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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Subunits
Subunits on EC 4.2.1.3 - aconitate hydratase
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dimer
homodimer
monomer
additional information
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x * 87606, calculated. By IEF-PAGE, identification of 9 different forms of 91000-93000 Da
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x * 80000, recombinant enzyme, SDS-PAGE, x * 85700, sequence calculation
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Paracoccidioides brasiliensis ATCC MYA 826
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x * 80000, recombinant enzyme, SDS-PAGE, x * 85700, sequence calculation
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structural analysis by X-ray scattering and modelling of wild-type and mutant enzymes, overview
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
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
monomer
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1 * 104800, recombinant N-terminally His-tagged aconitase, sequence calculation, 1 * 102300, recombinant aconitase with an additional Gly at the C-terminus, sequence calculation
monomer
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1 * 104800, recombinant N-terminally His-tagged aconitase, sequence calculation, 1 * 102300, recombinant aconitase with an additional Gly at the C-terminus, sequence calculation
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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
additional information
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enzyme binds to the 3 untranslated region of transcriptional activator GerE mRNA in in vitro gel shift assays
additional information
Aco1 domain structure, comparison to Aco3 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco1 domain structure, comparison to Aco3 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco1 domain structure, comparison to Aco3 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco2 domain structure, comparison to Aco1 and Aco3 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco2 domain structure, comparison to Aco1 and Aco3 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco2 domain structure, comparison to Aco1 and Aco3 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco3 domain structure, comparison to Aco1 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco3 domain structure, comparison to Aco1 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
Aco3 domain structure, comparison to Aco1 and Aco2 and to enzymes from Arabidopsis thaliana, overview
additional information
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depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
additional information
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
additional information
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peptide mapping and proteomic analysis, overview
additional information
Paracoccidioides brasiliensis ATCC MYA 826
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peptide mapping and proteomic analysis, overview
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additional information
peptide mapping, mass spectrometry analysis, overview