BRENDA - Enzyme Database
show all sequences of 4.2.1.3

Aconitate hydratase of mammals under oxidative stress

Matasova, L.V.; Popova, T.N.; Biochemistry (Moscow) 73, 957-964 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Mus musculus
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
Rattus norvegicus
Engineering
Amino acid exchange
Commentary
Organism
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Homo sapiens
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Mus musculus
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
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
Homo sapiens
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
Mus musculus
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
Rattus norvegicus
fructose-6-phosphate
-
Homo sapiens
fructose-6-phosphate
-
Mus musculus
fructose-6-phosphate
;
Rattus norvegicus
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
Homo sapiens
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
Mus musculus
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
Rattus norvegicus
Oxalomalate
inhibition of the enzyme by oxalomalate reduces glutamate secretion and eliminates the effect of iron ions on the latter
Homo sapiens
oxalosuccinate
-
Homo sapiens
oxalosuccinate
-
Mus musculus
oxalosuccinate
;
Rattus norvegicus
peroxynitrite
inactivation due to the release of iron from the Fe-S cluster, other nitric oxide sources decrease the activity of the mitochondrial isozyme
Homo sapiens
superoxide anion radical
-
Mus musculus
superoxide anion radical
-
Rattus norvegicus
trans-aconitate
a competitive inhibitor of the enzyme with respect to cis-aconitate and a non-competitive inhibitor with respect to citrate and isocitrate
Homo sapiens
Zn2+
a specific inhibitor of mitochondrial isozyme
Mus musculus
Zn2+
a specific inhibitor of mitochondrial isozyme
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
Homo sapiens
5829
-
cytosol
cytosolic isozyme cAH; IRP1 is a cytosolic isozyme devoid of labile Fe2+
Mus musculus
5829
-
cytosol
cytosolic isozyme cAH; IRP1 is a cytosolic isozyme devoid of labile Fe2+
Rattus norvegicus
5829
-
mitochondrion
mitochondrial isozyme mAH
Homo sapiens
5739
-
mitochondrion
mitochondrial isozyme mAH
Mus musculus
5739
-
mitochondrion
mitochondrial isozyme mAH
Rattus norvegicus
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
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
Homo sapiens
Fe2+
required, binding structure in the [Fe-S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Mus musculus
Fe2+
required, binding structure in the [4Fe-4S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Rattus norvegicus
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Rattus norvegicus
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
Rattus norvegicus
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
Mus musculus
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
?
-
-
-
additional information
Homo sapiens
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
Homo sapiens
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
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Homo sapiens
P21399
IRP1
-
Mus musculus
-
-
-
Mus musculus
P28271
-
-
Rattus norvegicus
Q63270
IRP1
-
Rattus norvegicus
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
mechanism controlling IRP1 activity at the level of its stability can be phosphorylation of Ser138, Ser138, Ser711, and flanking sequences are highly conserved
Homo sapiens
Purification (Commentary)
Commentary
Organism
native IRP1 from liver
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
A-549 cell
;
Homo sapiens
-
brain
inactive isozyme mAH multimers occur in rat brain in a model of Huntington’s disease
Rattus norvegicus
-
heart
;
Homo sapiens
-
HEK-293 cell
;
Homo sapiens
-
hepatoma cell
;
Mus musculus
-
kidney
;
Homo sapiens
-
liver
;
Homo sapiens
-
liver
;
Mus musculus
-
liver
;
Rattus norvegicus
-
additional information
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
Homo sapiens
-
PC-12 cell
;
Rattus norvegicus
-
prostate gland
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
Homo sapiens
-
prostate gland cancer cell line
;
Homo sapiens
-
umbilical vein endothelial cell
;
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
696168
Rattus norvegicus
?
-
-
-
-
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
696168
Rattus norvegicus
?
-
-
-
-
additional information
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
696168
Mus musculus
?
-
-
-
-
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
696168
Homo sapiens
?
-
-
-
-
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
696168
Homo sapiens
?
-
-
-
-
additional information
IRP shows RNA-binding activity, which is affected by some hormones and growth factors, e.g. thyroid, erythropoietin, and epidermal growth factor
696168
Rattus norvegicus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 95000-100000, IRP1, SDS-PAGE
Rattus norvegicus
More
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity; depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the maximal activity requires the presence of sulfhydryl compounds in the medium
Mus musculus
additional information
the maximal activity requires the presence of sulfhydryl compounds in the medium
Rattus norvegicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Homo sapiens
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Mus musculus
additional information
naturally occuring IRP1 has no [Fe-S] cluster and is devoid of aconitase activity due to the absence of cysteine residues binding the [Fe-S] cluster in the active center
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
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
Homo sapiens
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
Mus musculus
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
Rattus norvegicus
fructose-6-phosphate
-
Homo sapiens
fructose-6-phosphate
-
Mus musculus
fructose-6-phosphate
-
Rattus norvegicus
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
Homo sapiens
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
Mus musculus
additional information
enzyme competitive inhibition by di- and tricarboxylic acids, and inactivation due to modification of cysteine and tyrosine residues
Rattus norvegicus
Oxalomalate
inhibition of the enzyme by oxalomalate reduces glutamate secretion and eliminates the effect of iron ions on the latter
Homo sapiens
oxalosuccinate
-
Homo sapiens
oxalosuccinate
-
Mus musculus
oxalosuccinate
-
Rattus norvegicus
peroxynitrite
inactivation due to the release of iron from the Fe-S cluster, other nitric oxide sources decrease the activity of the mitochondrial isozyme
Homo sapiens
superoxide anion radical
-
Mus musculus
superoxide anion radical
-
Rattus norvegicus
trans-aconitate
a competitive inhibitor of the enzyme with respect to cis-aconitate and a non-competitive inhibitor with respect to citrate and isocitrate
Homo sapiens
Zn2+
a specific inhibitor of mitochondrial isozyme
Mus musculus
Zn2+
a specific inhibitor of mitochondrial isozyme
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
Homo sapiens
5829
-
cytosol
cytosolic isozyme cAH
Mus musculus
5829
-
cytosol
IRP1 is a cytosolic isozyme devoid of labile Fe2+
Mus musculus
5829
-
cytosol
cytosolic isozyme cAH
Rattus norvegicus
5829
-
cytosol
IRP1 is a cytosolic isozyme devoid of labile Fe2+
Rattus norvegicus
5829
-
mitochondrion
mitochondrial isozyme mAH
Homo sapiens
5739
-
mitochondrion
mitochondrial isozyme mAH
Mus musculus
5739
-
mitochondrion
mitochondrial isozyme mAH
Rattus norvegicus
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
required
Homo sapiens
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 [3Fe–3S]2+ type, structure, and mechanism of activation of the enzyme by Fe2+, overview
Homo sapiens
Fe2+
required, binding structure in the [Fe-S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Mus musculus
Fe2+
required, binding structure in the [4Fe-4S] cluster, mechanism of activation of the enzyme by Fe2+, overview
Rattus norvegicus
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Rattus norvegicus
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
Rattus norvegicus
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
Mus musculus
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
?
-
-
-
additional information
Homo sapiens
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
Homo sapiens
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
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
mechanism controlling IRP1 activity at the level of its stability can be phosphorylation of Ser138, Ser138, Ser711, and flanking sequences are highly conserved
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
native IRP1 from liver
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
A-549 cell
-
Homo sapiens
-
brain
inactive isozyme mAH multimers occur in rat brain in a model of Huntington’s disease
Rattus norvegicus
-
heart
-
Homo sapiens
-
HEK-293 cell
-
Homo sapiens
-
hepatoma cell
-
Mus musculus
-
kidney
-
Homo sapiens
-
liver
-
Homo sapiens
-
liver
-
Mus musculus
-
liver
-
Rattus norvegicus
-
additional information
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
Homo sapiens
-
PC-12 cell
-
Rattus norvegicus
-
prostate gland
mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate
Homo sapiens
-
prostate gland cancer cell line
-
Homo sapiens
-
umbilical vein endothelial cell
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
696168
Rattus norvegicus
?
-
-
-
-
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
696168
Rattus norvegicus
?
-
-
-
-
additional information
role of aconitate hydratase and structurally similar iron-regulatory protein in maintenance of homeostasis of cell iron, overview. Regulation, overview
696168
Mus musculus
?
-
-
-
-
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
696168
Homo sapiens
?
-
-
-
-
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
696168
Homo sapiens
?
-
-
-
-
additional information
IRP shows RNA-binding activity, which is affected by some hormones and growth factors, e.g. thyroid, erythropoietin, and epidermal growth factor
696168
Rattus norvegicus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 95000-100000, IRP1, SDS-PAGE
Rattus norvegicus
More
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
Homo sapiens
Other publictions for EC 4.2.1.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749367
Ben-Menachem
Yeast aconitase mitochondrial ...
Saccharomyces cerevisiae
Sci. Rep.
8
5903
2018
-
-
-
-
-
-
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
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-
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-
-
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-
-
-
-
-
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-
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3
-
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-
-
-
-
-
-
-
-
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-
-
-
-
-
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-
-
-
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1
1
-
-
-
747131
Reddick
First biochemical characteriz ...
Bacillus subtilis 168, Bacillus subtilis
Biochemistry
56
5698-5711
2017
-
-
1
-
-
-
-
-
-
-
-
2
-
2
-
-
1
-
-
-
-
-
4
-
1
-
-
-
1
-
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1
-
-
-
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1
1
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-
-
-
-
-
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-
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2
-
-
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1
-
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4
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
747087
Fernandes
Lysine acetylation activates ...
Mus musculus
Biochemistry
54
4008-4018
2015
1
1
-
1
-
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
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Michta
Proteomic approach to reveal ...
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Identification, characterizati ...
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Degu
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Condo
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Terol
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704735
Gupta
Enhancement of over expression ...
Saccharomyces cerevisiae
J. Biosci. Bioeng.
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2009
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1
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1
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706437
Cantu
Oxidative inactivation of mito ...
Rattus norvegicus
PLoS ONE
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e7095
2009
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1
1
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677832
Mason
Endotoxin challenge reduces ac ...
Rattus norvegicus
Arch. Biochem. Biophys.
469
151-156
2008
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679348
Sanni
Effects of acclimation tempera ...
Crassostrea virginica
Comp. Biochem. Physiol. C
147
101-112
2008
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680267
Lall
Iron regulates L-cystine uptak ...
Canis lupus familiaris
Invest. Ophthalmol. Vis. Sci.
49
310-319
2008
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1
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1
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3
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684713
Lin
Suppression of metabolic defec ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Arch. Biochem. Biophys.
474
205-212
2008
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1
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1
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8
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690535
Wuebbeler
Novel pathway for catabolism o ...
Advenella mimigardefordensis, Advenella mimigardefordensis DPN7T
Appl. Environ. Microbiol.
74
4028-4035
2008
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1
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696162
Makeeva
Effects of lipoic acid on citr ...
Rattus norvegicus
Biochemistry (Moscow)
73
76-79
2008
1
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1
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4
2
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1
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696168
Matasova
Aconitate hydratase of mammals ...
Homo sapiens, Mus musculus, Rattus norvegicus
Biochemistry (Moscow)
73
957-964
2008
2
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3
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19
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8
4
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6
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7
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1
1
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14
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7
2
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22
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5
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1
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26
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7
3
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696416
Tsuchiya
Versatile architecture of a ba ...
Escherichia coli
Biochim. Biophys. Acta
1784
1847-1856
2008
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1
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4
1
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1
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696992
Goncalves
Deferiprone targets aconitase: ...
Homo sapiens
BMC Neurol.
8
20
2008
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1
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1
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1
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700705
Clore
Increased levels of reactive o ...
Zea mays
Plant Cell Environ.
31
144-158
2008
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1
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2
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1
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1
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-
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677458
Zhang
Activation of aconitase in mou ...
Homo sapiens, Mus musculus
Am. J. Physiol.
293
C1154-C1159
2007
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1
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4
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1
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4
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4
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678067
Arnaud
The iron-responsive element (I ...
Arabidopsis thaliana
Biochem. J.
405
523-531
2007
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-
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1
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1
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7
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678291
Unciuleac
In vitro activation of apo-aco ...
Azotobacter vinelandii
Biochemistry
46
6812-6821
2007
-
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1
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2
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1
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679969
Tortora
Mitochondrial aconitase reacti ...
Sus scrofa
Free Radic. Biol. Med.
42
1075-1088
2007
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1
1
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3
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1
1
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1
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1
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1
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1
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1
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1
1
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1
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680491
Banerjee
Iron-dependent RNA-binding act ...
Mycobacterium tuberculosis
J. Bacteriol.
189
4046-4052
2007
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-
-
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1
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1
2
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5
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1
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2
1
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1
1
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1
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1
2
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1
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2
1
-
-
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1
1
-
-
-
-
-
-
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681116
Cherkasov
Temperature-dependent effects ...
Crassostrea virginica
J. Exp. Biol.
210
46-55
2007
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1
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4
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2
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6
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1
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6
4
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681552
Crooks
Manganese targets m-aconitase ...
Rattus norvegicus
J. Neurosci. Res.
85
1797-1809
2007
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1
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1
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-
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-
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-
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-
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682389
Moeder
Aconitase plays a role in regu ...
Arabidopsis thaliana, Nicotiana benthamiana
Plant Mol. Biol.
63
273-287
2007
-
-
-
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2
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-
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7
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1
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2
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
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682550
Chen
Yeast aconitase binds and prov ...
Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
104
13738-13743
2007
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2
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3
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1
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2
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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663589
Ilangovan
Heat shock-induced attenuation ...
Rattus norvegicus
Am. J. Physiol.
290
C313-324
2006
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-
-
-
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1
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1
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1
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1
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-
-
-
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680182
Gupta
Co-expression of chaperonin Gr ...
Saccharomyces cerevisiae
Int. J. Biochem. Cell Biol.
38
1975-1985
2006
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1
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3
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3
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1
1
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1
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-
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680465
Serio
Bacillus subtilis aconitase is ...
Bacillus subtilis
J. Bacteriol.
188
6396-6405
2006
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1
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1
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1
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-
-
1
-
-
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-
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680466
Serio
Expression of yeast mitochondr ...
Saccharomyces cerevisiae
J. Bacteriol.
188
6406-6410
2006
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1
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1
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1
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1
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2
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-
-
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-
-
-
-
-
-
-
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680663
Lind
Of two cytosolic aconitases ex ...
Drosophila melanogaster
J. Biol. Chem.
281
18707-18714
2006
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1
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1
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1
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1
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7
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1
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3
1
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2
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1
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2
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2
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2
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-
-
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3
2
-
-
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-
-
-
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-
681626
Hunzinger
Comparative profiling of the m ...
Bos taurus
J. Proteome Res.
5
625-633
2006
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-
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1
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1
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1
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1
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1
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2
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1
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1
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1
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1
-
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-
1
-
-
-
-
-
-
-
2
-
-
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-
-
-
681745
Yarian
Aconitase is the main function ...
Mus musculus
Mech. Ageing Dev.
127
79-84
2006
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1
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4
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1
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1
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1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681864
Singh
Mitochondrial aconitase and ci ...
Homo sapiens
Mol. Cancer
5
14
2006
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1
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-
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2
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2
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5
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1
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5
-
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-
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-
-
-
-
-
-
-
-
-
-
682876
Dupuy
Crystal structure of human iro ...
Homo sapiens
Structure
14
129-139
2006
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1
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1
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Aconitase is the main functio ...
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Dupuy
Crystal structure of human ir ...
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Structure
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Dupuy
Crystallization and preliminar ...
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Acta Crystallogr. Sect. F
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IRP1 Ser-711 is a phosphorylat ...
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An iron regulatory-like protei ...
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666296
Regev-Rudzki
Yeast aconitase in two locatio ...
Saccharomyces cerevisiae
Mol. Biol. Cell
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2005
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Tang
Switching aconitase B between ...
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Andreeshcheva
Free radical oxidation and cat ...
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Iron dependence and zinc inhib ...
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Modulation of iron on mitochon ...
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Pitula
Selective inhibition of the ci ...
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Proc. Natl. Acad. Sci. USA
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Bulteau
Redox-dependent modulation of ...
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Cytosolic aconitase and ferrit ...
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Oxidation of propionate to pyr ...
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Tricarboxylic acid cycle aconi ...
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Sulfolobus aconitase, a regula ...
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650165
James
Mitochondrial aconitase modifi ...
Rattus norvegicus, Rattus norvegicus Male Fischer 344
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Eprintsev
Induction of aconitate hydrata ...
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Williams
E. coli aconitase B structure ...
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Baughn
A mitochondrial-like aconitase ...
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Exercise decreases cytosolic a ...
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Purification and characterizat ...
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Rzymkiewicz
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Cots
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Alen
Bacillus subtilis aconitase is ...
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The mechanism of aconitase:1.8 ...
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33808
Zheng
Manganese inhibits mitochondri ...
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Brain Res.
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1998
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33785
Gruer
Construction and properties of ...
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Microbiology
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1
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Costello
Zinc inhibition of mitochondri ...
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J. Biol. Chem.
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1997
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3
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33807
Lauble
The reaction of fluorocitrate ...
Bos taurus
Proc. Natl. Acad. Sci. USA
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1996
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Mitchell
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Biochem. J.
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2
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Bennett
Spectroscopic characterisation ...
Escherichia coli
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33809
De Bellis
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Purification and characterizat ...
Cucurbita sp.
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2
1
1
1
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33811
Kennedy
Purification and characterizat ...
Bos taurus
Proc. Natl. Acad. Sci. USA
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1992
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5
1
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5
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33814
Prodromou
The aconitase of Escherichia c ...
Escherichia coli
J. Gen. Microbiol.
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1991
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1
1
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33817
Baldwin
Purification and partial amino ...
Homo sapiens, Sus scrofa
Protein Seq. Data Anal.
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1991
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Zheng
Cloning and structural charact ...
Sus scrofa
J. Biol. Chem.
265
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1990
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33815
Cheung
Thiols protect the inhibition ...
Rattus norvegicus
Arch. Biochem. Biophys.
350
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1988
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33786
Brouquisse
Characterization of a cytosoli ...
Acer pseudoplatanus
Plant Physiol.
84
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1987
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33787
Dingman
Purification of aconitase from ...
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J. Bacteriol.
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33798
Robbins
Iron-sulfur cluster in aconita ...
Sus scrofa
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33788
Schloss
pH profiles and isotope effect ...
Bos taurus, Saccharomycopsis lipolytica
Biochemistry
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1984
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7
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33799
Ramsay
Molecular forms of aconitase a ...
Bos taurus
Biochem. J.
221
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33800
Ryden
Molecular weight of beef heart ...
Bos taurus
J. Biol. Chem.
259
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1984
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33789
Scholze
Studies on aconitase species f ...
Bos taurus, Saccharomyces cerevisiae, Sus scrofa
Biochim. Biophys. Acta
746
133-137
1983
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Robbins
Single crystals of the iron-su ...
Sus scrofa
J. Biol. Chem.
257
9061-9063
1982
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Hattori
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Inactivation by oxygen and sta ...
Escherichia coli
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33790
Treton
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Etude de quelques proprietes d ...
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Agric. Biol. Chem.
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1978
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Lee
Crystals of pig heart aconitas ...
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33791
Agrawal
Studies on two isozymes of aco ...
Bacillus cereus
Biochem. Biophys. Res. Commun.
70
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1976
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2
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33792
Agrawal
Studies on two isozymes of aco ...
Bacillus cereus, Bacillus cereus T
Biochem. Biophys. Res. Commun.
70
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1976
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4
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33795
Suzuki
The aconitase of yeast. IV. St ...
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799-804
1976
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33793
Agrawal
Studies on two isozymes of aco ...
Bacillus cereus, Bacillus cereus T
Biochem. Biophys. Res. Commun.
67
645-652
1975
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2
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Suzuki
The aconitase of yeast. II. Cr ...
Yarrowia lipolytica
J. Biochem.
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367-372
1975
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1
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33806
Suzuki
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Induction and stabilization of ...
Corynebacterium glutamicum, Corynebacterium glutamicum D-248, Streptomyces aureus, Trametes sanguinea, Xanthomonas campestris, Yarrowia lipolytica
Agric. Biol. Chem.
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2
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Gawron
Properties of pig heart aconit ...
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Biochem. J.
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717-722
1974
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-
33797
Guarriero-Bobyleva
Parallel partial purification ...
Rattus norvegicus
Eur. J. Biochem.
34
455-458
1973
-
-
-
-
-
-
-
4
2
-
-
-
-
1
-
-
1
-
-
1
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
1
-
1
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33803
Suzuki
-
Crystallization and reconstitu ...
Yarrowia lipolytica
Agric. Biol. Chem.
37
2211-2212
1973
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
33805
Kennedy
On pig heart aconitase ...
Sus scrofa
Biochem. Biophys. Res. Commun.
47
740-745
1972
-
-
-
-
-
-
-
-
-
1
1
-
-
2
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33784
Pickworth Glusker
-
Aconitase ...
Aspergillus niger, Bacillus subtilis, Bos taurus, Glycine max, Oryctolagus cuniculus, Rattus norvegicus, Rheum sp., Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium, Sinapis alba, Solanum tuberosum, Sus scrofa
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
413-439
1971
-
-
-
-
-
-
24
16
4
-
1
-
-
12
-
-
5
-
-
6
-
-
16
-
-
-
-
2
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
24
-
16
4
-
1
-
-
-
-
5
-
6
-
-
16
-
-
-
-
2
8
-
-
-
-
-
-
-
-
-