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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: Escherichia coli 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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additional information
AcnB is a member of the aconitase family
aconitase
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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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(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
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(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
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(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
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r
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
cis-aconitate + H2O
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?
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
isocitrate
cis-aconitate + H2O
additional information
?
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cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
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r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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additional information
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no detectable activity with (2S,3S)-methylcitrate
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additional information
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no detectable activity with (2S,3S)-methylcitrate
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additional information
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the HEAT-like domain, implies a role in protein-protein recognition
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additional information
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the HEAT-like domain, implies a role in protein-protein recognition
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additional information
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weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle
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additional information
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the active sites within ICDH-AcnB catalyze the three consecutive reactions, in which citrate is converted to 2-oxoglutarate, via cisaconitate and isocitrate
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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additional information
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aconitase B is the major isoenzyme which is synthesized earlier in the growth cycle than aconitase A and is subject to catabolite and anaerobic repression
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additional information
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aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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additional information
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the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
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(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
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r
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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r
additional information
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cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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additional information
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the HEAT-like domain, implies a role in protein-protein recognition
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additional information
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the HEAT-like domain, implies a role in protein-protein recognition
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additional information
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weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle
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additional information
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aconitase B is the major isoenzyme which is synthesized earlier in the growth cycle than aconitase A and is subject to catabolite and anaerobic repression
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additional information
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aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator
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Fe2+
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Fe
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a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed
Fe2+
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Iron
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the active form contains a [4Fe-4S]+ cluster, the inactive form contains a [3Fe-4S]+ cluster
Iron
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a significant proportion of the enzyme is in the inactive [3Fe-4S]1+ or apoenzyme forms. AcnB contains a much higher proportion of inactive enzyme than AcnA
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0.21
(2R,3S)-2-methylisocitrate
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0.016 - 0.058
cis-aconitate
additional information
additional information
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0.016
cis-aconitate
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20°C, pH 7.4, enzyme form AcnB
0.058
cis-aconitate
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20°C, pH 7.4, enzyme form AcnA
1.16
citrate
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20°C, pH 7.4, enzyme form AcnA
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citrate
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20°C, pH 7.4, enzyme form AcnB
additional information
additional information
steady-state kinetics
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additional information
additional information
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two values are obtained for KM-value with isocitrate as substrate, depending on substrate concentration
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additional information
additional information
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additional information
additional information
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additional information
additional information
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7.5
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enzyme form AcnA and AcnB, the maximal activity of AcnB is nearly 2fold the activity of AcnA
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5 - 10
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pH 5.0: about 75% of maximal activity, pH 10.0: about 60% of maximal activity, AcnA
6 - 9
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pH 6.0: about 55% of maximal activity, pH 9.0: about 20% of maximal activity, AcnB
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SwissProt
brenda
AcnB; gene AcnB
SwissProt
brenda
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94000
x * 94000, SDS-PAGE
97500
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1 * 97500, SDS-PAGE
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homodimer
structural modeling, homo-oligomerization of AcnA yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview
monomer
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1 * 97500, SDS-PAGE
homodimer
structural analysis by X-ray scattering and modelling of wild-type and mutant enzymes, overview
homodimer
structural modeling, homo-oligomerization of AcnB yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview
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additional information
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a postranslational activation-inactivation mechanism might be operating
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2.4 A structure of AcnB, hanging drop vapor diffusion at 17°C
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additional information
construction of a fusion protein of aconitase B and isocitrate dehydrogenase, ICDH and AcnB, i.e. ICDH-AcnB, structure determination of ICDH-AcnB, overview
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fluorocitrate protects from inactivation by O2
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more than 50% of total aconitase activity is lost when cell-free extracts are prepared under air by a French press, by osmotic rupture of spheroplasts or by sonic treatment
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rapid inactivation by exposure to air
488175
fluorocitrate protects from inactivation by O2
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33804
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native and SeMet [3Fe-4S] form of AcnB expressed in Escherichia coli
recombinant enzymes from Escherichia coli strain BL21(DE3) by gel filtration
recombinant His-tagged AcnB by metal affinity chromatography
recombinant AcnB5-4 polypeptide
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recombinant His-tagged AcnA by metal affinity chromatography
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gene acnB, expression of wild-type enzyme and the fusion protein ICDH-AcnB in Escherichia coli strain BL21 (DE3)
gene ACnB, overexpression of the His-tagged protein in an ASKA library
AcnB domain 5-4 polypeptide is expressed in Escherichia coli as a GST-AcnB5-4 fusion protein
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gene AcnA, overexpression of the His-tagged protein in an ASKA library, i.e. the 'a complete set of Escherichia coli K-12 ORF archive library
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Gruer, M.J.; Bradbury, A.J.; Guest, J.R.
Construction and properties of aconitase mutants of Escherichia coli
Microbiology
143
1837-1846
1997
Escherichia coli
brenda
Hattori, Y.; Hino, S.
Inactivation by oxygen and stabilization by fluorocitrate of aconitase from Escherichia coli
J. Gen. Appl. Microbiol.
27
33-41
1981
Escherichia coli
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brenda
Bennett, B.; Gruer, M.J.; Guest, J.R.; Thomson, A.J.
Spectroscopic characterisation of an aconitase (AcnA) of Escherichia coli
Eur. J. Biochem.
233
317-326
1995
Escherichia coli
brenda
Prodromou, C.; Haynes, M.J.; Guest, J.R.
The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn)
J. Gen. Microbiol.
137
2505-2515
1991
Escherichia coli
brenda
Brock, M.; Maerker, C.; Schuetz, A.; Voelker, U.; Buckel, W.
Oxidation of propionate to pyruvate in Escherichia coli: Involvement of methylcitrate dehydratase and aconitase
Eur. J. Biochem.
269
6184-6194
2002
Escherichia coli (P36683), Escherichia coli, Escherichia coli W3350 (P36683)
brenda
Jordan, P.A.; Tang, Y.; Bradbury, A.J.; Thomson, A.J.; Guest, J.R.
Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)
Biochem. J.
344
739-746
1999
Escherichia coli, Escherichia coli JRG2387
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brenda
Williams, C.H.; Stillman, T.J.; Barynin, V.V.; Sedelnikova, S.E.; Tang, Y.; Green, J.; Guest, J.R.; Artymiuk, P.J.
E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition
Nat. Struct. Biol.
9
447-452
2002
Escherichia coli (P36683), Escherichia coli
brenda
Tang, Y.; Guest, J.R.; Artymiuk, P.J.; Green, J.
Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation
Mol. Microbiol.
56
1149-1158
2005
Escherichia coli
brenda
Tsuchiya, D.; Shimizu, N.; Tomita, M.
Cooperativity of two active sites in bacterial homodimeric aconitases
Biochem. Biophys. Res. Commun.
379
485-488
2009
Escherichia coli (P25516), Escherichia coli (P36683), Escherichia coli
brenda
Tsuchiya, D.; Shimizu, N.; Tomita, M.
Versatile architecture of a bacterial aconitase B and its catalytic performance in the sequential reaction coupled with isocitrate dehydrogenase
Biochim. Biophys. Acta
1784
1847-1856
2008
Escherichia coli (P36683)
brenda