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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General Information
General Information on EC 4.2.1.3 - aconitate hydratase
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malfunction
metabolism
physiological function
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acnA mutants grow very poorly, have secondary mutations, and are quickly outgrown by pseudorevertants. The acnA gene is stably interrupted in a citrate synthase (gltA) null background, indicating that the intracellular accumulation of citrate may be deleterious for survival. No aconitase activity is detected in this mutant. To uncover a function of AcnA beyond its catalytic role in the tricarboxylic acid cycle pathway, the citrate synthase/aconitase (acnA) double mutant is compared with the citrate synthase single mutant. No differences are found
malfunction
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acnA expression is enhanced in an acnB mutant
malfunction
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aconitase down-regulation suppresses pink1 mutant phenotypes. In contrast to partial loss of aconitase that rescues mitochondrial defects in pink1 mutants, overexpression of aconitase in transgenic mice causes mitochondrial morphological defects and swelling of mitochondria in dopaminergic neurons
malfunction
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cell wall-modifying enzyme peptidoglycan deacetylase, PgdA expression is significantly decreased in an acnB mutant. Mutant strain is more susceptible to lysozyme-mediated killing and is attenuated in its ability to colonize mice
malfunction
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in acnB mutants proliferation of pepper plants is significantly impaired. Deletion of acnB leads to reduced hypersensitive response induction in resistant pepper plants and an increased susceptibility to the superoxide generating compound menadione
malfunction
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mutant shows severe defects in morphology and physiology, as is unable to form any aerial mycelium, spores or phosphinothricin tripeptide
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ACO is an enzyme that catalyzes the isomerization of citrate to isocitrate in both the Krebs cycle and the glyoxylate cycle
metabolism
Paracoccidioides brasiliensis ATCC MYA 826
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ACO is an enzyme that catalyzes the isomerization of citrate to isocitrate in both the Krebs cycle and the glyoxylate cycle
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aconitase is destabilized in the absence of the Fe4S4 cluster. Apo-form has higher surface hydrophobicity than the holo-form. The lower ground state stability and higher solvent exposed hydrophobic surface of the apo-form makes it aggregation prone. Binding of apo-aconitase to GroEL (molecular chaperone) not only rescues it from the aggregation, but also assists in the final stage of maturation by orienting the cluster insertion site of GroEL bound apo-protein
physiological function
iron restriction suppresses mitochondrial and cytosolic aconitase activity in erythroid but not granulocytic or megakaryocytic progenitors. The mechanism for aconitase regulation of erythropoiesis most likely involves both production of metabolic intermediates as well as modulation of erythropoietin signaling
physiological function
it is investigated if oxidative inactivation of mitochondrial aconitase results in the release of redox-active iron and hydrogen peroxide and whether this contributes to cell death. Using an adenoviral construct mitochondrial aconitase is over-expressed in primary mesencephalic cultures. Oxidative inactivation of m-aconitase over-expressing cultures results in exacerbation of H2O2 production, Fe2+ accumulation and increased neuronal death. Increased cell death in m-aconitase overexpressing cultures is attenuated by addition of catalase and/or a cell permeable iron chelator suggesting that neuronal death occurred in part via astrocyte-derived H2O2
physiological function
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aconitase is a bifunctional enzyme, which can not only interconvert citrate and isocitrate, but also has the RNA binding function similar to the eukaryotic protein IRP-1, iron regulatory protein 1
physiological function
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the increase in citrate, caused by aconitase inhibition, induces amino acid synthesis and the gamma-aminobutyrate shunt, in accordance with the suggested fate of citrate during the acid decline stage in citrus fruit
physiological function
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aconitase directly regulates citrate synthase production by interacting with the citZ transcript
physiological function
a comparative proteomic approach with the wild-type and the AcnA mutant strain under oxidative stress conditions identifies up to 90 differentially expressed proteins in both strains. Some of the respective target mRNAs show the presence of iron responsive element motifs. Aconitase controls translation elongation factor Tu expression upon oxidative stress and may be directly involved in regulation upon oxidative stress
physiological function
a zinc hyper-tolerant deletion mutant, which lacks the Pif1 DNA helicase, shows increased iron accumulation, redistribution of the aconitase protein to mitochondria, and also a loss of aconitase activity, despite normal Aco1 protein levels being present. Lack of Aco1 enzymatic activity in mitochondria, citrate accumulation and lack of activity of [Fe-S] enzymes, e.g. succinate dehydrogenase, appear to be direct molecular indicators of increased zinc tolerance
physiological function
apo-AcnB is able to bind to RNA transcripts of hpn encoding a nickel-sequestering protein, ahpC encoding alkyl hydroperoxide reductase, and flgR encoding flagellum response regulator. Compared to the wild-type, the AcnB mutant strain has decreased activities of the nickel-containing enzymes urease and hydrogenase, and lower total nickel levels within the cells. Binding of apo-AcnB to the hpn 5' untranslated region may inhibit the expression of Hpn. AcnB mutant cells display oxidative-stress-sensitive phenotypes and have a lesser motility ability than the wild-type strain
physiological function
the Aco3 mutant shows delayed early seedling growth, altered assimilation of [14C]acetate feeding and elevated citrate levels, which are nearly 4fold greater than in wild-type, or isoforms Aco1 or Aco2 mutants
physiological function
the aconitase N and C-terminal domains interact and this interaction is important for efficient aconitase posttranslational import into mitochondria and for aconitase dual targeting to mitochondria and cytosol. The C-terminal domain may have a chaperone-like function towards the N-terminal domains, which can be modulated by cytosolic Hsp70 protein Ssa1/2
physiological function
the gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21. The viability defect of an Aco2 mutation is complemented not by the aconitase domain but by the bL21 domain, which enables mitochondrial translation
physiological function
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apo-AcnB is able to bind to RNA transcripts of hpn encoding a nickel-sequestering protein, ahpC encoding alkyl hydroperoxide reductase, and flgR encoding flagellum response regulator. Compared to the wild-type, the AcnB mutant strain has decreased activities of the nickel-containing enzymes urease and hydrogenase, and lower total nickel levels within the cells. Binding of apo-AcnB to the hpn 5' untranslated region may inhibit the expression of Hpn. AcnB mutant cells display oxidative-stress-sensitive phenotypes and have a lesser motility ability than the wild-type strain
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physiological function
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the gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21. The viability defect of an Aco2 mutation is complemented not by the aconitase domain but by the bL21 domain, which enables mitochondrial translation
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physiological function
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a comparative proteomic approach with the wild-type and the AcnA mutant strain under oxidative stress conditions identifies up to 90 differentially expressed proteins in both strains. Some of the respective target mRNAs show the presence of iron responsive element motifs. Aconitase controls translation elongation factor Tu expression upon oxidative stress and may be directly involved in regulation upon oxidative stress
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physiological function
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aconitase is a bifunctional enzyme, which can not only interconvert citrate and isocitrate, but also has the RNA binding function similar to the eukaryotic protein IRP-1, iron regulatory protein 1
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