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Information on EC 4.2.1.3 - aconitate hydratase
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4.2.1.3 aconitate hydrataseIUBMB Comments
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
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Word Map
- 4.2.1.3
-
iron-sulfur
-
transferrin
-
tricarboxylic
- succinate
- malate
-
citric
-
rna-binding
- frataxin
- heme
- neurodegenerative
-
krebs
- fumarase
-
iron-dependent
- friedreich
- ataxia
- overload
- parkinson
- alpha-ketoglutarate
-
stem-loops
-
erythroid
-
bioenergetics
- fluorocitrate
-
ferrous
-
county
- peroxynitrite
- mnsod
-
iron-deficient
-
ferroportin
- fluoroacetate
-
post-transcriptionally
- alabama
-
iron-induced
-
georgia
-
hepcidin
-
iron-mediated
-
cluster-containing
-
iron-replete
- cubane
-
nadp-isocitrate
-
kennedy
- itaconate
-
mitochondria-targeted
-
soxrs
- l-ferritin
- isopropylmalate
-
desulfurase
- hemochromatosis
-
ferrochelatase
-
rna-protein
- biotechnology
- environmental protection
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aconitase, irp-1, iron regulatory protein, ire-bp, macon, iron regulatory protein 1, cytoplasmic aconitase, aconitase a, c-aconitase, iron-responsive element binding protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AcnA
AcnA3
AcnB
ACO
Aco1
Aco2
aconitase
aconitase B
aconitase/2-methylaconitate hydratase
Aconitate hydratase
cis-aconitase
-
-
-
-
citB
citrate hydro-lyase
-
-
-
-
Ferritin repressor protein
-
-
-
-
hydratase, aconitate
-
-
-
-
IP210
-
-
-
-
IRE-BP
-
-
-
-
Iron regulatory protein
-
-
-
-
iron regulatory protein 1
iron-responsive element binding protein
-
-
-
-
IRP
-
-
-
-
IRP-1
IRP1
Major iron-containing protein
-
-
-
-
MICP
-
-
-
-
SPBP4H10.15
aconitase
-
-
-
-
Aconitate hydratase
-
-
-
-
Aconitate hydratase
B3TZE0
bifunctional enzyme: aconitate hydratase 2/2-methylisocitrate dehydratase
Aconitate hydratase
B3TZE0
bifunctional enzyme: aconitate hydratase 2/2-methylisocitrate dehydratase
-
IRP1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Citrate = cis-aconitate + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
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CAS REGISTRY NUMBER
COMMENTARY
9024-25-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
?
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
?
(Z)-2-methylaconitate
2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
-
-
?
(Z)-2-methylaconitate
2-methylisocitrate
the enzyme is involved in the methylcitric acid cycle
-
-
?
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
additional information
?
-
-
additionally to catalytic activity, enzyme is able to bind specifically the 5’ UTP of the Arabidopsis chloroplastic CuZn superoxide dismutase 2 mRNA. Enzyme does not bind an iron responsive element of the human ferritin gene
-
-
-
additional information
?
-
-
bifunctional protein, showing aconitase activity in presence of iron and RNA binding activity when cells are iron-deprived
-
?
additional information
?
-
-
amino acid residues Arg741 and Gln745 play great role in the aconitase function
-
-
-
additional information
?
-
-
aconitase binds bound to the citrate synthase 5' leader RNA in vitro
-
-
-
additional information
?
-
-
amino acid residues Arg741 and Gln745 play great role in the aconitase function
-
-
-
additional information
?
-
-
Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
-
?
additional information
?
-
Q8RP87
Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
-
?
additional information
?
-
-
iron-responsive element binding protein is required in the posttranscriptional regulation of ferritin mRNA translation and stabilization of transferrin receptor mRNA
-
-
-
additional information
?
-
isoform IRP-1A binds in vitro both Drosophila ferritin iron-responsive element and human ferritin iron-responsive element in the presence of a reducing agent
-
-
-
additional information
?
-
isoform IRP-1A binds in vitro both Drosophila ferritin iron-responsive element and human ferritin iron-responsive element in the presence of a reducing agent
-
-
-
additional information
?
-
no detectable activity with (2S,3S)-methylcitrate
-
?
additional information
?
-
-
aconitase B is the major isoenzyme which is synthesized earlier in the growth cycle than aconitase A and is subject to catabolite and anaerobic repression
-
-
-
additional information
?
-
-
the HEAT-like domain, implies a role in protein-protein recognition
-
?
additional information
?
-
-
aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator
-
-
-
additional information
?
-
-
weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle
-
-
-
additional information
?
-
-
the active sites within ICDH-AcnB catalyze the three consecutive reactions, in which citrate is converted to 2-oxoglutarate, via cisaconitate and isocitrate
-
-
-
additional information
?
-
the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
-
-
-
additional information
?
-
the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity
-
-
-
additional information
?
-
no detectable activity with (2S,3S)-methylcitrate
-
?
additional information
?
-
-
C1 aconitase is constitutive of the glyoxylate cycle. In addition, the same isoform is found to be active during pathogenic attack as well, hypocotyls. It might by assumed that in such a case the glyoxylate cycle is reinitiated as a part of a carbon reallocation system feeding on the diseased tissue cellular components
-
?
additional information
?
-
-
using electrophoretic mobility shift assays and RNA footprinting it is shown that apo-AcnB binds to the 3'-untranslated region of the pgdA RNA transcript
-
-
-
additional information
?
-
-
2fold increase in mitochondrial cis-aconitase activity in UVA-exposed cells coincides with the time of maximal heme oxygenase-1 expression. Modulation of cis-aconitase activity at the translational level by an increase of cellular iron is an important consequence of heme oxygenase-1 activation
-
?
additional information
?
-
-
IRP1 functions as a cytoplasmic aconitase. It may provide a link between citrate and iron metabolism and may be involved in oxidative stress response
-
-
-
additional information
?
-
-
key enzyme for citrate oxidation in the epithelial cell of the human prostate. Hemin and ferric ammonium citrate increase activity and gene expression
-
-
-
additional information
?
-
-
impairing aconitase activity precedes decreased cell proliferation
-
-
-
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Blocking of isozyme mAH expression and activity by 40-60% causes a decrease in ATP biosynthesis, increase in citrate secretion, and reduction of the rate of proliferation of human prostate carcinoma cells. extracellular H2O2 strongly induces IRP1 through a signal cascade, introduction of a source of iron ions enhances glutamate secretion in cultivated lens cells and neurons through an increase in cAH activity and intensification of isocitrate formation. The maximal activity requires the presence of sulfhydryl compounds in the medium
-
-
-
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. A decrease in enzyme activity is observed in some neurodegenerative diseases associated with the development of oxidative stress, in particular, Parkinson’s and Alzheimer’s diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
-
-
-
additional information
?
-
-
it is demonstrated that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1). The inability to produce normal levels of the mitochondrial protein frataxin causes the hereditary degenerative disorder Friedreich’s Ataxia (FRDA)
-
-
-
additional information
?
-
-
iron regulatory protein-1 controls the expression of several mRNAs by binding to iron-responsive elements in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. Iron regulatory protein activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2
-
?
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
-
-
-
additional information
?
-
-
in addition to aconitase activity, enzyme binds with high specificity to iron-responsive element-like RNA sequences. Iron is required for aconitase activity, but inhibits the RNA-binding activity, the two activities are mutually exclusive
-
-
-
additional information
?
-
-
one or more of the aconitases may contribute to the control of the synthesis of the virulence factor exotoxin A
-
-
-
additional information
?
-
-
aconitase is part of a multienzyme complex of the tricarboxylic acid cycle. Individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex
-
-
-
additional information
?
-
-
Mn2+ exposure leads to a region-specific alteration in total aconitase: 48.5% reduction of the enzyme activity in frontal cortex, 33.7% in striatum and 20.6% in substantia nigra. This leads to the disruption of mitochondrial energy production and cellular Fe metabolism in the brain
-
-
-
additional information
?
-
-
the enzyme is involved in the assimilation of Fe and excess dietary Zn can result in negative interactions
-
-
-
additional information
?
-
-
effects of lipoic acid on intensity of free radical reactions, citrate content, and aconitate hydratase during myocardial ischemia, overview
-
-
-
additional information
?
-
regulation of mitochondrial aconitase activity by protein kinase C-dependent phosphorylation, augmented phosphorylation of mitochondrial aconitase in diabetic hearts is associated with an increase in its reverse activity, converting isocitrate to aconitate, while the rate of the forward activity is unchanged, overview
-
-
-
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
-
additional information
?
-
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. IRP2 dominates in the regulation of iron metabolism in mammals. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
-
additional information
?
-
IRP shows RNA-binding activity, which is affected by some hormones and growth factors, e.g. thyroid, erythropoietin, and epidermal growth factor
-
-
-
additional information
?
-
-
toxic hepatitis is accompanied by inactivation of aconitate hydratase. Inhibition of the enzyme probably contributes to intracellular accumulation of citrate and inhibition of the Fenton reaction
-
-
-
additional information
?
-
-
in cytosol the enzyme participates in the glyoxylate shunt, in mitochondria the enzyme participates in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
enzyme binds to both ds- and ssDNA, with a preference for GC-containing sequences. It protects mitochondrial DNA from excessive accumulation of point mutations and ssDNA breaks and suppresses reductive recombination of mitochondrial DNA
-
-
-
additional information
?
-
-
inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
-
?
additional information
?
-
-
apo-AcnA is an RNA binding protein as shown in gel shift assays
-
-
-
additional information
?
-
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
/ Tu 494
-
inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
-
?
additional information
?
-
the mechanism requires that the intermediate product cis-aconitate, flip over by 180° about the Calpha-Cbeta double bond
-
?
additional information
?
-
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
-
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
-
inductively formed in presence of fluorocitrate
-
-
-
additional information
?
-
-
inductively formed in presence of fluoroacetate
-
-
-
additional information
?
-
-
inductively formed in presence of fluoroacetate
-
-
-
additional information
?
-
-
cytoplasmic aconitase/iron regulatory protein 1 homolog is up-regulated in the pulvinus bundle sheath cells after gravistimulation in presence of H2O2 and ascorbic acid, overview. Reactive oxygen species levels increase rapidly in gravistimulated maize pulvini
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(Z)-2-methylaconitate
2-methylisocitrate
P09339
the enzyme is involved in the methylcitric acid cycle
-
-
?
(Z)-2-methylaconitate
2-methylisocitrate
P09339
the enzyme is involved in the methylcitric acid cycle
-
-
?
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
P36683
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
P36683
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
cis-aconitate + H2O
isocitrate
P25516, P36683
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
P25516, P36683
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
additional information
?
-
-
bifunctional protein, showing aconitase activity in presence of iron and RNA binding activity when cells are iron-deprived
-
?
additional information
?
-
-
aconitase binds bound to the citrate synthase 5' leader RNA in vitro
-
-
-
additional information
?
-
-
Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
-
?
additional information
?
-
Q8RP87
Bacteroides fragilis has two separate pathways to generate alpha-ketoglutarate, either of which is sufficient for growth, a heme-dependent pathway and a heme-independent pathway. Aconitase is involved in the heme-independent pathway
-
?
additional information
?
-
-
iron-responsive element binding protein is required in the posttranscriptional regulation of ferritin mRNA translation and stabilization of transferrin receptor mRNA
-
-
-
additional information
?
-
-
aconitase B is the major isoenzyme which is synthesized earlier in the growth cycle than aconitase A and is subject to catabolite and anaerobic repression
-
-
-
additional information
?
-
-
the HEAT-like domain, implies a role in protein-protein recognition
-
?
additional information
?
-
-
aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator
-
-
-
additional information
?
-
-
weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle
-
-
-
additional information
?
-
-
C1 aconitase is constitutive of the glyoxylate cycle. In addition, the same isoform is found to be active during pathogenic attack as well, hypocotyls. It might by assumed that in such a case the glyoxylate cycle is reinitiated as a part of a carbon reallocation system feeding on the diseased tissue cellular components
-
?
additional information
?
-
-
using electrophoretic mobility shift assays and RNA footprinting it is shown that apo-AcnB binds to the 3'-untranslated region of the pgdA RNA transcript
-
-
-
additional information
?
-
-
2fold increase in mitochondrial cis-aconitase activity in UVA-exposed cells coincides with the time of maximal heme oxygenase-1 expression. Modulation of cis-aconitase activity at the translational level by an increase of cellular iron is an important consequence of heme oxygenase-1 activation
-
?
additional information
?
-
-
IRP1 functions as a cytoplasmic aconitase. It may provide a link between citrate and iron metabolism and may be involved in oxidative stress response
-
-
-
additional information
?
-
-
key enzyme for citrate oxidation in the epithelial cell of the human prostate. Hemin and ferric ammonium citrate increase activity and gene expression
-
-
-
additional information
?
-
-
impairing aconitase activity precedes decreased cell proliferation
-
-
-
additional information
?
-
P21399
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Blocking of isozyme mAH expression and activity by 40-60% causes a decrease in ATP biosynthesis, increase in citrate secretion, and reduction of the rate of proliferation of human prostate carcinoma cells. extracellular H2O2 strongly induces IRP1 through a signal cascade, introduction of a source of iron ions enhances glutamate secretion in cultivated lens cells and neurons through an increase in cAH activity and intensification of isocitrate formation. The maximal activity requires the presence of sulfhydryl compounds in the medium
-
-
-
additional information
?
-
P21399
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. The enzyme may be involved also in regulation of individual enzyme activities. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. A decrease in enzyme activity is observed in some neurodegenerative diseases associated with the development of oxidative stress, in particular, Parkinson’s and Alzheimer’s diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
-
-
-
additional information
?
-
-
it is demonstrated that the extramitochondrial form of frataxin directly interacts with cytosolic aconitase/iron regulatory protein-1 (IRP1). The inability to produce normal levels of the mitochondrial protein frataxin causes the hereditary degenerative disorder Friedreich’s Ataxia (FRDA)
-
-
-
additional information
?
-
-
iron regulatory protein-1 controls the expression of several mRNAs by binding to iron-responsive elements in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. Iron regulatory protein activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2
-
?
additional information
?
-
P28271
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
-
-
-
additional information
?
-
-
one or more of the aconitases may contribute to the control of the synthesis of the virulence factor exotoxin A
-
-
-
additional information
?
-
-
aconitase is part of a multienzyme complex of the tricarboxylic acid cycle. Individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex
-
-
-
additional information
?
-
-
Mn2+ exposure leads to a region-specific alteration in total aconitase: 48.5% reduction of the enzyme activity in frontal cortex, 33.7% in striatum and 20.6% in substantia nigra. This leads to the disruption of mitochondrial energy production and cellular Fe metabolism in the brain
-
-
-
additional information
?
-
-
the enzyme is involved in the assimilation of Fe and excess dietary Zn can result in negative interactions
-
-
-
additional information
?
-
-
effects of lipoic acid on intensity of free radical reactions, citrate content, and aconitate hydratase during myocardial ischemia, overview
-
-
-
additional information
?
-
Q9ER34
regulation of mitochondrial aconitase activity by protein kinase C-dependent phosphorylation, augmented phosphorylation of mitochondrial aconitase in diabetic hearts is associated with an increase in its reverse activity, converting isocitrate to aconitate, while the rate of the forward activity is unchanged, overview
-
-
-
additional information
?
-
Q63270
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
-
additional information
?
-
Q63270
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. IRP2 dominates in the regulation of iron metabolism in mammals. Decrease in enzyme activity and increase in citrate content in the tissues of mammals under hypoxia, ischemia, hyperoxia, and CCl4-induced hepatitis. Regulation, overview
-
-
-
additional information
?
-
-
toxic hepatitis is accompanied by inactivation of aconitate hydratase. Inhibition of the enzyme probably contributes to intracellular accumulation of citrate and inhibition of the Fenton reaction
-
-
-
additional information
?
-
-
in cytosol the enzyme participates in the glyoxylate shunt, in mitochondria the enzyme participates in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
-
?
additional information
?
-
-
apo-AcnA is an RNA binding protein as shown in gel shift assays
-
-
-
additional information
?
-
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
/ Tu 494
-
inactivation of the tricarboxylic acid cycle aconitase gene impairs the morphological and physiological differentiation of Streptomyces viridochromogenes Tue949, which produces the herbicide phosphinothricin tripeptide
-
?
additional information
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Q9NJQ8
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
Q9NJQ9
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
-
the enzyme does not take part in the mitochondrial Krebs cycle but may have a yet unknown function in the cytoplasm of the parasite
-
?
additional information
?
-
-
inductively formed in presence of fluorocitrate
-
-
-
additional information
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-
-
inductively formed in presence of fluoroacetate
-
-
-
additional information
?
-
-
inductively formed in presence of fluoroacetate
-
-
-
additional information
?
-
-
cytoplasmic aconitase/iron regulatory protein 1 homolog is up-regulated in the pulvinus bundle sheath cells after gravistimulation in presence of H2O2 and ascorbic acid, overview. Reactive oxygen species levels increase rapidly in gravistimulated maize pulvini
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
-
HOSCN induces rapid and efficient release of iron from aconitase. Blocking the [4Fe-4 S] cluster inhibits HOSCN-mediated inactivation
[4Fe-4S]-center
the [4Fe-4S]2+ cluster of AcnA3 is more stable against oxidative inactivation by ferricyanide than that of isoform AcnA4
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
Iron
Mg2+
Zn
-
an X-ray fluorescence measurement performed on a gold-derivative crystal shows the unexpected presence of zinc, in addition to gold and iron
[4Fe-4S] center
-
acon harbors a single unligated iron atom in its [4Fe-4S], enzyme is in this respect unique in mitochondria
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+
Fe
-
a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed
Fe
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
Fe2+
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview; the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Fe2+
required; required, both isoenzymes have an [4Fe-4S] iron-sulfur cluster bound with cysteine residues Cys437, Cys503, and Cys506, under the action of reductants, the active enzyme form is produced with a complex cation of the [3Fe–3S]2+ type, structure, and mechanism of activation of the enzyme by Fe2+, overview
Fe2+
-
required, the enzyme contains iron-sulfur clusters. Chelating mitochondrial free iron in various cell systems causes loss of aconitase activity
Fe2+
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
Fe2+
required, binding structure in the [Fe-S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Fe2+
required, binding structure in the [4Fe-4S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Fe2+
-
enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
Fe2+
-
activates the enzyme under normal conditions and in animals with toxic hepatitis. The stimulatory effect of Fe2+ in concentrations below 1 mM is less pronounced than in animals with toxic hepatitis
Iron
-
[4Fe-4S] cluster. 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
Iron
-
inactive aconitase contains an oxidized [3Fe-4S]+cluster. Full activity is achieved with one electron per 3Fe cluster and at least 0.6 gatoms of Fe2+ per mol. The process involves building up of [4Fe-4S]2+ clusters
Iron
-
cytosolic and mitochondrial isoenzyme require an intact [4Fe-4S] cluster. Mitochondrial aconitase is isolated predominantly in the [3Fe-4S] form (Fe/S ratio of 0.73) and must be activated by the addition of Fe2+. The cytoplasmic aconitase as isolated is about 80% active with a Fe/S ratio of 1.1
Iron
-
iron-induced increase in L-glutamate availability increases via the aconitase pathway L-cystine uptake, with subsequent increases in glutathione levels
Iron
-
the active form contains a [4Fe-4S]+ cluster, the inactive form contains a [3Fe-4S]+ cluster
Iron
-
a significant proportion of the enzyme is in the inactive [3Fe-4S]1+ or apoenzyme forms. AcnB contains a much higher proportion of inactive enzyme than AcnA
Iron
under iron-replete conditions, enzyme binds a [4Fe-4S] cluster und functions as cytosolic aconitase. Under iron shortage, enzyme is involved in translational control as an iron regulatory protein
Iron
-
iron regulatory protein-1 controls the expression of several mRNAs by binding to iron-responsive elements in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. Iron regulatory protein activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2
Iron
-
iron is required for aconitase activity, but inhibits the RNA-binding activity, the two activities are mutually exclusive
Iron
-
Cys358, Cys421 and Cys424 are ligands to the Fe-S cluster in the inactive [3Fe-4S] form and the active [4Fe-4S] form
Iron
in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deferiprone
-
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
-
isoenzyme is inhibited, isoenzyme I is less or not sensitive
HOCl
-
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
-
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
-
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+
-
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
-
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
-
irreversible inactivation both in presence and absence of substrate
oxalomalic acid
-
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+
-
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
-
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
-
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
-
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
-
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
-
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+
-
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
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
-
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
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
lipoic acid
-
causes an increase in cardiac enzyme activity at doses of 35 and 70 mg/kg of 1.3 and 2.4fold in the animals
menadione sodium bisulfite
-
causes a modest activation of IRP-1 to bind to iron resonsive elements within 15-30 min. Menadione-induced oxidative stress leads to post-translational inactivation of both genetic and enzymatic functions of IRP-1 by a mechanism that lies beyond the classical Fe-S cluster switch and exerts multiple effects on cellular iron metabolism
additional information
the maximal activity requires the presence of sulfhydryl compounds in the medium; the maximal activity requires the presence of sulfhydryl compounds in the medium
-
additional information
acetyl-CoA-driven acetylation leads to about 45% activation. The increase in activity is a result of increased maximal velocity
-
additional information
the maximal activity requires the presence of sulfhydryl compounds in the medium; the maximal activity requires the presence of sulfhydryl compounds in the medium
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
cis-aconitate
-
pH 8, 25°C, Lineweaver-Burk method
5.3
citrate
-
pH 8, 25°C, Lineweaver-Burk method
0.9
isocitrate
-
pH 8, 25°C, Lineweaver-Burk method
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
Saccharomycopsis lipolytica
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
two values are obtained for KM-value with isocitrate as substrate, depending on substrate concentration
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
citrate
-
pH 8, 25°C, Lineweaver-Burk method
1.1
isocitrate
-
pH 8, 25°C, Lineweaver-Burk method
5.2
cis-aconitate
-
pH 8, 25°C, Lineweaver-Burk method
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26
cis-aconitate
-
pH 8, 25°C, Lineweaver-Burk method
1
citrate
-
pH 8, 25°C, Lineweaver-Burk method
1.2
isocitrate
-
pH 8, 25°C, Lineweaver-Burk method
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.81
D-glucose 1-phosphate
-
mitochondrial enzyme, with isocitrate as substrate
1.14
D-glucose 6-phosphate
-
mitochondrial enzyme, with isocitrate as substrate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
Fluorocitrate
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication, tissue: brain
0.012
Fluorocitrate
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication, tissue: heart
0.024
Fluorocitrate
Rattus norvegicus
-
pH 7.4, temperature not specified in the publication, tissue: kidney; pH 7.4, temperature not specified in the publication, tissue: liver
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.011 - 0.06
-
aconitate hydratase in blood serum of control rats and rats subjected to myocardial ischemia and treatment with lipoic acid, overview
0.068 - 0.198
-
aconitate hydratase in myocardium of control rats and rats subjected to myocardial ischemia and treatment with lipoic acid, overview
0.433
-
reverse reaction, hydration of citrate or isocitrate, pH 8.0, 30°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5
7.5
-
enzyme form AcnA and AcnB, the maximal activity of AcnB is nearly 2fold the activity of AcnA
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
6 - 9
6.4 - 8.2
-
pH 6.4: about 60% of maximal activity, pH 8.2: about 75% of maximal activity
5 - 10
-
pH 5.0: about 75% of maximal activity, pH 10.0: about 60% of maximal activity, AcnA
6 - 9
-
pH 6: about 55% of maximal activity, pH 9: about 40% of maximal activity, isoenzyme I. pH 6: about 25% of maximal activity, pH 9: about 75% of maximal activity isoenzyme II
6 - 9
-
pH 6.0: about 55% of maximal activity, pH 9.0: about 20% of maximal activity, AcnB
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
about 60% of maximal activity at 20°C and at 40°C, isoenzyme I. 20°C: about 40% of maximal activity, 40°C: about 20% of maximal activity, isoenzyme II
50 - 90
-
50°C: about 40% of maximal activity, 90°C: about 45% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.2
-
by IEF-PAGE, identification of 9 different forms with pI-values from 6.5-7.2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strain JRG3171, contains two major aconitases, AcnA and AcnB
-
-
brenda
bifunctional enzyme with aconitase activity and working as iron-responsive protein. Since iron is required for aconitase activity, but inhibits the RNA-binding activity, the two activities are mutually exclusive
-
-
brenda
gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21. Two types of aco2+ transcripts are generated, producing both a single aconitase domain protein and the fusion form
UniProt
brenda
gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21. Two types of aco2+ transcripts are generated, producing both a single aconitase domain protein and the fusion form
UniProt
brenda
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
strain Tu494
-
-
brenda
under iron-sufficiency conditions, AcnA functions as an enzyme of the tricarboxylic acid cycle, whereas under iron depletion it is a regulator of iron metabolism and oxidative stress response
UniProt
brenda
isoforms Aco1, Aco2, Aco3. Cytosolic aconitase is not converted into an iron-responsive element and does not regulate iron homeostasis
-
-
brenda
early aconitase (isoenzyme I) is present in a culture of 5 h age, late aconitase (isoenzyme II) is present in 12 h age
-
-
brenda
early aconitase (isoenzyme I) is present in a culture of 5 h age, late aconitase (isoenzyme II) is present in 12 h age; T
-
-
brenda
bifunctional protein, with aconitase activity and RNA binding activity
-
-
brenda
isoforms IRP-1A, the isoform shows aconitase activity, and additionally binds to iron-responsive elements
SwissProt
brenda
isoforms IRP-1B, the isoform shows aconitase activity, but does not bind to iron-responsive elements
SwissProt
brenda
-
-
-
brenda
bifunctional iron regulatory protein and cytosolic acontiatse
UniProt
brenda
-
-
-
brenda
aconitase 2; Wistar rats, aconitase 2 encoded by gene Aco2
UniProt
brenda
-
-
-
brenda
under iron-sufficiency conditions, AcnA functions as an enzyme of the tricarboxylic acid cycle, whereas under iron depletion it is a regulator of iron metabolism and oxidative stress response
UniProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is significantly higher in bone marrow of rats treated with N-nitro-L-arginine methylester
brenda
-
repeated contractions increase aconitase activity by 50%. Increase is not accompanied by increase in aconitase protein, but is markedly inhibited by cyclosporin A
brenda
-
undifferentiated neonatal cardiomyocyte. In heat-shocked cells aconitase activity is reduced
brenda
-
mitochondrial aconitase is over-expressed in primary mesencephalic cultures
brenda
purified human CD34+ progenitors derived from granulocyte-colony stimulating factor mobilized peripheral blood cells of normal donors; purified human CD34+ progenitors derived from granulocyte-colony stimulating factor mobilized peripheral blood cells of normal donors
brenda
-
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
brenda
expression is transiently induced during germination
brenda
-
muscle exercise does not affect aconitase activity despite increased oxidative stress
brenda
-
activity is significantly higher in spleen of rats treated with N-nitro-L-arginine methylester
brenda
additional information
inactive isozyme mAH multimers occur in rat brain in a model of Huntington’s disease
brenda
-
aconitase-specific activity increases by 42% at 2% O2 compared to 21% O2
brenda
-
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
brenda
Streptomyces viridochromogenes DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 / Tu 494
-
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
-
brenda
aconitase isozyme expression profile during fruit development, overview; aconitase isozyme expression profile during fruit development, overview; aconitase isozyme expression profile during fruit development, overview
brenda
-
changes in enzyme activity in myocardial ischemia are coupled to accumulation of citrate, overview
brenda
-
aconitase-specific activity increases by 12% at 2% O2 compared to 21% O2
brenda
-
activity is significantly higher in liver of rats treated with N-nitro-L-arginine methylester
brenda
-
under normal conditions and during toxic hepatitis. Toxic hepatitis is accompanied by inactivation of aconitate hydratase
brenda
mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate; mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate
brenda
additional information
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
brenda
additional information
-
the carbon source, e.g. glucose, sucrose, glycerol, or sunflower oil, influences the citrate/isocitrate ratio in the cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
isoforms Aco1, Aco2, Aco3. Cytosolic aconitase is not converted into an iron-responsive element and does not regulate iron homeostasis
brenda
more than 90% of ACO3 activity is cytosolic. An iron-sulfur centre assembly mutant atm3-1 shows reduced cytosolic ACO activity
brenda
cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
brenda
cytosolic isozyme cAH; IRP1 is a cytosolic isozyme devoid of labile Fe2+
brenda
cytosolic isozyme cAH; IRP1 is a cytosolic isozyme devoid of labile Fe2+
brenda
-
79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
brenda
-
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
brenda
-
localized both to the cytosol and mitochondria by a reverse translocation mechanism
brenda
-
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
-
brenda
bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
brenda
-
bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
-
brenda
-
analysis of mitochondrial proteome, identification of two particular N-formylkynurenine modifications of enzyme
brenda
-
acclimation at 28°C results in strong decrease in enzyme mRNA and activity as well as in LON protease mRNA and activity
brenda
-
mitochondrial aconitase activity represents up to 80% of the total aconitase activity in skin fibroblasts
brenda
-
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
brenda
-
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
brenda
-
particulate-bound mitochondrial enzyme, the soluble mitochondrial enzyme is released from the mitochondria by freezing and thawing
brenda
-
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
brenda
-
-
brenda
-
79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
brenda
-
enzyme is a component of mitochondrial DNA nucleoids
brenda
-
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
brenda
-
localized both to the cytosol and mitochondria by a reverse translocation mechanism
brenda
-
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
-
brenda
bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
brenda
-
bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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brenda
bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
brenda
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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brenda
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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brenda
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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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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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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mutant shows severe defects in morphology and physiology, as is unable to form any aerial mycelium, spores or phosphinothricin tripeptide
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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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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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
metabolism
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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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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; 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
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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
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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
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 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
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
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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
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
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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
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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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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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PDB
SCOP
CATH
UNIPROT
ORGANISM