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
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malate
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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
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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
-
iron-sulfur
- transferrin
-
tricarboxylic
- dismutase
- fe-s
- succinate
- tca
- malate
-
citric
- cardiac
-
rna-binding
- neurodegenerative
- frataxin
-
krebs
- fumarase
- friedreich
- heme
- ataxia
- parkinson
- overload
-
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
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Metals Ions
Metals Ions on EC 4.2.1.3 - aconitate hydratase
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Fe
Fe2+
Iron
Mg2+
Zn
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an X-ray fluorescence measurement performed on a gold-derivative crystal shows the unexpected presence of zinc, in addition to gold and iron
[4Fe-4S] center
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acon harbors a single unligated iron atom in its [4Fe-4S], enzyme is in this respect unique in mitochondria
additional information
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a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed
Fe
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Fe2+
required, both isoenzymes have an [4Fe-4S] iron-sulfur cluster bound with cysteine residues Cys437, Cys503, and Cys506, under the action of reductants, the active enzyme form is produced with a complex cation of the [3Fe3S]2+ type, structure, and mechanism of activation of the enzyme by Fe2+, overview
Fe2+
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required, the enzyme contains iron-sulfur clusters. Chelating mitochondrial free iron in various cell systems causes loss of aconitase activity
Fe2+
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
Fe2+
required, binding structure in the [Fe-S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Fe2+
required, binding structure in the [4Fe-4S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Fe2+
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enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
Fe2+
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activates the enzyme under normal conditions and in animals with toxic hepatitis. The stimulatory effect of Fe2+ in concentrations below 1 mM is less pronounced than in animals with toxic hepatitis
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[4Fe-4S] cluster. The [4Fe-4S] cluster loaded form of the IscU [Fe-S] cluser scaffolding protein can be used for intact cluster transfer to an apo form of aconitase A. IscU mutant D39A is an effective inhibitor of IscU-directed activation of apo-aconitase A
Iron
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cytosolic and mitochondrial isoenzyme require an intact [4Fe-4S] cluster. Mitochondrial aconitase is isolated predominantly in the [3Fe-4S] form (Fe/S ratio of 0.73) and must be activated by the addition of Fe2+. The cytoplasmic aconitase as isolated is about 80% active with a Fe/S ratio of 1.1
Iron
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inactive aconitase contains an oxidized [3Fe-4S]+cluster. Full activity is achieved with one electron per 3Fe cluster and at least 0.6 gatoms of Fe2+ per mol. The process involves building up of [4Fe-4S]2+ clusters
Iron
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iron-induced increase in L-glutamate availability increases via the aconitase pathway L-cystine uptake, with subsequent increases in glutathione levels
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
Iron
under iron-replete conditions, enzyme binds a [4Fe-4S] cluster und functions as cytosolic aconitase. Under iron shortage, enzyme is involved in translational control as an iron regulatory protein
Iron
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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
Iron
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iron is required for aconitase activity, but inhibits the RNA-binding activity, the two activities are mutually exclusive
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
in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+