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EC Tree
IUBMB Comments Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
The taxonomic range for the selected organisms is: Sus scrofa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aconitase, iron regulatory protein, irp-1, ire-bp, macon, iron regulatory protein 1, aconitate hydratase, cytoplasmic aconitase, aconitase a, c-aconitase,
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Aconitate hydratase
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citrate hydro-lyase
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Ferritin repressor protein
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hydratase, aconitate
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Iron regulatory protein
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iron-responsive element binding protein
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Major iron-containing protein
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citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
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cis-aconitate + H2O
citrate
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r
cis-aconitate + H2O
isocitrate
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r
citrate
cis-aconitate + H2O
citrate
isocitrate
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r
isocitrate
cis-aconitate + H2O
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isocitrate
citrate
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r
additional information
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the mechanism requires that the intermediate product cis-aconitate, flip over by 180° about the Calpha-Cbeta double bond
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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r
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Iron
in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms
Iron
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Cys358, Cys421 and Cys424 are ligands to the Fe-S cluster in the inactive [3Fe-4S] form and the active [4Fe-4S] form
Iron
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crystallographic evidence for a three-iron center
Iron
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contains 2 gatoms of non-heme iron per mol of enzyme
Iron
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iron-sulfur enzyme
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1,2,3,4-tetracarboxycyclopentane
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competitive
1,2,3-tricarboxycyclopentene-1
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competitive
1,3,5-tricarboxypentane
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competitive
4-hydroxy-2-oxoglutarate
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competitive
Fluorocitrate
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linear competitive
nitric oxide
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brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed
nitrosoglutathione
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irreversible inactivation both in presence and absence of substrate
oxaloacetate
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parabolic noncompetitive
Oxalomalate
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competitive
p-hydroxymercuribenzoate
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peroxynitrite
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reacts with [4Fe-4S] cluster yielding an inactive [3Fe-4S] enzyme. Carbon dioxide enhances the reaction. Peroxynitrite also induces aconitase tyrosine nitration, without contributing to inactivation
Phthalic acid
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competitive
pyromellitic acid
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competitive
trans-aconitate
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linear competitive
trimellitic acid
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competitive
trimesic acid
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competitive
Zn2+
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inhibition of mitochondrial isoenzyme
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additional information
additional information
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additional information
additional information
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0.035
nitric oxide
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reversible inhibition after brief exposure
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additional information
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7.5
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glycerophosphate buffer
8.1
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N-ethylmorpholine buffer
8.6
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veronal acetate buffer
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Uniprot
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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ACON_PIG
781
0
85761
Swiss-Prot
Mitochondrion (Reliability: 2 )
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79000
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ultracentrifugation
82754
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x * 82754, calculation from nucleotide sequence
89000
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equilibrium sedimentation
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x * 82754, calculation from nucleotide sequence
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proteolytic modification
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the porcine heart enzyme is synthesized as a precursor containing a mitochondrial targeting sequence of 27 amino acid residues which is cleaved to yield a mature enzyme of 754 amino acids
side-chain modification
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traces of carbohydrate of less than 1%
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1.8 A resolution crystal structure of the S642A:citrate complex of mitochondrial aconitase
computational modeling of aconitase inactivation by superoxide and nitric oxide
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crystallographic evidence for a three-iron center
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-20°C, enzyme frozen after dialysis against 0.05 M Tris-HCl, pH 7.5, complete inactivation after 10 days
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expression in Escherichia coli
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Pickworth Glusker, J.
Aconitase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
413-439
1971
Aspergillus niger, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Glycine max, Rattus norvegicus, Rheum sp., Salmonella enterica subsp. enterica serovar Typhimurium, Sinapis alba, Solanum tuberosum, Sus scrofa
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brenda
Scholze, H.
Studies on aconitase species from Saccharomyces cerevisiae, porcine and bovine heart, obtained by a modified isolation method
Biochim. Biophys. Acta
746
133-137
1983
Bos taurus, Saccharomyces cerevisiae, Sus scrofa
brenda
Gawron, O.; Kennedy, M.C.; Rauner, R.A.
Properties of pig heart aconitase
Biochem. J.
143
717-722
1974
Yarrowia lipolytica, Sus scrofa
brenda
Robbins, A.H.; Stout, C.D.
Iron-sulfur cluster in aconitase. Crystallographic evidence for a three-iron center
J. Biol. Chem.
260
2328-2333
1985
Sus scrofa
brenda
Robbins, A.H.; Stout, C.D.; Piszkiewicz, D.; Gawron, O.; Yoo, C.S.; Wang, B.C.; Sax, M.
Single crystals of the iron-sulfur enzyme aconitase
J. Biol. Chem.
257
9061-9063
1982
Sus scrofa
brenda
Lee, J.; Chang, S.C.; Hahm, K.; Glaid, A.J.; Gawron, O.; Wang, B.C.; Yoo, C.S.; Sax, M.
Crystals of pig heart aconitase
J. Mol. Biol.
112
531-534
1977
Sus scrofa
brenda
Kennedy, S.C.; Rauner, R.; Gawron, O.
On pig heart aconitase
Biochem. Biophys. Res. Commun.
47
740-745
1972
Sus scrofa
brenda
Costello, L.C.; Liu, Y.; Franklin, R.B.; Kennedy, M.C.
Zinc inhibition of mitochondrial aconitase and its importance in citrate metabolism of prostate epithelial cells
J. Biol. Chem.
272
28875-28881
1997
Bos taurus, Rattus norvegicus, Sus scrofa
brenda
Zheng, L.; Andrews, P.C.; Hermodson, M.A.; Dixon, J.E.; Zalkin, H.
Cloning and structural characterization of porcine heart aconitase
J. Biol. Chem.
265
2814-2821
1990
Sus scrofa
brenda
Baldwin, G.S.; Seet, K.L.; Callaghan, J.; Toncich, G.; Toh, B.H.; Moritz, R.L.; Rubira, M.R.; Simpson, R.
Purification and partial amino acid sequence of human aconitase
Protein Seq. Data Anal.
4
63-67
1991
Homo sapiens, Sus scrofa
brenda
Lloyd, S.J.; Lauble, H.; Prasad, G.S.; Stout, C.D.
The mechanism of aconitase:1.8 A resolution crystal structure of the S642A:citrate complex
Protein Sci.
8
2655-2662
1999
Sus scrofa (P16276)
brenda
Tortora, V.; Quijano, C.; Freeman, B.; Radi, R.; Castro, L.
Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation
Free Radic. Biol. Med.
42
1075-1088
2007
Sus scrofa
brenda