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4.2.1.3: aconitate hydratase

This is an abbreviated version!
For detailed information about aconitate hydratase, go to the full flat file.

Word Map on EC 4.2.1.3

Reaction

citrate
=
cis-aconitate
+
H2O

Synonyms

Acn, AcnA, AcnA3, AcnB, ACO, Aco1, Aco2, Aco3, ACO4, acon, aconitase, aconitase 2, aconitase A, aconitase B, aconitase/2-methylaconitate hydratase, Aconitate hydratase, AH, c-acon, c-aconitase, CAA, cis-aconitase, citB, citrate hydro-lyase, cytoplasmic aconitase, cytoplasmic aconitase/iron regulatory protein 1 homolog, EC 4.2.1.4, Ferritin repressor protein, hydratase, aconitate, IP210, IRE-BP, Iron regulatory protein, iron regulatory protein 1, iron regulatory-like protein, iron-regulatory protein 1, iron-responsive element binding protein, IRP, IRP-1, IRP1, mACON, Major iron-containing protein, MICP, More, PfIRPa, SPBP4H10.15

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.3 aconitate hydratase

Engineering

Engineering on EC 4.2.1.3 - aconitate hydratase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C450S
-
mutant is enzymatically inactive, glutamate auxotroph and accumulates citrate. Mutant strain exhibits overexpression of the citB promoter and accumulates high levels of aconitase protein. Mutant strain exhibits increased levels of citrate synthase protein. Mutant enzyme does not bind to the citrate synthase 5' leader RNA in vitro
C517A
-
enzymatically inactive mutant enzyme that still binds iron responsive elements
R740E/Q744E/F661L/I809T/V852A
-
sixfold increase in specific activity compared to wild-type. Mutant strain is defective in sporulation, affecting the expression of deltaK-dependent genes. Accumulation of transcriptional activator GerE mRNa and protein is delayed in the mutant
R741E
-
mutant is designed to be defective in RNA binding. Mutant strain is glutamate prototroph and accumulates citrate. Mutant strain exhibits overexpression of the citB promoter and accumulates high levels of aconitase protein. Mutant strain exhibits increased levels of citrate synthase protein. Mutant enzyme does not bind to the citrate synthase 5' leader RNA in vitro
R741E/Q745E
C459S
-
catalytically inactive mutant without its [4Fe-4S]-cluster. Mitochondrial morphological defects as a consequence of acon inactivation depend on its [4Fe-4S] cluster
S677A
-
catalytically inactive mutant
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
C381A
-
site-directed mutagenesis
C447A
-
site-directed mutagenesis
H170A
-
site-directed mutagenesis
C381A
-
site-directed mutagenesis
-
C447A
-
site-directed mutagenesis
-
H170A
-
site-directed mutagenesis
-
C538A
-
mutation of cysteine residue involved in the coordination of the [4Fe-4S] cluster, mutant shows no catalytic activity. Mutant displays a lower affinity for the IRE sequence than the wild-type aconitase as shown in gel shift assays
DELTA125-129
-
mutant shows lower activity compared to wild-type
R763E/Q767E
-
mutant shows no enzymatic activity, mutant does not bind at all to IRE-like structure as shown in gel shift assays
additional information