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
4.2.1.3 aconitate hydrataseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 4.2.1.3 - aconitate hydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
deferiprone
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the loss of aconitase activity observed in cells should be ascribed to the chelation of available iron rather than to a direct effect of the chelator on the iron-sulfur clusters of the enzyme
ethyl picolinate
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isoenzyme is inhibited, isoenzyme I is less or not sensitive
HOCl
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exposure of human coronary artery endothelial cells to 0-50 microM HOCl or 0-150 microM HOSCN results in an increase in intracellular iron, loss of aconitase activity and a loss of mitochondrial aconitase protein. Cytosolic aconitase is not affected
HOSCN
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exposure of human coronary artery endothelial cells to 0-50 microM HOCl or 0-150 microM HOSCN results in an increase in intracellular iron, loss of aconitase activity and a loss of mitochondrial aconitase protein. Cytosolic aconitase is not affected. HOSCN induces rapid and efficient release of iron from aconitase. Blocking the [4Fe-4 S] cluster inhibits HOSCN-mediated inactivation
indomethacin
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a non-steroidal anti-inflammatory drug, carbonylation of aconitase and release of iron along with the loss of activity in vivo after indomethacin treatment, activation of mitochondrial death pathway by indomethacin, overview
Mn2+
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inhibition of enzyme, resulting in up to 90% increase in intracellular citrate. Mitochondrial isoform is significantly more sensitive to Mn2+ than cytosolic isoform. Inhibition leads to conversion of enzyme to iron regulatory protein IRP 1 and increases the abundance of IRP2, leading to reduced H-ferritin expression, inreased transferrin receptor expression, and increased uptake of transferrin. IRP2 has a dominant role in Mn2+-induced alteration of iron homeostasis over aconitase/IRP1
nitric oxide
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brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed
nitrite
inactivation rate constant is 0.0078/min, which is 1.6- and 7.8fold lower than those for AcnA4 and AcnB, respectively. When exposed to NO2-, the acnA3 mutant accumulates higher levels of cellular citrate compared with the other aconitase mutants
nitrosoglutathione
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irreversible inactivation both in presence and absence of substrate
oxalomalic acid
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inhibition of aconitase activity, leading to inhibition of L-glutamate production, L-cystine uptake, and decrease in glutathione concentration in lens epithelial cells and retinal pigment epithelial cells
oxygen
atmospheric oxygen inactivates isoform AcnA3 at a rate of 0.0016/min, which is 2.7- and 37fold lower compared with isoforms AcnA4 and AcnB, respectively
S(1,1,2,2)-tetrafluoroethyl-L-cysteine
inhibition of renal aconitase activity both in vivo and in vitro is a functional consequence of difluorothioamidyl-L-lysine formation by S(1,1,2,2)-tetrafluoroethyl-L-cysteine
Cd2+
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exposure of isolated mitochondria to 0.05 mM Cd2+ results in 20-25% inhibition of mitochondrial aconitase activity. Exposure of whole oysters to Cd2+ for 3-6 weeks has no effect on aconitase activity
citramalate
a competitive inhibitor of aconitase activity; a competitive inhibitor of aconitase activity; a competitive inhibitor of aconitase activity
citramalate
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an endogenous compound of fruit pulp, is a competitive endogenous inhibitor of citrus aconitase, it significantly increases citrate content and reduces the mitochondrial isozyme activity, while slightly inducing its protein level
citrate
citrate accumulation under enzyme inhibition restricts the formation of hydroxyl radical in the Fenton reaction through the binding of iron ions, and it thus protects the enzyme from inactivation
citrate
citrate accumulation under enzyme inhibition restricts the formation of hydroxyl radical in the Fenton reaction through the binding of iron ions, and it thus protects the enzyme from inactivation
citrate
citrate accumulation under enzyme inhibition restricts the formation of hydroxyl radical in the Fenton reaction through the binding of iron ions, and it thus protects the enzyme from inactivation
Fluorocitrate
active site aconitase inhibitor blocks erythroid differentiation in a manner similar to iron deprivation; active site aconitase inhibitor blocks erythroid differentiation in a manner similar to iron deprivation
H2O2
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H2O2 does not exert its inhibitory effects by acting directly on the enzyme, rather inactivation appears to result from interactions between aconitase and a mitochondrial membrane component responsive to H2O2. Prolonged exposure of mitochondria to steady-state levels of H2O2 or O2- results in disassembly of the [4Fe-4S]2+ cluster, carbonylation, and protein degradation
Oxalomalate
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significantly increases citrate content and reduces the enzyme's activity, while slightly inducing its protein level. Specific activities of amino acid-metabolizing enzymes are induced in oxalomalate-treated callus cells, overview
Oxalomalate
inhibition of the enzyme by oxalomalate reduces glutamate secretion and eliminates the effect of iron ions on the latter
peroxynitrite
inactivation due to the release of iron from the Fe-S cluster, other nitric oxide sources decrease the activity of the mitochondrial isozyme
peroxynitrite
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i.e. ONOO-. 0.03-3 mM L-Cys, 0.03-3 mM glutathione, or 0.1-3 mM N-(2-mercaptopropionyl)glycine protects. 1 mM FeSO4 markedly enhances the protection provided by L-Cys, but not by glutathione or N-(2-mercaptopropionyl)glycine
peroxynitrite
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reacts with [4Fe-4S] cluster yielding an inactive [3Fe-4S] enzyme. Carbon dioxide enhances the reaction. Peroxynitrite also induces aconitase tyrosine nitration, without contributing to inactivation
trans-aconitate
a competitive inhibitor of the enzyme with respect to cis-aconitate and a non-competitive inhibitor with respect to citrate and isocitrate
Zn2+
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competitive, the inhibitory effect is specific for the citrate to cis-aconitate reaction; inhibition of mitochondrial isoenzyme; no inhibition of the cytopsolic isoenzyme
additional information
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superoxide inactivates the mRNA-binding activity through direct chemical attack, enzyme competitive inhibition by di- and tricarboxylic acids and inactivation due to modification of cysteine and tyrosine residues, e.g. S-glutathionylation
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additional information
superoxide inactivates the mRNA-binding activity through direct chemical attack, enzyme competitive inhibition by di- and tricarboxylic acids and inactivation due to modification of cysteine and tyrosine residues, e.g. S-glutathionylation
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additional information
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superexpression of mitochondrial ferritin in mouse cells leads to iron deficiency in the cytosol, decrease in the level of cytosolic ferritin, and inhibition of cAH and mAH isozyme activities. Enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues
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additional information
superexpression of mitochondrial ferritin in mouse cells leads to iron deficiency in the cytosol, decrease in the level of cytosolic ferritin, and inhibition of cAH and mAH isozyme activities. Enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues
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additional information
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enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues; enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues
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additional information
enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues; enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues
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