4.2.1.3: aconitate hydratase
This is an abbreviated version!
For detailed information about aconitate hydratase, go to the full flat file.
Word Map on EC 4.2.1.3
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4.2.1.3
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iron-sulfur
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transferrin
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tricarboxylic
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dismutase
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fe-s
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succinate
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tca
-
malate
-
citric
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cardiac
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rna-binding
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neurodegenerative
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frataxin
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krebs
-
fumarase
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friedreich
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heme
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ataxia
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parkinson
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overload
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iron-dependent
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alpha-ketoglutarate
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stem-loops
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fluorocitrate
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bioenergetics
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ferroportin
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county
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hepcidin
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peroxynitrite
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mnsod
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fluoroacetate
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georgia
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cluster-containing
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iron-deficient
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iscu
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iron-replete
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iron-induced
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iron-mediated
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alabama
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kennedy
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itaconic
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ferrochelatase
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cubane
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desulfurase
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nadp-isocitrate
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rna-protein
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iron-related
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soxrs
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l-ferritin
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isopropylmalate
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medicine
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environmental protection
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synthesis
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biotechnology
- 4.2.1.3
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iron-sulfur
- transferrin
-
tricarboxylic
- dismutase
- fe-s
- succinate
- tca
- malate
-
citric
- cardiac
-
rna-binding
- neurodegenerative
- frataxin
-
krebs
- fumarase
- friedreich
- heme
- ataxia
- parkinson
- overload
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iron-dependent
- alpha-ketoglutarate
-
stem-loops
- fluorocitrate
-
bioenergetics
-
ferroportin
-
county
- hepcidin
- peroxynitrite
- mnsod
- fluoroacetate
-
georgia
-
cluster-containing
-
iron-deficient
- iscu
-
iron-replete
-
iron-induced
-
iron-mediated
- alabama
-
kennedy
-
itaconic
-
ferrochelatase
- cubane
-
desulfurase
-
nadp-isocitrate
-
rna-protein
-
iron-related
-
soxrs
- l-ferritin
- isopropylmalate
- medicine
- environmental protection
- synthesis
- biotechnology
Reaction
Synonyms
Acn, AcnA, AcnA3, AcnB, ACO, Aco1, Aco2, Aco3, ACO4, acon, aconitase, aconitase 2, aconitase A, aconitase B, aconitase/2-methylaconitate hydratase, Aconitate hydratase, AH, c-acon, c-aconitase, CAA, cis-aconitase, citB, citrate hydro-lyase, cytoplasmic aconitase, cytoplasmic aconitase/iron regulatory protein 1 homolog, EC 4.2.1.4, Ferritin repressor protein, hydratase, aconitate, IP210, IRE-BP, Iron regulatory protein, iron regulatory protein 1, iron regulatory-like protein, iron-regulatory protein 1, iron-responsive element binding protein, IRP, IRP-1, IRP1, mACON, Major iron-containing protein, MICP, More, PfIRPa, SPBP4H10.15
ECTree
4.2.1.3 aconitate hydrataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.2.1.3 - aconitate hydratase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
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-
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r
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
?
(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
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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-
-
-
?
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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-
-
-
?
isocitrate
cis-aconitate + H2O
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-
-
-
?
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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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)-methylcitrate
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?
additional information
?
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C1 aconitase is constitutive of the glyoxylate cycle. In addition, the same isoform is found to be active during pathogenic attack as well, hypocotyls. It might by assumed that in such a case the glyoxylate cycle is reinitiated as a part of a carbon reallocation system feeding on the diseased tissue cellular components
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?
additional information
?
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using electrophoretic mobility shift assays and RNA footprinting it is shown that apo-AcnB binds to the 3'-untranslated region of the pgdA RNA transcript
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?
additional information
?
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2fold increase in mitochondrial cis-aconitase activity in UVA-exposed cells coincides with the time of maximal heme oxygenase-1 expression. Modulation of cis-aconitase activity at the translational level by an increase of cellular iron is an important consequence of heme oxygenase-1 activation
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?
additional information
?
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IRP1 functions as a cytoplasmic aconitase. It may provide a link between citrate and iron metabolism and may be involved in oxidative stress response
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?
additional information
?
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key enzyme for citrate oxidation in the epithelial cell of the human prostate. Hemin and ferric ammonium citrate increase activity and gene expression
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?
additional information
?
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impairing aconitase activity precedes decreased cell proliferation
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?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Blocking of isozyme mAH expression and activity by 40-60% causes a decrease in ATP biosynthesis, increase in citrate secretion, and reduction of the rate of proliferation of human prostate carcinoma cells. extracellular H2O2 strongly induces IRP1 through a signal cascade, introduction of a source of iron ions enhances glutamate secretion in cultivated lens cells and neurons through an increase in cAH activity and intensification of isocitrate formation. The maximal activity requires the presence of sulfhydryl compounds in the medium
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-
?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Blocking of isozyme mAH expression and activity by 40-60% causes a decrease in ATP biosynthesis, increase in citrate secretion, and reduction of the rate of proliferation of human prostate carcinoma cells. extracellular H2O2 strongly induces IRP1 through a signal cascade, introduction of a source of iron ions enhances glutamate secretion in cultivated lens cells and neurons through an increase in cAH activity and intensification of isocitrate formation. The maximal activity requires the presence of sulfhydryl compounds in the medium
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?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. A decrease in enzyme activity is observed in some neurodegenerative diseases associated with the development of oxidative stress, in particular, Parkinsons and Alzheimers diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
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?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. A decrease in enzyme activity is observed in some neurodegenerative diseases associated with the development of oxidative stress, in particular, Parkinsons and Alzheimers diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
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?
additional information
?
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it is demonstrated that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1). The inability to produce normal levels of the mitochondrial protein frataxin causes the hereditary degenerative disorder Friedreichs Ataxia (FRDA)
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?
additional information
?
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iron regulatory protein-1 controls the expression of several mRNAs by binding to iron-responsive elements in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. Iron regulatory protein activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2
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?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
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-
?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
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?
additional information
?
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in addition to aconitase activity, enzyme binds with high specificity to iron-responsive element-like RNA sequences. Iron is required for aconitase activity, but inhibits the RNA-binding activity, the two activities are mutually exclusive
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?
additional information
?
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one or more of the aconitases may contribute to the control of the synthesis of the virulence factor exotoxin A
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?
additional information
?
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aconitase is part of a multienzyme complex of the tricarboxylic acid cycle. Individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex
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?
additional information
?
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Mn2+ exposure leads to a region-specific alteration in total aconitase: 48.5% reduction of the enzyme activity in frontal cortex, 33.7% in striatum and 20.6% in substantia nigra. This leads to the disruption of mitochondrial energy production and cellular Fe metabolism in the brain
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?
additional information
?
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the enzyme is involved in the assimilation of Fe and excess dietary Zn can result in negative interactions
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?
additional information
?
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effects of lipoic acid on intensity of free radical reactions, citrate content, and aconitate hydratase during myocardial ischemia, overview
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?
additional information
?
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regulation of mitochondrial aconitase activity by protein kinase C-dependent phosphorylation, augmented phosphorylation of mitochondrial aconitase in diabetic hearts is associated with an increase in its reverse activity, converting isocitrate to aconitate, while the rate of the forward activity is unchanged, overview
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?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
?
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
?
additional information
?
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-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. IRP2 dominates in the regulation of iron metabolism in mammals. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
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-
?
additional information
?
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role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. IRP2 dominates in the regulation of iron metabolism in mammals. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
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?
additional information
?
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IRP shows RNA-binding activity, which is affected by some hormones and growth factors, e.g. thyroid, erythropoietin, and epidermal growth factor
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?
additional information
?
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IRP shows RNA-binding activity, which is affected by some hormones and growth factors, e.g. thyroid, erythropoietin, and epidermal growth factor
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?
additional information
?
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toxic hepatitis is accompanied by inactivation of aconitate hydratase. Inhibition of the enzyme probably contributes to intracellular accumulation of citrate and inhibition of the Fenton reaction
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?
additional information
?
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in cytosol the enzyme participates in the glyoxylate shunt, in mitochondria the enzyme participates in the tricarboxylic acid cycle
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?
additional information
?
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enzyme binds to both ds- and ssDNA, with a preference for GC-containing sequences. It protects mitochondrial DNA from excessive accumulation of point mutations and ssDNA breaks and suppresses reductive recombination of mitochondrial DNA
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?
additional information
?
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inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
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?
additional information
?
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apo-AcnA is an RNA binding protein as shown in gel shift assays
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?
additional information
?
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Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
/ Tu 494
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inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
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?
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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?
additional information
?
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the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
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?
additional information
?
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the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
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?
additional information
?
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the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
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?
additional information
?
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inductively formed in presence of fluorocitrate
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?
additional information
?
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inductively formed in presence of fluoroacetate
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?
additional information
?
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inductively formed in presence of fluoroacetate
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?
additional information
?
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cytoplasmic aconitase/iron regulatory protein 1 homolog is up-regulated in the pulvinus bundle sheath cells after gravistimulation in presence of H2O2 and ascorbic acid, overview. Reactive oxygen species levels increase rapidly in gravistimulated maize pulvini
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