Information on EC 4.2.1.3 - aconitate hydratase

Word Map on EC 4.2.1.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.2.1.3
-
RECOMMENDED NAME
GeneOntology No.
aconitate hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Citrate = cis-aconitate + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citric acid cycle
-
-
Citrate cycle (TCA cycle)
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
acetic acid bacteria
-
-
-
Automatic Mining of ENzyme DAta
strain DPN7T (DSM 17166T, LMG 22922T)
TrEMBL
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
gene citB
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
strain D-248
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
Cucurbita sp.
3 isoforms: Aco I, Aco II and Aco III
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
strain JRG2387 and JRG3171, contains two major aconitases, AcnA and AcnB
-
-
Manually annotated by BRENDA team
strain W3350
SwissProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
isolate Pb01, gene Pbaco
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
quail
-
-
-
Automatic Mining of ENzyme DAta
-
1056776 A+, 1057233 A+, 1064896 A+, 1347244 A+, 1366517 A+, 1370008 A+, 1375717 A+, 1375744 A+, 1375783 A+, 1375801 A+, 1375853 A+, 1375864 A+, 1375876 A+, 1375922 A+, 1375926 A+, 1375943 A+, 1375948 A+, 1375953 A+, 1376010 A+, 1376013 A+, 1376025 A+, 1376072 A+, 1376139 A+, 1376159 A+, 1376167 A+, 1376169 A+, 1376181 A+, 2142131 A+, 2142134 A+, 2386913 A+, 2454570 A+, 2504932 A+, 2506096 A+, 2506117 A+, 2506216 A+, 2506236 A+, 2506247 A+, 2506308 A+, 2506314 A+, 2506364 A+, 2506385 A+, 2506418 A+, 696162 A+, 706437 A+, 729779 A+, 809593 A+, 809594 A+, 809596 A+, 809599 A+, 809685 A+, 1013942 A++, 1022798 A++, 1029364 A++, 1057124 A++, 1057126 A++, 1106049 A++, 1368250 A++, 1375503 A++, 1375679 A++, 1375680 A++, 1375691 A++, 1375692 A++, 1375693 A++, 1375694 A++, 1375695 A++, 1375704 A++, 1375716 A++, 1375719 A++, 1375723 A++, 1375726 A++, 1375740 A++, 1375745 A++, 1375751 A++, 1375757 A++, 1375771 A++, 1375786 A++, 1375814 A++, 1375821 A++, 1375832 A++, 1375846 A++, 1375847 A++, 1375907 A++, 1375986 A++, 1375987 A++, 1376046 A++, 2142054 A++, 2142056 A++, 2142071 A++, 2142074 A++, 2142077 A++, 2142081 A++, 2142123 A++, 2481053 A++, 2505940 A++, 2506071 A++, 2506078 A++, 2506156 A++, 2506159 A++, 2506169 A++, 2506179 A++, 2506192 A++, 2506198 A++, 2506201 A++, 2506221 A++, 2506230 A++, 2506261 A++, 2506280 A++, 2506363 A++, 33808 A++, 33810 A++, 677832 A++, 684976 A++, 692231 A++, 698948 A++, 778556 A++, 1268913 A++, 1370621 A++, 1375676 A++, 1375705 A++, 1375732 A++, 1375934 A++, 1375940 A++, 1376132 A++, 2142051 A++, 2142059 A++, 2142072 A++, 2142079 A++, 2142087 A++, 2142107 A++, 2142132 A++, 2274299 A++, 2322640 A++, 2506098 A++, 2506109 A++, 2506124 A++, 2506133 A++, 2506152 A++, 2506171 A++, 2506181 A++, 2506217 A++, 2506408 A++, 649566 A++, 748111 A++, 809533 A++, 809534 A++, 809542 A++, 809558 A++, 809574 A++, 809580 A++, 809588 A++, 809635 A++, 809640 A++, 809668 A++, 809673 A++, 809713 A++, 809730 A++, 809752 A++, 809553 A+++, 809704 A+++, 809767 A+++, 650272 A++++, 662693 A++++, 664485 A++++, 697220 A++++, 809557 A++++, 809611 A++++, 809620 A++++, 809631 A++++, 809632 A++++, 809649 A++++, 809660 A++++, 809672 A++++, 809677 A++++, 809731 A++++, 809740 A++++, 809741 A++++, 809742 A++++, 809753 A++++
-
-
Automatic Mining of ENzyme DAta
Rattus norvegicus Male Fischer 344
strain Male Fischer 344
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
strain Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rheum sp.
i.e. rhubarb
-
-
Manually annotated by BRENDA team
strain MMY011, gene aco1
-
-
Manually annotated by BRENDA team
Saccharomycopsis lipolytica
-
-
-
Manually annotated by BRENDA team
salmon
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
snake
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
IFO 12371
-
-
Manually annotated by BRENDA team
Streptomyces viridochromogenes strain Tu494
strain Tu494
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
IFO 4923
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
yeasts
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3S)-2-methylisocitrate
(Z)-2-methylaconitate + H2O
show the reaction diagram
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
show the reaction diagram
alpha-methyl-cis-aconitate
alpha-methylisocitrate
show the reaction diagram
cis-aconitate
citrate
show the reaction diagram
cis-aconitate
isocitrate
show the reaction diagram
cis-aconitate + H2O
?
show the reaction diagram
cis-aconitate + H2O
citrate
show the reaction diagram
cis-aconitate + H2O
isocitrate
show the reaction diagram
citrate
cis-aconitate
show the reaction diagram
citrate
cis-aconitate + H2O
show the reaction diagram
citrate
isocitrate
show the reaction diagram
isocitrate
?
show the reaction diagram
isocitrate
cis-aconitate
show the reaction diagram
isocitrate
cis-aconitate + H2O
show the reaction diagram
isocitrate
citrate
show the reaction diagram
threo-D-alpha-methylisocitrate
?
show the reaction diagram
Saccharomycopsis lipolytica
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(Z)-2-methylaconitate + H2O
(2R,3S)-2-methylisocitrate
show the reaction diagram
cis-aconitate + H2O
isocitrate
show the reaction diagram
citrate
cis-aconitate + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn
-
an X-ray fluorescence measurement performed on a gold-derivative crystal shows the unexpected presence of zinc, in addition to gold and iron
[4Fe-4S] center
-
acon harbors a single unligated iron atom in its [4Fe-4S], enzyme is in this respect unique in mitochondria
additional information
IRP1 is a cytosolic isozyme devoid of labile Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,2,3,4-tetracarboxycyclopentane
-
competitive
1,2,3-tricarboxycyclopentene-1
-
competitive
1,3,5-tricarboxypentane
-
competitive
2,2'-dipyridyl
-
noncompetitive
4-hydroxy-2-oxoglutarate
-
competitive
adipate
Saccharomycopsis lipolytica
-
-
ADP
-
inhibition at levels well above its physiological concentration
alpha-picolinic acid
-
noncompetitive
citramalate
citrate
D-glucose 1-phosphate
-
-
D-glucose 6-phosphate
-
-
deferiprone
-
the loss of aconitase activity observed in cells should be ascribed to the chelation of available iron rather than to a direct effect of the chelator on the iron-sulfur clusters of the enzyme
ethyl picolinate
-
isoenzyme is inhibited, isoenzyme I is less or not sensitive
fluoroacetate
Saccharomycopsis lipolytica
-
-
Fluorocitrate
fructose-6-phosphate
fumarate
-
-
GDP
-
inhibition at levels well above its physiological concentration
glyoxylate
-
-
hydrogen peroxide
-
inhibits enzyme activity in cell-free extracts
indomethacin
-
a non-steroidal anti-inflammatory drug, carbonylation of aconitase and release of iron along with the loss of activity in vivo after indomethacin treatment, activation of mitochondrial death pathway by indomethacin, overview
Maleate
Saccharomycopsis lipolytica
-
-
Mn2+
-
inhibition of enzyme, resulting in up to 90% increase in intracellular citrate. Mitochondrial isoform is significantly more sensitive to Mn2+ than cytosolic isoform. Inhibition leads to conversion of enzyme to iron regulatory protein IRP 1 and increases the abundance of IRP2, leading to reduced H-ferritin expression, inreased transferrin receptor expression, and increased uptake of transferrin. IRP2 has a dominant role in Mn2+-induced alteration of iron homeostasis over aconitase/IRP1
nitric oxide
-
brief exposure leads to a reversible inhibition competitive with isocitrate. subsequently, an irreversible inactivation is observed
nitrosoglutathione
-
irreversible inactivation both in presence and absence of substrate
oxaloacetate
Oxalomalate
oxalomalic acid
-
inhibition of aconitase activity, leading to inhibition of L-glutamate production, L-cystine uptake, and decrease in glutathione concentration in lens epithelial cells and retinal pigment epithelial cells
oxalosuccinate
p-hydroxymercuribenzoate
-
-
peroxynitrite
Phthalic acid
-
competitive
pyromellitic acid
-
competitive
Quinaldic acid
S(1,1,2,2)-tetrafluoroethyl-L-cysteine
inhibition of renal aconitase activity both in vivo and in vitro is a functional consequence of difluorothioamidyl-L-lysine formation by S(1,1,2,2)-tetrafluoroethyl-L-cysteine
Sodium mersalyl
-
-
succinate
-
-
superoxide anion radical
threo-Ls-isocitrate
-
competitive
-
trans-aconitate
tricarballylate
trimellitic acid
-
competitive
trimesic acid
-
competitive
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
Fe4-S4 cluster
ferric ammonium citrate
-
increases activity and gene expression
Hemin
-
increases activity and gene expression
lipoic acid
-
causes an increase in cardiac enzyme activity at doses of 35 and 70 mg/kg of 1.3 and 2.4fold in the animals
menadione sodium bisulfite
-
causes a modest activation of IRP-1 to bind to iron resonsive elements within 15-30 min. Menadione-induced oxidative stress leads to post-translational inactivation of both genetic and enzymatic functions of IRP-1 by a mechanism that lies beyond the classical Fe-S cluster switch and exerts multiple effects on cellular iron metabolism
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
(2R,3S)-2-methylisocitrate
-
0.0035 - 0.2
cis-aconitate
0.12 - 11
citrate
0.012 - 3.33
isocitrate
0.0089 - 0.158
methyl-cis-aconitate
-
0.032 - 0.268
methylisocitrate
additional information
additional information
-