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(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
(Z)-2-methylaconitate
2-methylisocitrate
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
2-methylisocitrate
alpha-methyl-cis-aconitate
alpha-methylisocitrate
cis-aconitate + H2O
citrate
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
isocitrate
cis-aconitate + H2O
threo-D-alpha-methylisocitrate
?
Saccharomycopsis lipolytica
-
-
-
-
?
additional information
?
-
(2R,3S)-2-methylisocitrate

(Z)-2-methyl-aconitate + H2O
-
-
-
r
(2R,3S)-2-methylisocitrate
(Z)-2-methyl-aconitate + H2O
-
-
-
r
(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
(Z)-2-methylaconitate + H2O

2-methylisocitrate
-
-
-
?
(Z)-2-methylaconitate + H2O
2-methylisocitrate
-
-
-
?
alpha-methyl-cis-aconitate

alpha-methylisocitrate
-
-
-
?
alpha-methyl-cis-aconitate
alpha-methylisocitrate
Saccharomycopsis lipolytica
-
-
-
?
cis-aconitate

citrate
-
-
-
r
cis-aconitate
citrate
-
-
-
r
cis-aconitate

isocitrate
-
-
-
?
cis-aconitate
isocitrate
-
-
-
r
cis-aconitate
isocitrate
-
-
-
?
cis-aconitate
isocitrate
-
-
-
?
cis-aconitate
isocitrate
-
-
-
-
?
cis-aconitate
isocitrate
-
-
-
-
?
cis-aconitate
isocitrate
-
-
-
r
cis-aconitate + H2O

?
-
-
-
?
cis-aconitate + H2O
?
-
-
-
?
cis-aconitate + H2O

citrate
-
-
-
-
r
cis-aconitate + H2O
citrate
-
-
-
-
?
cis-aconitate + H2O
citrate
-
-
-
-
r
cis-aconitate + H2O
citrate
Saccharomycopsis lipolytica
-
-
-
-
r
cis-aconitate + H2O
citrate
-
-
-
-
r
cis-aconitate + H2O
citrate
-
-
-
?
cis-aconitate + H2O

isocitrate
-
-
-
?
cis-aconitate + H2O
isocitrate
-
-
-
?
cis-aconitate + H2O
isocitrate
-
-
-
r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
cis-aconitate + H2O
isocitrate
-
-
-
-
?
cis-aconitate + H2O
isocitrate
-
-
-
-
?
citrate

cis-aconitate
-
-
-
?
citrate
cis-aconitate
-
-
-
?
citrate
cis-aconitate
-
-
-
r
citrate
cis-aconitate
-
-
-
?
citrate
cis-aconitate
-
-
-
?
citrate
cis-aconitate
-
-
-
-
?
citrate
cis-aconitate
-
-
-
?
citrate
cis-aconitate
-
-
-
r
citrate

cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate

isocitrate
-
-
-
r
citrate
isocitrate
-
-
-
-
?
citrate
isocitrate
-
-
-
-
?
citrate
isocitrate
-
-
-
-
?
citrate
isocitrate
-
-
-
?
citrate
isocitrate
-
-
-
r
citrate
isocitrate
-
-
-
-
?
citrate
isocitrate
-
-
-
-
r
citrate
isocitrate
-
-
-
-
?
citrate
isocitrate
Saccharomycopsis lipolytica
-
-
-
-
?
citrate
isocitrate
-
-
-
r
citrate
isocitrate
-
-
-
-
r
isocitrate

?
-
-
-
?
isocitrate

cis-aconitate
-
-
-
?
isocitrate
cis-aconitate
-
-
-
r
isocitrate
cis-aconitate
-
-
-
?
isocitrate
cis-aconitate
-
-
-
?
isocitrate
cis-aconitate
-
-
-
?
isocitrate
cis-aconitate
-
-
-
-
?
isocitrate
cis-aconitate
-
-
-
r
isocitrate
cis-aconitate
-
-
-
-
?
isocitrate
cis-aconitate
-
-
-
?
isocitrate

cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
?
isocitrate
cis-aconitate + H2O
-
-
-
?
isocitrate
cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
-
?
isocitrate
cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
-
?
isocitrate
cis-aconitate + H2O
-
-
-
-
r
isocitrate
cis-aconitate + H2O
-
-
-
-
?
isocitrate

citrate
-
-
-
r
isocitrate
citrate
-
-
-
-
?
isocitrate
citrate
-
-
-
-
?
isocitrate
citrate
-
-
-
-
?
isocitrate
citrate
-
-
-
r
isocitrate
citrate
-
-
-
-
?
isocitrate
citrate
Saccharomycopsis lipolytica
-
-
-
-
?
isocitrate
citrate
-
-
-
r
isocitrate
citrate
-
-
-
-
r
additional information

?
-
-
additionally to catalytic activity, enzyme is able to bind specifically the 5â 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
?
-
-
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
?
-
Cucurbita sp.
-
enzyme is involved in the glyoxylate cycle
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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. 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, Parkinsonâs and Alzheimerâs diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
-
-
?
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, Parkinsonâs and Alzheimerâs 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 Friedreichâs 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
?
-
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. 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
?
-
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
?
-
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.
(Z)-2-methylaconitate
2-methylisocitrate
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
cis-aconitate + H2O
isocitrate
citrate
cis-aconitate + H2O
additional information
?
-
(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
-
-
-
?
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
cis-aconitate + H2O
isocitrate
-
-
-
-
?
citrate

cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
r
citrate
cis-aconitate + H2O
-
-
-
?
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
?
citrate
cis-aconitate + H2O
-
-
-
-
?
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
?
-
-
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
?
-
Cucurbita sp.
-
enzyme is involved in the glyoxylate cycle
-
-
?
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
?
-
-
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
?
-
-
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. 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, Parkinsonâs and Alzheimerâs diseases. Regulation, overview. Extracellular H2O2 strongly induces IRP1 through a signal cascade
-
-
?
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, Parkinsonâs and Alzheimerâs 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 Friedreichâs 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
?
-
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
?
-
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. 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
?
-
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
?
-
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
-
-
?
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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
Fe

-
a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed
Fe
-
IRP1 binds a [4Fe-4S] cluster
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
Fe2+
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 [3Feâ3S]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+
-
mitochondrial aconitase contains iron-sulfur cluster
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 a single [3Fe-4S]cluster
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
-
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
activity is posttranslationally regulated by iron
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
-
contains a [4Fe-4D] cluster
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
-
the enzyme contains a [4Fe-4S]2+ cluster
Iron
-
the enzyme hosts an interconvertible [3Fe-4S] cluster
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
-
crystallographic evidence for a three-iron center
Iron
-
contains 2 gatoms of non-heme iron per mol of enzyme
Iron
-
iron-sulfur enzyme
Iron
in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms
Iron
-
contains 2.1 mol of iron per mol of enzyme
Iron
-
contains 2 gatoms of non-heme iron per mol of enzyme
Mg2+

-
additional information

-
IRP1 is a cytosolic isozyme devoid of labile Fe2+
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+
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1,2,3,4-tetracarboxycyclopentane
-
competitive
1,2,3-tricarboxycyclopentene-1
-
competitive
1,3,5-tricarboxypentane
-
competitive
2,2'-dipyridyl
-
noncompetitive
4-hydroxy-2-oxoglutarate
-
competitive
adipate
Saccharomycopsis lipolytica
-
-
ADP
-
inhibition at levels well above its physiological concentration
alpha-picolinic acid
-
noncompetitive
D-glucose 1-phosphate
-
-
D-glucose 6-phosphate
-
-
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
fluoroacetate
Saccharomycopsis lipolytica
-
-
GDP
-
inhibition at levels well above its physiological concentration
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
hydrogen peroxide
-
inhibits enzyme activity in cell-free extracts
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
Maleate
Saccharomycopsis lipolytica
-
-
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
p-hydroxymercuribenzoate
-
-
Phthalic acid
-
competitive
pyromellitic acid
-
competitive
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
threo-Ls-isocitrate
-
competitive
-
trimellitic acid
-
competitive
trimesic acid
-
competitive
1,10-phenanthroline

-
noncompetitive
1,10-phenanthroline
Saccharomycopsis lipolytica
-
-
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
Cd2+
-
inactivation of enzyme, particularly at elevated temperature
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

-
-
Fluorocitrate
-
mechanism-based inhibitor
Fluorocitrate
Cucurbita sp.
-
competitive
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
Fluorocitrate
-
linear competitive
Fluorocitrate
-
linear competitive
fructose-6-phosphate

-
fumarate

-
-
glyoxylate

-
-
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
H2O2
-
2.3 mM, 90-95% inhibition
malate

-
-
oxaloacetate

-
-
oxaloacetate
-
parabolic noncompetitive
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
Oxalomalate
-
competitive
Oxalomalate
-
competitive
Oxalomalate
-
competitive
Oxalomalate
-
competitive
oxalosuccinate

-
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
Quinaldic acid

-
noncompetitive
Quinaldic acid
Saccharomycopsis lipolytica
-
-
succinate

-
-
superoxide anion radical

-
superoxide anion radical
-
trans-aconitate

a competitive inhibitor of the enzyme with respect to cis-aconitate and a non-competitive inhibitor with respect to citrate and isocitrate
trans-aconitate
-
linear competitive
tricarballylate

-
linear competitive
Zn2+

-
inhibition of mitochondrial isoenzyme
Zn2+
a specific inhibitor of mitochondrial isozyme
Zn2+
-
competitive, the inhibitory effect is specific for the citrate to cis-aconitate reaction; inhibition of mitochondrial isoenzyme; no inhibition of the cytopsolic isoenzyme
Zn2+
-
competitive inhibition
Zn2+
a specific inhibitor of mitochondrial isozyme
Zn2+
-
inhibition of mitochondrial 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
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
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
-
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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0.81 - 1.9
D-glucose 1-phosphate
1.14 - 2.35
D-glucose 6-phosphate
0.035
nitric oxide
-
reversible inhibition after brief exposure
0.18 - 3.41
trans-aconitate
0.81
D-glucose 1-phosphate

-
mitochondrial enzyme, with isocitrate as substrate
1.9
D-glucose 1-phosphate
-
cytosolic enzyme, with isocitrate as substrate
1.14
D-glucose 6-phosphate

-
mitochondrial enzyme, with isocitrate as substrate
2.35
D-glucose 6-phosphate
-
cytosolic enzyme, with isocitrate as substrate
0.4
fumarate

-
mitochondrial enzyme, with isocitrate as substrate
0.41
fumarate
-
isoform Aco1, pH 8.0, 25°C
0.51
fumarate
-
cytosolic enzyme, with isocitrate as substrate
0.58
fumarate
-
isoform Aco4, pH 8.0, 25°C
0.14
glyoxylate

-
mitochondrial enzyme, with isocitrate as substrate
0.42
glyoxylate
-
cytosolic enzyme, with isocitrate as substrate
0.68
glyoxylate
-
isoform Aco1, pH 8.0, 25°C
0.72
glyoxylate
-
isoform Aco4, pH 8.0, 25°C
0.71
malate

-
isoform Aco1, pH 8.0, 25°C
0.95
malate
-
isoform Aco4, pH 8.0, 25°C
1.81
malate
-
cytosolic enzyme, with isocitrate as substrate
2.94
malate
-
mitochondrial enzyme, with isocitrate as substrate
1.03
oxaloacetate

-
mitochondrial enzyme, with isocitrate as substrate
2.8
oxaloacetate
-
cytosolic enzyme, with isocitrate as substrate
0.33
succinate

-
mitochondrial enzyme, with isocitrate as substrate
0.58
succinate
-
isoform Aco1, pH 8.0, 25°C
0.61
succinate
-
cytosolic enzyme, with isocitrate as substrate
0.68
succinate
-
isoform Aco4, pH 8.0, 25°C
0.18
trans-aconitate

-
substrate isocitrate, isoform Aco1, pH 8.0, 25°C
0.25
trans-aconitate
-
substrate isocitrate, isoform Aco4, pH 8.0, 25°C
0.26
trans-aconitate
-
substrate citrate, isoform Aco1, pH 8.0, 25°C
0.39
trans-aconitate
-
substrate citrate, isoform Aco4, pH 8.0, 25°C
1.37
trans-aconitate
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mitochondrial enzyme, with isocitrate as substrate
3.41
trans-aconitate
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cytosolic enzyme, with isocitrate as substrate
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Cucurbita sp.
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very low activity
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food
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IRP1
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isoforms Aco1, Aco2, Aco3. Cytosolic aconitase is not converted into an iron-responsive element and does not regulate iron homeostasis
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more than 90% of ACO3 activity is cytosolic. An iron-sulfur centre assembly mutant atm3-1 shows reduced cytosolic ACO activity
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identical with iron-responsive element binding protein
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soluble isozyme
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3 cytosolic aconitases: C1, C2 and C3
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cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
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cytosolic isozyme cAH
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IRP1 is a cytosolic isozyme devoid of labile Fe2+
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cytosolic isoform
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cytosolic isozyme cAH
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IRP1 is a cytosolic isozyme devoid of labile Fe2+
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79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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localized both to the cytosol and mitochondria by a reverse translocation mechanism
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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cytoplasmic aconitase
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isoform Aco1
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isoform Aco4
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analysis of mitochondrial proteome, identification of two particular N-formylkynurenine modifications of enzyme
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mitochondrial isozyme
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acclimation at 28°C results in strong decrease in enzyme mRNA and activity as well as in LON protease mRNA and activity
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2 mitochondrial aconitases: M1 and M2
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mitochondrial aconitase activity represents up to 80% of the total aconitase activity in skin fibroblasts
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mitochondrial isozyme mAH
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significant decrease in activity with age, accompanied by relatively subtle alterations in activities of other citric acid cycle enzymes. Changes contribute to a decline in overall efficiency of mitochondrial bioenegetics with age
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mitochondrial isozyme mAH
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an age-related decrease in aconitase activity along with relatively subtle alterations in activities of other citric acid cycle enzymes may contribute to a decline in the overall efficiency of mitochondrial bioenergetics. The maximal activity of aconitase in mitochondria of 16-month-old (118 nmol aconitate/min/mg protein) and 24-month-old (108 nmol/min/mg protein) mice is consistently less than that from 6-month-old (147 aconitate/min/mg protein) mice
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particulate-bound mitochondrial enzyme, the soluble mitochondrial enzyme is released from the mitochondria by freezing and thawing
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mitochondrial isoform
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24 h after intraperitoneal administration of endotoxin, there is a 28% reduction in mitochondrial respiration and a 24% reduction in aconitase activity. Functional activity of the electron transport chain is unaffected
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mitochondrial isozyme mAH
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79% cytosolic enzyme and 21% mitochondrial enzyme for control animals, 83% cytosolic enzyme and 17% mitochondrial enzyme for starving animals
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enzyme is a component of mitochondrial DNA nucleoids
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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localized both to the cytosol and mitochondria by a reverse translocation mechanism
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aconitase in yeast is a single translation product, which is dual targeted and distributed between the mitochondria and the cytosol by a unique mechanism involving reverse translocation, dual localization, detailed overview
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus
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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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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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