Information on EC 3.1.2.29 - fluoroacetyl-CoA thioesterase

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

EC NUMBER
COMMENTARY hide
3.1.2.29
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RECOMMENDED NAME
GeneOntology No.
fluoroacetyl-CoA thioesterase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
fluoroacetyl-CoA + H2O = fluoroacetate + CoA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
fluoroacetyl-CoA hydrolase
Fluoroacetate is extremely toxic. It reacts with CoA to form fluoroacetyl-CoA, which substitutes for acetyl CoA and reacts with EC 2.3.3.1 (citrate synthase) to produce fluorocitrate, a metabolite of which binds very tightly to EC 4.2.1.3 (aconitase) and halts the TCA cycle. This enzyme hydrolyses fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance on the organisms that produce it. It has been described in the poisonous plant Dichapetalum cymosum and the bacterium Streptomyces cattleya, both of which are fluoroacetate producers.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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presence of enzyme protects its host from fluoroacetate toxicity in vivo
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
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poor substrate
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?
fluoroacetyl-CoA + H2O
fluoroacetate + CoA
show the reaction diagram
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fluoroacetyl-CoA
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substrate inhibition of mutants T42S and E50A above 0.012 and 0.019 mM, respectively; T42S mutant protein: substrate inhibition observed above 0.012 mM, E50A mutant protein: substrate inhibition observed above 0.019 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061 - 3
acetyl-CoA
0.001 - 1.5
Fluoroacetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.1
acetyl-CoA
0.003 - 390
Fluoroacetyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.16
acetyl-CoA
0.15 - 50000
Fluoroacetyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0295
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crude mitochondrial extract, pH not specified in the publication, temperature not specified in the publication
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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crystal structure analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FlK forms a dimer, in which each subunit adopts a hot dog fold as observed for type II thioesterases. Unlike other type II thioesterases, FlK employs a catalytic triad composed of Thr42, His76, and a water molecule; sitting drop method, polyethylene glycol monomethyl ether 2000
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wild-type in complex with fluoroacetate, mutant F36A both alone and as product complex, to 2.3 A, 2.3 A, and 2.0 A resolution, respectively
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Co2+), His tag removed, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli Rosetta (DE3)pLysS
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E50A
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disturbed protein folding. 37% of wild-type catalytic efficiency, substrate inhibition above 0.019 mM; putative member of the catalytic triad
E50Q
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about 5000fold decrease in catalytic efficiency
F33A
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about 1000fold decrease in catalytic efficiency
F36A
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about 100fold decrease in catalytic efficiency
H76D
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insoluble protein; putative member of the catalytic triad, completely insoluble
L26A
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about 1000fold decrease in catalytic efficiency
T42C
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about 1000fold decrease in catalytic efficiency
V23A
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about 100fold decrease in catalytic efficiency
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