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IUBMB CommentsBesides 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.
Synonyms
aconitase, iron regulatory protein, irp-1, ire-bp, macon, iron regulatory protein 1, aconitate hydratase, cytoplasmic aconitase, aconitase a, c-aconitase,
more
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(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
(Z)-2-methylaconitate
2-methylisocitrate
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
2-methylisocitrate
alpha-methyl-cis-aconitate
alpha-methylisocitrate
cis-aconitate + H2O
citrate
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
isocitrate
cis-aconitate + H2O
threo-D-alpha-methylisocitrate
?
Saccharomycopsis lipolytica
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additional information
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(2R,3S)-2-methylisocitrate

(Z)-2-methyl-aconitate + H2O
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r
(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
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r
(2R,3S)-2-methylisocitrate

(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
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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

2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
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(Z)-2-methylaconitate
2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
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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
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
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r
(Z)-2-methylaconitate + H2O

2-methylisocitrate
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?
(Z)-2-methylaconitate + H2O
2-methylisocitrate
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?
alpha-methyl-cis-aconitate

alpha-methylisocitrate
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?
alpha-methyl-cis-aconitate
alpha-methylisocitrate
Saccharomycopsis lipolytica
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cis-aconitate + H2O

?
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cis-aconitate + H2O
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?
cis-aconitate + H2O

citrate
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r
cis-aconitate + H2O
citrate
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r
cis-aconitate + H2O
citrate
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?
cis-aconitate + H2O
citrate
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r
cis-aconitate + H2O
citrate
Saccharomycopsis lipolytica
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r
cis-aconitate + H2O
citrate
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r
cis-aconitate + H2O
citrate
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cis-aconitate + H2O
citrate
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r
cis-aconitate + H2O

isocitrate
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cis-aconitate + H2O
isocitrate
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r
cis-aconitate + H2O
isocitrate
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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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r
cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
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cis-aconitate + H2O
isocitrate
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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
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citrate

cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
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r
citrate
cis-aconitate + H2O
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?
citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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?
citrate
cis-aconitate + H2O
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?
citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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citrate
cis-aconitate + H2O
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r
citrate
cis-aconitate + H2O
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citrate

isocitrate
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r
citrate
isocitrate
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citrate
isocitrate
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citrate
isocitrate
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citrate
isocitrate
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citrate
isocitrate
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citrate
isocitrate
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citrate
isocitrate
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r
citrate
isocitrate
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citrate
isocitrate
Saccharomycopsis lipolytica
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citrate
isocitrate
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r
citrate
isocitrate
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r
isocitrate

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?
isocitrate

cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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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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isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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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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r
isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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r
isocitrate
cis-aconitate + H2O
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isocitrate
cis-aconitate + H2O
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isocitrate

citrate
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r
isocitrate
citrate
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isocitrate
citrate
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isocitrate
citrate
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isocitrate
citrate
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r
isocitrate
citrate
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isocitrate
citrate
Saccharomycopsis lipolytica
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isocitrate
citrate
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r
isocitrate
citrate
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r
additional information

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additionally to catalytic activity, enzyme is able to bind specifically the 5 UTP of the Arabidopsis chloroplastic CuZn superoxide dismutase 2 mRNA. Enzyme does not bind an iron responsive element of the human ferritin gene
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additional information
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bifunctional protein, showing aconitase activity in presence of iron and RNA binding activity when cells are iron-deprived
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additional information
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amino acid residues Arg741 and Gln745 play great role in the aconitase function
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additional information
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aconitase binds bound to the citrate synthase 5' leader RNA in vitro
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additional information
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amino acid residues Arg741 and Gln745 play great role in the aconitase function
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additional information
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Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
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additional information
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Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
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additional information
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iron-responsive element binding protein is required in the posttranscriptional regulation of ferritin mRNA translation and stabilization of transferrin receptor mRNA
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additional information
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Cucurbita sp.
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enzyme is involved in the glyoxylate cycle
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additional information
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isoform IRP-1A binds in vitro both Drosophila ferritin iron-responsive element and human ferritin iron-responsive element in the presence of a reducing agent
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additional information
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isoform IRP-1A binds in vitro both Drosophila ferritin iron-responsive element and human ferritin iron-responsive element in the presence of a reducing agent
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additional information
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isoform IRP-1A binds in vitro both Drosophila ferritin iron-responsive element and human ferritin iron-responsive element in the presence of a reducing agent
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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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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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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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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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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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no detectable activity with (2S,3S)-