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Information on EC 4.2.1.3 - aconitate hydratase and Organism(s) Sus scrofa and UniProt Accession P16276

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.3 aconitate hydratase
IUBMB Comments
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds.
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Sus scrofa
UNIPROT: P16276
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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citrate
=
cis-aconitate
+
H2O
=
+
Synonyms
aconitase, iron regulatory protein, irp-1, ire-bp, macon, iron regulatory protein 1, aconitate hydratase, cytoplasmic aconitase, aconitase a, c-aconitase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
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 hide
9024-25-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-aconitate + H2O
citrate
show the reaction diagram
-
-
-
r
cis-aconitate + H2O
isocitrate
show the reaction diagram
-
-
-
r
citrate
cis-aconitate + H2O
show the reaction diagram
citrate
isocitrate
show the reaction diagram
-
-
-
r
isocitrate
cis-aconitate + H2O
show the reaction diagram
-
-
-
r
isocitrate
citrate
show the reaction diagram
-
-
-
r
additional information
?
-
the mechanism requires that the intermediate product cis-aconitate, flip over by 180° about the Calpha-Cbeta double bond
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
in the S642A:citrate complex citrate is directly coordinated to Fe4 of the [4Fe-4S] cluster via Cbeta carboxyl and hydroxyl oxygen atoms
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3,4-tetracarboxycyclopentane
-
competitive
1,2,3-tricarboxycyclopentene-1
-
competitive
1,3,5-tricarboxypentane
-
competitive
4-hydroxy-2-oxoglutarate
-
competitive
Fluorocitrate
-
linear competitive
nitric oxide
-
brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed
nitrosoglutathione
-
irreversible inactivation both in presence and absence of substrate
oxaloacetate
-
parabolic noncompetitive
Oxalomalate
-
competitive
p-hydroxymercuribenzoate
-
-
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
Phthalic acid
-
competitive
pyromellitic acid
-
competitive
trans-aconitate
-
linear competitive
tricarballylate
-
-
trimellitic acid
-
competitive
trimesic acid
-
competitive
Zn2+
-
inhibition of mitochondrial isoenzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
nitric oxide
-
reversible inhibition after brief exposure
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
glycerophosphate buffer
7.7
-
phosphate buffer
8.1
-
N-ethylmorpholine buffer
8.6
-
veronal acetate buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACON_PIG
781
0
85761
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
gel filtration
67000
-
gel filtration
79000
-
ultracentrifugation
82754
-
x * 82754, calculation from nucleotide sequence
89000
-
equilibrium sedimentation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 82754, calculation from nucleotide sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the porcine heart enzyme is synthesized as a precursor containing a mitochondrial targeting sequence of 27 amino acid residues which is cleaved to yield a mature enzyme of 754 amino acids
side-chain modification
-
traces of carbohydrate of less than 1%
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution crystal structure of the S642A:citrate complex of mitochondrial aconitase
computational modeling of aconitase inactivation by superoxide and nitric oxide
-
crystallographic evidence for a three-iron center
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme frozen after dialysis against 0.05 M Tris-HCl, pH 7.5, complete inactivation after 10 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pickworth Glusker, J.
Aconitase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
413-439
1971
Aspergillus niger, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Glycine max, Rattus norvegicus, Rheum sp., Salmonella enterica subsp. enterica serovar Typhimurium, Sinapis alba, Solanum tuberosum, Sus scrofa
-
Manually annotated by BRENDA team
Scholze, H.
Studies on aconitase species from Saccharomyces cerevisiae, porcine and bovine heart, obtained by a modified isolation method
Biochim. Biophys. Acta
746
133-137
1983
Bos taurus, Saccharomyces cerevisiae, Sus scrofa
Manually annotated by BRENDA team
Gawron, O.; Kennedy, M.C.; Rauner, R.A.
Properties of pig heart aconitase
Biochem. J.
143
717-722
1974
Yarrowia lipolytica, Sus scrofa
Manually annotated by BRENDA team
Robbins, A.H.; Stout, C.D.
Iron-sulfur cluster in aconitase. Crystallographic evidence for a three-iron center
J. Biol. Chem.
260
2328-2333
1985
Sus scrofa
Manually annotated by BRENDA team
Robbins, A.H.; Stout, C.D.; Piszkiewicz, D.; Gawron, O.; Yoo, C.S.; Wang, B.C.; Sax, M.
Single crystals of the iron-sulfur enzyme aconitase
J. Biol. Chem.
257
9061-9063
1982
Sus scrofa
Manually annotated by BRENDA team
Lee, J.; Chang, S.C.; Hahm, K.; Glaid, A.J.; Gawron, O.; Wang, B.C.; Yoo, C.S.; Sax, M.
Crystals of pig heart aconitase
J. Mol. Biol.
112
531-534
1977
Sus scrofa
Manually annotated by BRENDA team
Kennedy, S.C.; Rauner, R.; Gawron, O.
On pig heart aconitase
Biochem. Biophys. Res. Commun.
47
740-745
1972
Sus scrofa
Manually annotated by BRENDA team
Costello, L.C.; Liu, Y.; Franklin, R.B.; Kennedy, M.C.
Zinc inhibition of mitochondrial aconitase and its importance in citrate metabolism of prostate epithelial cells
J. Biol. Chem.
272
28875-28881
1997
Bos taurus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Zheng, L.; Andrews, P.C.; Hermodson, M.A.; Dixon, J.E.; Zalkin, H.
Cloning and structural characterization of porcine heart aconitase
J. Biol. Chem.
265
2814-2821
1990
Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lloyd, S.J.; Lauble, H.; Prasad, G.S.; Stout, C.D.
The mechanism of aconitase:1.8 A resolution crystal structure of the S642A:citrate complex
Protein Sci.
8
2655-2662
1999
Sus scrofa (P16276)
Manually annotated by BRENDA team
Tortora, V.; Quijano, C.; Freeman, B.; Radi, R.; Castro, L.
Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation
Free Radic. Biol. Med.
42
1075-1088
2007
Sus scrofa
Manually annotated by BRENDA team