Any feedback?
Information on EC 4.2.1.3 - aconitate hydratase and Organism(s) Homo sapiens and UniProt Accession P21399
for references in articles please use BRENDA:EC4.2.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.1.3 aconitate hydrataseIUBMB Comments
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
Specify your search results
Word Map
- 4.2.1.3
-
iron-sulfur
- transferrin
-
tricarboxylic
- dismutase
- fe-s
- succinate
- tca
- malate
-
citric
- cardiac
-
rna-binding
- neurodegenerative
- frataxin
-
krebs
- fumarase
- friedreich
- heme
- ataxia
- parkinson
- overload
-
iron-dependent
- alpha-ketoglutarate
-
stem-loops
- fluorocitrate
-
bioenergetics
-
ferroportin
-
county
- hepcidin
- peroxynitrite
- mnsod
- fluoroacetate
-
georgia
-
cluster-containing
-
iron-deficient
- iscu
-
iron-replete
-
iron-induced
-
iron-mediated
- alabama
-
kennedy
-
itaconic
-
ferrochelatase
- cubane
-
desulfurase
-
nadp-isocitrate
-
rna-protein
-
iron-related
-
soxrs
- l-ferritin
- isopropylmalate
- medicine
- environmental protection
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aconitase, iron regulatory protein, irp-1, ire-bp, macon, iron regulatory protein 1, aconitate hydratase, cytoplasmic aconitase, aconitase a, c-aconitase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aco1
aconitase
Aconitate hydratase
cis-aconitase
-
-
-
-
citrate hydro-lyase
-
-
-
-
Ferritin repressor protein
-
-
-
-
hydratase, aconitate
-
-
-
-
IP210
-
-
-
-
IRE-BP
-
-
-
-
Iron regulatory protein
-
-
-
-
iron-responsive element binding protein
-
-
-
-
IRP
-
-
-
-
IRP1
Major iron-containing protein
-
-
-
-
MICP
-
-
-
-
aconitase
-
-
-
-
Aconitate hydratase
-
-
-
-
IRP1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
citrate(isocitrate) hydro-lyase (cis-aconitate-forming)
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
CAS REGISTRY NUMBER
COMMENTARY
9024-25-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
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. 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, Parkinsons and Alzheimers 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, Parkinsons and Alzheimers 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 Friedreichs Ataxia (FRDA)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
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. 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, Parkinsons and Alzheimers 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, Parkinsons and Alzheimers 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 Friedreichs Ataxia (FRDA)
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
-
HOSCN induces rapid and efficient release of iron from aconitase. Blocking the [4Fe-4 S] cluster inhibits HOSCN-mediated inactivation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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
Fe
Fe2+
Zn
-
an X-ray fluorescence measurement performed on a gold-derivative crystal shows the unexpected presence of zinc, in addition to gold and iron
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 [3Fe3S]2+ type, structure, and mechanism of activation of the enzyme by Fe2+, overview
Fe2+
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
Fe
iron restriction reproducibly causes 60% decreases in both mitochondrial and cytosolic aconitase activities in erythroid samples
Fe2+
-
required, the enzyme contains iron-sulfur clusters. Chelating mitochondrial free iron in various cell systems causes loss of aconitase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
citrate
citrate accumulation under enzyme inhibition restricts the formation of hydroxyl radical in the Fenton reaction through the binding of iron ions, and it thus protects the enzyme from inactivation
Fluorocitrate
active site aconitase inhibitor blocks erythroid differentiation in a manner similar to iron deprivation
Oxalomalate
inhibition of the enzyme by oxalomalate reduces glutamate secretion and eliminates the effect of iron ions on the latter
peroxynitrite
inactivation due to the release of iron from the Fe-S cluster, other nitric oxide sources decrease the activity of the mitochondrial isozyme
trans-aconitate
a competitive inhibitor of the enzyme with respect to cis-aconitate and a non-competitive inhibitor with respect to citrate and isocitrate
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
Fluorocitrate
active site aconitase inhibitor blocks erythroid differentiation in a manner similar to iron deprivation
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
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
purified human CD34+ progenitors derived from granulocyte-colony stimulating factor mobilized peripheral blood cells of normal donors
mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate
purified human CD34+ progenitors derived from granulocyte-colony stimulating factor mobilized peripheral blood cells of normal donors
mitochondrial isozyme plays the key role in the bioenergetic theory of malignant transformation of the prostate
-
muscle exercise does not affect aconitase activity despite increased oxidative stress
additional information
additional information
-
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
additional information
isozymes cAH and mAH are present in all tissues, and are most active in the heart, kidney, and liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cytosolic isozyme cAH, IRP1 is a cytosolic isozyme devoid of labile Fe2+
-
mitochondrial aconitase activity represents up to 80% of the total aconitase activity in skin fibroblasts
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
iron restriction suppresses mitochondrial and cytosolic aconitase activity in erythroid but not granulocytic or megakaryocytic progenitors. The mechanism for aconitase regulation of erythropoiesis most likely involves both production of metabolic intermediates as well as modulation of erythropoietin signaling
physiological function
iron restriction suppresses mitochondrial and cytosolic aconitase activity in erythroid but not granulocytic or megakaryocytic progenitors. The mechanism for aconitase regulation of erythropoiesis most likely involves both production of metabolic intermediates as well as modulation of erythropoietin signaling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACOHC_HUMAN
889
0
98399
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
additional information
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
additional information
-
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
additional information
depending on the conditions, the enzyme can associate to dimer, trimer, and tetramer forms, followed by the loss of enzyme activity
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
mechanism controlling IRP1 activity at the level of its stability can be phosphorylation of Ser138, Ser138, Ser711, and flanking sequences are highly conserved
phosphoprotein
phosphoprotein
-
S711 of IRP1 is phosphorylated by proteinkinase C in vitro and in vivo in human HEK cells. Aconitase activity of the S711 phosphomimetic mutants is preferentially inhibited in the citrate mode of aconitase function. The substitution of phosphomimetic amino acids for S711 fails to affect the RNA-binding affinity of IRP1
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aconitase form of bifunctional enzyme, evaluation of model for iron regulatory form of enzyme and its binding to iron-responsive elements
structure of human IRP1 in its aconitase form and tentative model of an IRP1-iron-responsive element complex
recombinant enzyme, hanging-drop vapour-diffusion method. An X-ray fluorescence measurement performed on a gold-derivative crystal shows the unexpected presence of zinc, in addition to gold and iron
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S711A
-
citrate-to-isocitrate aconitase activity is about 70% of the wild-type activity, isocitrate-to-cis-aconitate activity is about 90% of wild-type activity
S711D
-
no citrate-to-isocitrate aconitase activity, isocitrate-to-cis-aconitate activity is identical to wild-type activity
S711E
S711T
-
citrate-to-isocitrate aconitase activity is about 60% of the wild-type activity, isocitrate-to-cis-aconitate activity is about 60% of wild-type activity
additional information
S711E
-
45% of the capacity to catalyze conversion of cis-aconitase into isocitrate, completely fails to bind RNA and to generate isocitrate from citrate
S711E
-
citrate-to-isocitrate aconitase activity is about 10% of the wild-type activity, isocitrate-to-cis-aconitate activity is about 20% of wild-type activity
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
mitochondrial enzyme is present in the glandular epithelium of normal glands, hyperplastic glands, adenocarcinomatous glands, and prostatic intraepithelial neoplastic fold. There is no difference in enzyme levels between malignant and non-malignant tissues
medicine
-
enzyme inhibition, e.g. by deferiprone, is helpful in Friedreich's ataxia treatment
medicine
-
it is shown that the cytosolic aconitase defect and consequent IRP1 activation occurring in Friedreich's Ataxia (FRDA) cells are reversed by the action of extramitochondrial frataxin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baldwin, G.S.; Seet, K.L.; Callaghan, J.; Toncich, G.; Toh, B.H.; Moritz, R.L.; Rubira, M.R.; Simpson, R.
Purification and partial amino acid sequence of human aconitase
Protein Seq. Data Anal.
4
63-67
1991
Homo sapiens, Sus scrofa
Rzymkiewicz, D.M.; Reddan, J.R.; Andley, U.P.
Induction of heme oxygenase-1 modulates cis-aconitase activity in lens epithelial cells
Biochem. Biophys. Res. Commun.
270
324-328
2000
Homo sapiens
Dupuy, J.; Darnault, C.; Brazzolotto, X.; Kuehn, L.C.; Moulis, J.M.; Volbeda, A.; Fontecilla-Camps, J.C.
Crystallization and preliminary x-ray diffraction data for the aconitase form of human iron-regulatory protein 1
Acta Crystallogr. Sect. F
F61
482-485
2005
Homo sapiens
Fillebeen, C.; Caltagirone, A.; Martelli, A.; Moulis, J.M.; Pantopoulos, K.
IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities
Biochem. J.
388
143-150
2005
Homo sapiens
Juang, H.H.
Modulation of iron on mitochondrial aconitase expression in human prostatic carcinoma cells
Mol. Cell. Biochem.
265
185-194
2004
Homo sapiens
Pitula, J.S.; Deck, K.M.; Clarke, S.L.; Anderson, S.A.; Vasanthakumar, A.; Eisenstein, R.S.
Selective inhibition of the citrate-to-isocitrate reaction of cytosolic aconitase by phosphomimetic mutation of serine-711
Proc. Natl. Acad. Sci. USA
101
10907-10912
2004
Homo sapiens
Zhang, S.; Sandstroem, M.E.; Lanner, J.T.; Thorell, A.; Westerblad, H.; Katz, A.
Activation of aconitase in mouse fast-twitch skeletal muscle during contraction-mediated oxidative stress
Am. J. Physiol.
293
C1154-C1159
2007
Homo sapiens, Mus musculus
Singh, K.K.; Desouki, M.M.; Franklin, R.B.; Costello, L.C.
Mitochondrial aconitase and citrate metabolism in malignant and nonmalignant human prostate tissues
Mol. Cancer
5
14
2006
Homo sapiens
Dupuy, J.; Volbeda, A.; Carpentier, P.; Darnault, C.; Moulis, J.; Fontecilla-Camps, J.C.
Crystal structure of human iron regulatory protein 1 as cytosolic aconitase
Structure
14
129-139
2006
Homo sapiens (P21399), Homo sapiens
Matasova, L.V.; Popova, T.N.
Aconitate hydratase of mammals under oxidative stress
Biochemistry (Moscow)
73
957-964
2008
Homo sapiens, Homo sapiens (P21399), Mus musculus, Mus musculus (P28271), Rattus norvegicus, Rattus norvegicus (Q63270)
Goncalves, S.; Paupe, V.; Dassa, E.P.; Rustin, P.
Deferiprone targets aconitase: implication for Friedreich's ataxia treatment
BMC Neurol.
8
20
2008
Homo sapiens
Bullock, G.C.; Delehanty, L.L.; Talbot, A.L.; Gonias, S.L.; Tong, W.H.; Rouault, T.A.; Dewar, B.; Macdonald, J.M.; Chruma, J.J.; Goldfarb, A.N.
Iron control of erythroid development by a novel aconitase-associated regulatory pathway
Blood
116
97-108
2010
Homo sapiens (P21399), Homo sapiens (Q99798), Homo sapiens
Condo, I.; Malisan, F.; Guccini, I.; Serio, D.; Rufini, A.; Testi, R.
Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin
Hum. Mol. Genet.
19
1221-1229
2010
Homo sapiens
Talib, J.; Cook, N.; Pattison, D.; Davies, M.
Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants
Free Radic. Biol. Med.
75 Suppl 1
S27-S28
2014
Homo sapiens
EXTERNAL LINKS (specific for EC-Number 4.2.1.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
