Any feedback?
Information on EC 4.2.1.3 - aconitate hydratase and Organism(s) Escherichia coli and UniProt Accession P25516
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: Escherichia coli
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
AcnB
aconitase
aconitase B
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
-
-
-
-
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
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
?
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
additional information
?
-
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
?
-
-
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
-
-
?
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
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
enzyme is involved in pathway of oxidation of propionate to pyruvate
-
r
cis-aconitate + H2O
isocitrate
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
citrate
cis-aconitate + H2O
aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle
-
-
r
additional information
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Fe
-
a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed
Fe2+
the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview
Iron
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
two values are obtained for KM-value with isocitrate as substrate, depending on substrate concentration
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
enzyme form AcnA and AcnB, the maximal activity of AcnB is nearly 2fold the activity of AcnA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 5.0: about 75% of maximal activity, pH 10.0: about 60% of maximal activity, AcnA
6 - 9
-
pH 6.0: about 55% of maximal activity, pH 9.0: about 20% of maximal activity, AcnB
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
structural modeling, homo-oligomerization of AcnA yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview
homodimer
homodimer
structural analysis by X-ray scattering and modelling of wild-type and mutant enzymes, overview
homodimer
structural modeling, homo-oligomerization of AcnB yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
a postranslational activation-inactivation mechanism might be operating
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of a fusion protein of aconitase B and isocitrate dehydrogenase, ICDH and AcnB, i.e. ICDH-AcnB, structure determination of ICDH-AcnB, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
more than 50% of total aconitase activity is lost when cell-free extracts are prepared under air by a French press, by osmotic rupture of spheroplasts or by sonic treatment
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzymes from Escherichia coli strain BL21(DE3) by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AcnA, overexpression of the His-tagged protein in an ASKA library, i.e. the 'a complete set of Escherichia coli K-12 ORF archive library
AcnB domain 5-4 polypeptide is expressed in Escherichia coli as a GST-AcnB5-4 fusion protein
-
gene acnB, expression of wild-type enzyme and the fusion protein ICDH-AcnB in Escherichia coli strain BL21 (DE3)
gene ACnB, overexpression of the His-tagged protein in an ASKA library
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gruer, M.J.; Bradbury, A.J.; Guest, J.R.
Construction and properties of aconitase mutants of Escherichia coli
Microbiology
143
1837-1846
1997
Escherichia coli
Hattori, Y.; Hino, S.
Inactivation by oxygen and stabilization by fluorocitrate of aconitase from Escherichia coli
J. Gen. Appl. Microbiol.
27
33-41
1981
Escherichia coli
-
Bennett, B.; Gruer, M.J.; Guest, J.R.; Thomson, A.J.
Spectroscopic characterisation of an aconitase (AcnA) of Escherichia coli
Eur. J. Biochem.
233
317-326
1995
Escherichia coli
Prodromou, C.; Haynes, M.J.; Guest, J.R.
The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn)
J. Gen. Microbiol.
137
2505-2515
1991
Escherichia coli
Brock, M.; Maerker, C.; Schuetz, A.; Voelker, U.; Buckel, W.
Oxidation of propionate to pyruvate in Escherichia coli: Involvement of methylcitrate dehydratase and aconitase
Eur. J. Biochem.
269
6184-6194
2002
Escherichia coli (P36683), Escherichia coli, Escherichia coli W3350 (P36683)
Jordan, P.A.; Tang, Y.; Bradbury, A.J.; Thomson, A.J.; Guest, J.R.
Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)
Biochem. J.
344
739-746
1999
Escherichia coli, Escherichia coli JRG2387
-
Williams, C.H.; Stillman, T.J.; Barynin, V.V.; Sedelnikova, S.E.; Tang, Y.; Green, J.; Guest, J.R.; Artymiuk, P.J.
E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition
Nat. Struct. Biol.
9
447-452
2002
Escherichia coli (P36683), Escherichia coli
Tang, Y.; Guest, J.R.; Artymiuk, P.J.; Green, J.
Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation
Mol. Microbiol.
56
1149-1158
2005
Escherichia coli
Tsuchiya, D.; Shimizu, N.; Tomita, M.
Cooperativity of two active sites in bacterial homodimeric aconitases
Biochem. Biophys. Res. Commun.
379
485-488
2009
Escherichia coli (P25516), Escherichia coli (P36683), Escherichia coli
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
