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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Source Tissue
Source Tissue on EC 4.2.1.3 - aconitate hydratase
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activity is significantly higher in bone marrow of rats treated with N-nitro-L-arginine methylester
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repeated contractions increase aconitase activity by 50%. Increase is not accompanied by increase in aconitase protein, but is markedly inhibited by cyclosporin A
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undifferentiated neonatal cardiomyocyte. In heat-shocked cells aconitase activity is reduced
mitochondrial aconitase is over-expressed in primary mesencephalic cultures
purified human CD34+ progenitors derived from granulocyte-colony stimulating factor mobilized peripheral blood cells of normal donors
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highest activity of both forms of aconitase on the 4th day of germination, then the activity and expression of the cytosolic form sharply decreases, while those of the mitochondrial form decrease more slowly
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muscle exercise does not affect aconitase activity despite increased oxidative stress
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activity is significantly higher in spleen of rats treated with N-nitro-L-arginine methylester
additional information
inactive isozyme mAH multimers occur in rat brain in a model of Huntingtons disease
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aconitase-specific activity increases by 42% at 2% O2 compared to 21% O2
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two prominent maxima of enzyme activity are measured: the first maximum is found at an early stage of growth, the second lower maximum is detected at the beginning of the expression of the phosphinothricin tripeptide-specific biosynthetic phsA, implying the onset of secondary metabolism
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
/ Tu 494
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two prominent maxima of enzyme activity are measured: the first maximum is found at an early stage of growth, the second lower maximum is detected at the beginning of the expression of the phosphinothricin tripeptide-specific biosynthetic phsA, implying the onset of secondary metabolism
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aconitase isozyme expression profile during fruit development, overview
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changes in enzyme activity in myocardial ischemia are coupled to accumulation of citrate, overview
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aconitase-specific activity increases by 12% at 2% O2 compared to 21% O2
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activity is significantly higher in liver of rats treated with N-nitro-L-arginine methylester
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under normal conditions and during toxic hepatitis. Toxic hepatitis is accompanied by inactivation of aconitate hydratase
mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate
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isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
additional information
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
additional information
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the carbon source, e.g. glucose, sucrose, glycerol, or sunflower oil, influences the citrate/isocitrate ratio in the cells, overview