Information on EC 1.97.1.8 - tetrachloroethene reductive dehalogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.97.1.8
-
RECOMMENDED NAME
GeneOntology No.
tetrachloroethene reductive dehalogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dechlorination
-
-
reductive dechlorination
-
dehalogenation
-
-
reductive dehalogenation
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrachloroethene degradation
-
-
Chloroalkane and chloroalkene degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
acceptor:trichloroethene oxidoreductase (chlorinating)
This enzyme allows the common pollutant tetrachloroethene to support bacterial growth and is responsible for disposal of a number of chlorinated hydrocarbons by this organism. The reaction occurs in the reverse direction. The enzyme also reduces trichloroethene to dichloroethene. Although the physiological reductant is unknown, the supply of reductant in some organisms is via reduced menaquinone, itself formed from molecular hydrogen, via EC 1.12.5.1 (hydrogen:quinone oxidoreductase). The enzyme contains a corrinoid and two iron-sulfur clusters. Methyl viologen can act as electron donor.
CAS REGISTRY NUMBER
COMMENTARY hide
163913-51-7
-
175780-16-2
deleted registry number
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clostridium bifermentans
DPH-1
-
-
Manually annotated by BRENDA team
Dehalococcoides sp.
-
UniProt
Manually annotated by BRENDA team
strain TCE1
-
-
Manually annotated by BRENDA team
strain Y51
-
-
Manually annotated by BRENDA team
strictly anaerobic, gram-positive bacterium
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-
Manually annotated by BRENDA team
strain Y51
-
-
Manually annotated by BRENDA team
Sulfurospirillum sp. mixed culture
-
UniProt
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1,1,2,2,3,3-heptachloropropane + reduced acceptor
1,1,2,3,3,3-hexachloroprop-1-ene + chloride + acceptor
show the reaction diagram
1,1,1,2-tetrachloroethane + reduced acceptor
1,1-dichlorethene + chloride + acceptor
show the reaction diagram
1,1,2,2-tetrachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
show the reaction diagram
1,1,2-trichloroethane + reduced acceptor
? + chloride + acceptor
show the reaction diagram
Clostridium bifermentans
-
-
-
-
?
1,1,2-trichloroethene + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
show the reaction diagram
1,1,3-trichloro-1-propene + Ti(III) citrate
1,1-dichloro-1-propene + Cl- + ?
show the reaction diagram
-
-
-
-
?
1,1,3-trichloropropene + reduced acceptor
1,1-dichloropropene + chloride + acceptor
show the reaction diagram
-
22.9% activity compared with perchloroethene as substrate
-
-
?
1,1-dichloroethylene + reduced acceptor
? + chloride + acceptor
show the reaction diagram
Clostridium bifermentans
-
-
-
-
?
1,2-dichloropropane + reduced acceptor
? + chloride + acceptor
show the reaction diagram
Clostridium bifermentans
-
-
-
-
?
2,3-dichloro-1-propene + Ti(III) citrate
2-chloropropene + Cl- + ?
show the reaction diagram
-
as a side product, 2,5-dichloro-1,5-hexadiene is formed demonstrating that the reductive dechlorination of 2,3-dichloropropene proceeds via a radical reaction mechanism
-
-
?
2,3-dichloropropene + reduced acceptor
2-chloropropene + chloride + acceptor
show the reaction diagram
-
14.4% activity compared with perchloroethene as substrate
-
-
?
chlorinated propenes + reduced acceptor
dechlorinated propene + chloride + acceptor
show the reaction diagram
-
22% of the reduction rates with perchloroethene
-
-
?
chloroacetamide + reduced acceptor
acetamide + chloride + acceptor
show the reaction diagram
-
very poor substrate
-
-
?
cis-1,2-dichloroethylene + reduced acceptor
? + chloride + acceptor
show the reaction diagram
Clostridium bifermentans
-
-
-
-
?
cis-1,3-dichloropropene + reduced acceptor
mono-chloropropene + chloride + acceptor
show the reaction diagram
-
chlorination rate is lower than for trans-1,3-dichloropropene and reaction ceases after 2-3 min
-
?
hexachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
show the reaction diagram
-
-
-
-
?
pentachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
show the reaction diagram
-
-
-
-
?
tetrachloroethene + 2 H2
cis-1,2-dichloroethene + 2 chloride + 2 H+
show the reaction diagram
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
show the reaction diagram
tetrachloroethene + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
show the reaction diagram
tetrachloroethene + reduced acceptor
trans-1,2 dichloroethene + acceptor + chloride
show the reaction diagram
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
show the reaction diagram
tetrachloroethene + reduced benzylviologen
trichloroethene + chloride + benzylviologen
show the reaction diagram
-
-
-
-
?
tetrachloroethene + reduced cobaltocene
trichloroethene + chloride + cobaltocene
show the reaction diagram
-
-
-
-
?
tetrachloroethene + reduced ethyl viologen
cis-1,2-dichloroethene + chloride + ethyl viologen
show the reaction diagram
-
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + chloride + methyl viologen
show the reaction diagram
-
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + methyl viologen
show the reaction diagram
tetrachloroethene + reduced methyl viologen
trichloroethene + chloride + methyl viologen
show the reaction diagram
-
-
-
?
tetrachloroethene + reduced methylviologen
trichloroethene + chloride + methylviologen
show the reaction diagram
tetrachloromethane + reduced acceptor
? + chloride + acceptor
show the reaction diagram
-
very poor substrate
-
-
?
tetraiodoethene + reduced acceptor
triiodoethene + iodide + acceptor
show the reaction diagram
-
reaction rate is considerably slower than with tetrachloroethene
-
-
?
trans-1,2-dichloroethylene + reduced acceptor
? + chloride + acceptor
show the reaction diagram
Clostridium bifermentans
-
-
-
-
?
trans-1,3-dichloropropene + reduced acceptor
mono-chloropropene + chloride + acceptor
show the reaction diagram
-
5.7% activity compared with perchloroethene as substrate
-
?
trichloroethene + chloride + methyl viologen
cis-1,2-dichloroethene + chloride + methyl viologen
show the reaction diagram
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
show the reaction diagram
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
tetrachloroethene + 2 H2
cis-1,2-dichloroethene + 2 chloride + 2 H+
show the reaction diagram
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
show the reaction diagram
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
show the reaction diagram
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corrinoid
menaquinone
-
membrane-bound menaquinone
vitamin B12
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cobalamin
Cobalt
Iron-sulfur cluster
iron-sulfur clusters
NH4Cl
-
activation of dechlorination of perchloroethene, 4 mM: 2fold activation
sulfur
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Iodopropane
carbon tetrachloride
-
growth inhibition at 0.001 mM
CCl4
-
0.1 mM: 50% inhibition
CH2Cl2
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0.05 mM: 50% inhibition
CH3Cl
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0.0008 mM: 50% inhibition
CHCl3
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0.025 mM: 50% inhibition
Chloroform
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significant growth inhibition of wild-type, no growth inhibition with mutant strains lacking the promoter of the enzyme gene cluster or the entire gene cluster
cis-1,2-dichloroethene
cis-1,3-dichloropropene
-
50% inhibition
CuCl2
-
1 mM cuprous chloride: slight inhibition
cyanide
Dithionite
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2 mM sodium dithionite: complete inhibition
Iodoethane
-
in the presence of titanium(III)citrate: 85% inhibition; light-reversible inhibition
nitrite
-
strong inhibition, 1 mM NO2-: complete inhibition
Propyl iodide
propyliodide
-
25 mM, 13% residual activity. When exposed to light, the activity is restored to 59% after 6 h and 90% after 24 h
sulfite
tetrachloroethene
-
substrate inhibition, Ki: 18 mM
trichloroethene
ZnCl2
-
5 mM zinc cloride: slight inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vitamin B12
-
tetrachloroethene dehalogenase formation in fumarate-grown cells is influenced by vitamin B12
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.773
1,1,1,2-tetrachloroethane
-
-
0.336
1,1,2,2-tetrachloroethane
-
-
0.535
1,1,2-trichloroethene
-
pH 7.5, 37C
0.25
1,1,3-trichloropropene
-
reduced 1.6 mM methyl viologen as electron donor
0.6
2,3-dichloropropene
-
reduced 1.6 mM methyl viologen as electron donor
0.125
hexachloroethane
-
-
0.28 - 0.3
methyl viologen
0.6199
pentachloroethane
-
-
0.024
reduced methyl viologen
30C
0.01 - 2
tetrachloroethene
0.25
trans-1,3-dichloropropene
-
reduced 1.6 mM methyl viologen as electron donor
0.004 - 0.24
trichloroethene
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 20.4
tetrachloroethene
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.086
Clostridium bifermentans
-
-
13.6
purified enzyme, 30C
113.6
-
pH 7.5, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
approximately
8
-
pH-optimum about 8.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
Clostridium bifermentans
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
Dehalococcoides sp.
predicted from cDNA
53000
-
SDS-PAGE, processed enzyme
55000
deduced from cDNA
55890
-
amino acid sequence analysis
57000
-
processed enzyme, pceA' gene product, SDS-PAGE
58000
-
gel filtration
59430
enzyme mass + cobalamin cofactor + iron-sulfur clusters, calculated from deduced amino acid sequence
61000
-
unprocessed enzyme, expressed in Escherichia coli, SDS-PAGE
65000
-
membrane proteins tend to form aggregates due to their high hydrophobicity, apparent MW of 200 kDa for the native enzyme may be a purification artifact, and the enzyme may be essentially monomeric with MW: 65000 Da in vivo, SDS-PAGE
70000
Clostridium bifermentans
-
gel filtration
71000
gel filtration
200000
-
membrane proteins tend to form aggregates due to their high hydrophobicity, apparent MW of 200 kDa for the native enzyme may be a purification artifact, and the enzyme may be essentially monomeric with MW of 65000 Da in vivo, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
trimer
-
3 * 65000, membrane proteins tend to form aggregates due to their high hydrophobicity, apparent MW of 200 kDa for the native enzyme may be a purification artifact, and the enzyme may be essentially monomeric with MW: 65000 Da in vivo, SDS-PAGE
additional information
-
membrane proteins tend to form aggregates due to their high hydrophobicity, apparent MW of 200 kDa for the native enzyme may be a purification artifact, and the enzyme may be essentially monomeric with MW: 65000 Da in vivo
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
unstable above pH 8 or below pH 5
349703
7
-
stable at neutral pH
349703
7.5 - 8
Clostridium bifermentans
-
most stable between
349709
additional information
-
stable at neutral pH
349703
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 35
Clostridium bifermentans
-
relatively stable between
50
-
thermolabile above 50C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cysteine stabilizes
-
enzyme generally unstable
Clostridium bifermentans
-
enzyme insensitive towards oxygen
-
enzyme oxygen sensitive
Clostridium bifermentans
-
enzyme slightly oxygen-sensitive
-
enzyme very labile during purification
-
ferrous ammonium sulfate stabilizes
-
oxygen-sensitive with half-life of approximately 50 min
-
purified enzyme not stable, 50% loss of activity at -30C
Clostridium bifermentans
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxygen exposure, half-life of 280 h upon exposure to air
657587
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30C, purified enzyme not stable, 50% loss of activity
Clostridium bifermentans
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Clostridium bifermentans
-
expressed in Escherichia coli DH5alpha
expression of pceA gene in Escherichia coli BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dceA6 gene is expressed 10fold after exposure to tetrachloroethene
tetrachloroethene-depleted cells grown for several subcultivation steps on fumarate as an alternative electron acceptor lose the tetrachloroethene-reductive dehalogenase PceA activity by the transposition of the pce gene cluster. In the absence of vitamin B12, a gradual decrease of the PceA activity and protein amount is observed. In the presence of vitamin B12, a significant delay in the decrease of the PceA activity with an more than 90% loss after 20 subcultivation steps is observed. This corresponds to the decrease in the pceA gene level. In the absence or presence of exogenous vitamin B12, the intracellular corrinoid level decreases in fumarate-grown cells and the PceA precursor forms catalytically inactive, corrinoid-free multiprotein aggregates
the level of gene transcription for tetrahalogene dehalogenase is very low
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in presence of 25 mM propyliodide, 13% residual activity. When exposed to light, the activity is restored to 59% after 6 h and 90% after 24 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
reductive dehalogenation assay can be used for the sensitive and rapid quantification of the corrinoid cofactor