The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

ACO2  -  aconitase 2, mitochondrial

Bos taurus

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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

References

  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]
 
WikiGenes - Universities