and ARR1 confirms the available mapping information based on synteny and provides a physical assignment for the genes [7].
  • In spite of substantial homology between the amino acid sequences of mammalian mitochondrial aconitase and IRE-BP, the mitochondrial protein does not bind IREs [4].

Anatomical context of ACO2

  • The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase [8].
  • Properties of soluble high potential type iron-sulfur protein (HiPIP) from beef heart mitochondria were compared to those of aconitase from pig heart [8].
  • Mito-Q and MitoVit-E inhibited H(2)O(2)- and lipid peroxide-induced inactivation of complex I and aconitase, TfR overexpression, and mitochondrial uptake of (55)Fe, while restoring the mitochondrial membrane potential and proteasomal activity [9].
  • H2O2-mediated inactivation of cytosolic aconitase was responsible for activation of iron regulatory protein-1 and increased expression of TfR, resulting in an increased iron uptake into endothelial cells [10].

Associations of ACO2 with chemical compounds


Other interactions of ACO2


Analytical, diagnostic and therapeutic context of ACO2


  1. E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition. Williams, C.H., Stillman, T.J., Barynin, V.V., Sedelnikova, S.E., Tang, Y., Green, J., Guest, J.R., Artymiuk, P.J. Nat. Struct. Biol. (2002) [Pubmed]
  2. Characterization of the Fe-S cluster in aconitase using low temperature magnetic circular dichroism spectroscopy. Johnson, M.K., Thomson, A.J., Richards, A.J., Peterson, J., Robinson, A.E., Ramsay, R.R., Singer, T.P. J. Biol. Chem. (1984) [Pubmed]
  3. The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex. Lauble, H., Kennedy, M.C., Emptage, M.H., Beinert, H., Stout, C.D. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Kennedy, M.C., Mende-Mueller, L., Blondin, G.A., Beinert, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Somatic cell mapping of the mitochondrial aconitase gene (ACO2) to bovine chromosome 5. Ryan, A.M., Womack, J.E. Anim. Genet. (1994) [Pubmed]
  6. Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Lauble, H., Kennedy, M.C., Beinert, H., Stout, C.D. Biochemistry (1992) [Pubmed]
  7. Isolation of coding sequences from bovine cosmids by means of exon trapping. Comincini, S., Drisaldi, B., Ferretti, L. Mamm. Genome (1997) [Pubmed]
  8. The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase. Ruzicka, F.J., Beinert, H. J. Biol. Chem. (1978) [Pubmed]
  9. Supplementation of endothelial cells with mitochondria-targeted antioxidants inhibit peroxide-induced mitochondrial iron uptake, oxidative damage, and apoptosis. Dhanasekaran, A., Kotamraju, S., Kalivendi, S.V., Matsunaga, T., Shang, T., Keszler, A., Joseph, J., Kalyanaraman, B. J. Biol. Chem. (2004) [Pubmed]
  10. Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis. Tampo, Y., Kotamraju, S., Chitambar, C.R., Kalivendi, S.V., Keszler, A., Joseph, J., Kalyanaraman, B. Circ. Res. (2003) [Pubmed]
  11. Cysteine labeling studies of beef heart aconitase containing a 4Fe, a cubane 3Fe, or a linear 3Fe cluster. Plank, D.W., Kennedy, M.C., Beinert, H., Howard, J.B. J. Biol. Chem. (1989) [Pubmed]
  12. Identification of the reactive sulfhydryl and sequences of cysteinyl-tryptic peptides from beef heart aconitase. Plank, D.W., Howard, J.B. J. Biol. Chem. (1988) [Pubmed]
  13. Ceramide-induced intracellular oxidant formation, iron signaling, and apoptosis in endothelial cells: protective role of endogenous nitric oxide. Matsunaga, T., Kotamraju, S., Kalivendi, S.V., Dhanasekaran, A., Joseph, J., Kalyanaraman, B. J. Biol. Chem. (2004) [Pubmed]
  14. Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase. Kennedy, M.C., Kent, T.A., Emptage, M., Merkle, H., Beinert, H., Münck, E. J. Biol. Chem. (1984) [Pubmed]
  15. Crystal structures of aconitase with trans-aconitate and nitrocitrate bound. Lauble, H., Kennedy, M.C., Beinert, H., Stout, C.D. J. Mol. Biol. (1994) [Pubmed]
  16. Identification of the high-molecular-mass mitochondrial oxaloacetate keto-enol tautomerase as inactive aconitase. Belikova YuO, n.u.l.l., Kotlyar, A.B., Vinogradov, A.D. FEBS Lett. (1989) [Pubmed]
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