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
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Localization
Localization on EC 4.2.1.3 - aconitate hydratase
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additional information
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isoforms Aco1, Aco2, Aco3. Cytosolic aconitase is not converted into an iron-responsive element and does not regulate iron homeostasis
more than 90% of ACO3 activity is cytosolic. An iron-sulfur centre assembly mutant atm3-1 shows reduced cytosolic ACO activity
cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
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79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
localized both to the cytosol and mitochondria by a reverse translocation mechanism
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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analysis of mitochondrial proteome, identification of two particular N-formylkynurenine modifications of enzyme
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acclimation at 28°C results in strong decrease in enzyme mRNA and activity as well as in LON protease mRNA and activity
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mitochondrial aconitase activity represents up to 80% of the total aconitase activity in skin fibroblasts
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significant decrease in activity with age, accompanied by relatively subtle alterations in activities of other citric acid cycle enzymes. Changes contribute to a decline in overall efficiency of mitochondrial bioenegetics with age
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an age-related decrease in aconitase activity along with relatively subtle alterations in activities of other citric acid cycle enzymes may contribute to a decline in the overall efficiency of mitochondrial bioenergetics. The maximal activity of aconitase in mitochondria of 16-month-old (118 nmol aconitate/min/mg protein) and 24-month-old (108 nmol/min/mg protein) mice is consistently less than that from 6-month-old (147 aconitate/min/mg protein) mice
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particulate-bound mitochondrial enzyme, the soluble mitochondrial enzyme is released from the mitochondria by freezing and thawing
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24 h after intraperitoneal administration of endotoxin, there is a 28% reduction in mitochondrial respiration and a 24% reduction in aconitase activity. Functional activity of the electron transport chain is unaffected
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79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
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enzyme is a component of mitochondrial DNA nucleoids
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
localized both to the cytosol and mitochondria by a reverse translocation mechanism
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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subcellular localization study, overview. All mutant aconitase protein molecules are partially imported into mitochondria, then the N-terminal mitochondrial targeting sequence is cleaved off by the mitochondrial processing peptidase. After the cleavage, a subpopulation of the protein molecules moves back into the cytosol by reverse translocation. The aconitase C-terminal domain confers dual targeting
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additional information
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subcellular localization study, overview. All mutant aconitase protein molecules are partially imported into mitochondria, then the N-terminal mitochondrial targeting sequence is cleaved off by the mitochondrial processing peptidase. After the cleavage, a subpopulation of the protein molecules moves back into the cytosol by reverse translocation. The aconitase C-terminal domain confers dual targeting
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