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Information on EC 1.21.99.5 - tetrachloroethene reductive dehalogenase
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1.21.99.5 tetrachloroethene reductive dehalogenaseIUBMB Comments
This enzyme allows the common pollutant tetrachloroethene to support bacterial growth and is responsible for disposal of a number of chlorinated hydrocarbons. 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 involves menaquinol, which is reduced by molecular hydrogen via the action of 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 in vitro.
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Word Map
- 1.21.99.5
-
dechlorination
- dehalococcoides
-
chlorinate
-
dehalogenation
- mccartyi
-
bioremediation
-
organohalide
- desulfitobacterium
-
vinyl
-
organohalide-respiring
-
groundwater
- dehalobacter
-
rdhas
- corrinoids
- cis-1,2-dichloroethene
- hafniense
- multivorans
-
bioaugmentation
- sulfurospirillum
-
microcosm
- chloroflexi
- restrictus
- ethenogenes
-
dehalorespiration
-
cis-dce
-
aquifer
- chlorophenols
-
cpras
- cis-dichloroethene
- geobacter
-
debromination
- cobamide
- dehalogenans
- 2,4,6-trichlorophenol
-
epsilonproteobacterium
- 1,1,2-trichloroethane
- 1,1-dichloroethane
- analysis
- 1,2-dichloropropane
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
reductive dehalogenase, rdase, tetrachloroethene reductive dehalogenase, pce dehalogenase, pce reductive dehalogenase, tetrachloroethene (pce) reductive dehalogenase, tetrachloroethene dehalogenase, rdha3, pce-reductive dehalogenase, pce reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dceA6
dehalogenase, polychloroethene
-
-
-
-
EC 1.97.1.8
-
-
formerly
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mbrA
PCE dehalogenase
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-
-
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PCE reductase
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-
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PCE reductive dehalogenase
PCE-dechlorinating enzyme
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-
-
-
PCE-RD
-
-
-
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PCE-RDase
-
-
-
-
PCE-reductive dehalogenase
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-
-
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PCE/PCB RDase
PCE/TCERD
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-
-
-
PceA
pceA gene product
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-
-
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PceA1
highly homologous to PceA of Sulfurospirillum multivorans (93%)
PceA2
highly homologous to PceA of Sulfurospirillum multivorans (63%)
PceC
-
-
-
-
pceC gene product
-
-
-
-
PCER
-
-
-
-
PCERD
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-
-
-
perchloroethylene dehalogenase
-
-
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polychloroethane dehalogenase
-
-
-
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RD11
RD8
RDase
RdhA3
reductive dehalogenase
reductive PCE dehalogenase
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-
-
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TCE dehalogenase
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-
-
-
TCE reductase
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-
-
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tetrachloroethene (PCE) dehalogenase
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-
-
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tetrachloroethene and trichloroethene dehalogenase
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-
-
-
tetrachloroethene dehalogenase
-
-
-
-
tetrachloroethene reductase
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-
-
-
tetrachloroethene reductive dehalogenase
tetrachloroethene reductive dehalogenase catalytic subunit PceA
tetrachloroethylene reductase
-
-
-
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trichloroethene dehalogenase
-
-
-
-
PCE reductive dehalogenase
-
-
-
-
tetrachloroethene reductive dehalogenase
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-
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tetrachloroethene reductive dehalogenase catalytic subunit PceA
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-
tetrachloroethene reductive dehalogenase catalytic subunit PceA
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
mechanism
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
mechanism
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
mechanism
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
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 1.12.99.3: hydrogen:quinone oxidoreductase. The enzyme contains a corrinoid and two iron-sulfur clusters. Methyl viologen can act as electron donor
-
-
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
chemiosmotic mechanism
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
chemiosmotic mechanism
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
thermodynamics
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
thermodynamics
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
an electron transfer mechanism is not consistent with experimental data of rate constants. The actual mechanism involves more intimate interactions between the electron donor and the substrate in which the latter enters the cobalt coordination sphere
-
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor
standard potential of the electron acceptor center in -0.57 V
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dechlorination
-
-
reductive dechlorination
-
dehalogenation
-
-
reductive dehalogenation
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oxidation
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redox reaction
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-
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reduction
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-
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-
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PATHWAY SOURCE
PATHWAYS
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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. 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 involves menaquinol, which is reduced by molecular hydrogen via the action of 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 in vitro.
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CAS REGISTRY NUMBER
COMMENTARY
163913-51-7
-
175780-16-2
deleted registry number
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
1,1,1-trichloroethane + reduced acceptor
1,1-dichloroethane + chloride + acceptor
Dehalobacter sp. THM1
-
-
-
?
1,1,2-trichloroethane + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
1,1,3-trichloro-1-propene + Ti(III) citrate
1,1-dichloro-1-propene + Cl- + ?
-
-
-
-
?
1,1,3-trichloropropene + reduced acceptor
1,1-dichloropropene + chloride + acceptor
-
22.9% activity compared with perchloroethene as substrate
-
-
?
1,1-dichloroethylene + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
1,2,4,5-tetrachlorobenzene + reduced acceptor
1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + acceptor
-
-
-
-
?
1,2,4,5-tetrachlorobenzene + reduced methyl viologen
1,2,4-trichlorobenzene + chloride + methyl viologen
-
-
-
-
?
1,2,4-trichlorobenzene + reduced acceptor
1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + acceptor
-
-
-
-
?
1,2,4-trichlorobenzene + reduced methyl viologen
1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + methyl viologen
-
-
-
-
?
1,2-dichloropropane + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
2,3-dichloro-1-propene + Ti(III) citrate
2-chloropropene + Cl- + ?
-
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
-
14.4% activity compared with perchloroethene as substrate
-
-
?
2,4,5-trichlorophenol + reduced acceptor
3,4-dichlorophenol + chloride + oxidized acceptor
3,5-dichlorophenol + reduced acceptor
? + chloride + oxidized acceptor
-
-
-
?
chlorinated propenes + reduced acceptor
propene + chloride + acceptor
-
22% of the reduction rates with perchloroethene
-
-
?
chloroacetamide + reduced acceptor
acetamide + chloride + acceptor
-
very poor substrate
-
-
?
chloroethene + reduced acceptor
ethene + chloride + acceptor
-
-
-
-
?
cis-1,2-dichloroethene + reduced acceptor
monochloroethene + chloride + acceptor
-
-
-
-
?
cis-1,2-dichloroethylene + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
cis-1,3-dichloropropene + reduced acceptor
mono-chloropropene + chloride + acceptor
-
chlorination rate is lower than for trans-1,3-dichloropropene and reaction ceases after 2-3 min
-
?
dichloroethene + reduced acceptor
chloroethene + chloride + acceptor
-
-
-
-
?
hexachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
monochloroethene + reduced acceptor
ethene + chloride + acceptor
-
-
-
-
?
pentachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + 2 H2
cis-1,2-dichloroethene + 2 chloride + 2 H+
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
tetrachloroethene + reduced benzylviologen
trichloroethene + chloride + benzylviologen
-
-
-
-
?
tetrachloroethene + reduced cobaltocene
trichloroethene + chloride + cobaltocene
-
-
-
-
?
tetrachloroethene + reduced ethyl viologen
cis-1,2-dichloroethene + chloride + ethyl viologen
-
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + 2 chloride + methyl viologen
tetrachloroethene + reduced methyl viologen
trichloroethene + chloride + methyl viologen
-
-
-
?
tetrachloromethane + reduced acceptor
? + chloride + acceptor
-
very poor substrate
-
-
?
tetraiodoethene + reduced acceptor
triiodoethene + iodide + acceptor
-
reaction rate is considerably slower than with tetrachloroethene
-
-
?
trans-1,2-dichloroethylene + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
trans-1,3-dichloropropene + reduced acceptor
mono-chloropropene + chloride + acceptor
-
5.7% activity compared with perchloroethene as substrate
-
?
trichloroethene + reduced acceptor
dichloroethene + chloride + acceptor
-
-
-
-
?
1,1,1,2,2,3,3-heptachloropropane + reduced acceptor
1,1,2,3,3,3-hexachloroprop-1-ene + chloride + acceptor
-
-
-
-
?
1,1,1,2,2,3,3-heptachloropropane + reduced acceptor
1,1,2,3,3,3-hexachloroprop-1-ene + chloride + acceptor
-
-
-
-
?
1,1,1,2-tetrachloroethane + reduced acceptor
1,1-dichlorethene + chloride + acceptor
-
-
-
-
?
1,1,1,2-tetrachloroethane + reduced acceptor
1,1-dichlorethene + chloride + acceptor
-
-
-
-
?
1,1,2,2-tetrachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
1,1,2,2-tetrachloroethane + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
1,1,2-trichloroethene + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
1,1,2-trichloroethene + reduced acceptor
cis-1,2-dichlorethene + chloride + acceptor
-
-
-
-
?
2,2',3,4,4',5,5'-heptachlorobiphenyl + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
2,2',3,4,4',5,5'-heptachlorobiphenyl + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
2,3-dichlorophenol + reduced acceptor
2-chlorophenol + chloride + oxidized acceptor
-
-
-
?
2,3-dichlorophenol + reduced acceptor
2-chlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4,5-trichlorophenol + reduced acceptor
3,4-dichlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4,5-trichlorophenol + reduced acceptor
3,4-dichlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4,6-trichlorophenol + reduced acceptor
4-chlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4,6-trichlorophenol + reduced acceptor
4-chlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4-dichlorophenol + reduced acceptor
4-chlorophenol + chloride + oxidized acceptor
-
-
-
?
2,4-dichlorophenol + reduced acceptor
4-chlorophenol + chloride + oxidized acceptor
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
terminal component of the respiratory chain
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
terminal component of the respiratory chain
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
Sulfurospirillum multivorans DSMZ 12446
-
-
-
-
?
tetrachloroethene + reduced acceptor
cis-1,2-dichlorethene + 2 chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
cis-1,2-dichlorethene + 2 chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
cis-1,2-dichlorethene + 2 chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
cis-1,2-dichlorethene + 2 chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trans-1,2 dichloroethene + acceptor + 2 chloride
dechlorination activity of tetrachloroethene to trans-1,2 dichloroethene is detected after 24 h of incubating the corresponding unstained gel fragment
-
-
?
tetrachloroethene + reduced acceptor
trans-1,2 dichloroethene + acceptor + 2 chloride
dechlorination activity of tetrachloroethene to trans-1,2 dichloroethene is detected after 24 h of incubating the corresponding unstained gel fragment
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
lipophilic solvent tetrachloroethene, one of the most abundant halogenated xenobiotic pollutants in the environment
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
PCE reductase is the final enzyme of the perchloroethene respiratory chain that catalyzes the reductive cleavage of a carbon chlorine bond
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
quite specific for tetrachloroethene
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
artificial electron donor: reduced methyl viologen, physiological electron donor is not known
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
artificial electron donor: reduced methyl viologen, physiological electron donor is not known
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
besides reduced methyl viologen, titanium(III)citrate can serve as electron donor for reductive dehalogenation
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
perchloroethylene, perchloroethene, PCE
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
PCE, physiological electron donor is not known
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + oxidized acceptor
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + oxidized acceptor
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + oxidized acceptor
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + oxidized acceptor
-
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + 2 chloride + methyl viologen
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + 2 chloride + methyl viologen
-
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + 2 chloride + methyl viologen
via trichloroethene
-
-
?
tetrachloroethene + reduced methyl viologen
cis-1,2-dichloroethene + 2 chloride + methyl viologen
-
via trichloroethene
-
-
?
tetrachloroethene + reduced methylviologen
trichloroethene + chloride + methylviologen
-
-
-
-
?
tetrachloroethene + reduced methylviologen
trichloroethene + chloride + methylviologen
-
-
-
?
trichloroethene + chloride + acceptor
tetrachloroethene + reduced acceptor
-
-
-
-
?
trichloroethene + chloride + acceptor
tetrachloroethene + reduced acceptor
-
-
-
-
?
trichloroethene + chloride + methyl viologen
tetrachloroethene + reduced methyl viologen
-
-
-
?
trichloroethene + chloride + methyl viologen
tetrachloroethene + reduced methyl viologen
-
-
-
-
r
trichloroethene + chloride + methyl viologen
tetrachloroethene + reduced methyl viologen
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
artificial electron donor: reduced methyl viologen, physiological electron donor is not known
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
good substrate, comparable to tetrachloroethene
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
70% of activity compared with tetrachloroethene
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
good substrate, comparable to tetrachloroethene
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
poor substrate, 10% of the rate of tetrachloroethene
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
artificial electron donor: reduced methyl viologen, physiological electron donor is not known
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
besides reduced methyl viologen, titanium(III)citrate can serve as electron donor for reductive dehalogenation
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
physiological electron donor is not known
-
-
?
additional information
?
-
-
physiological electron donor is not known
-
-
?
additional information
?
-
-
PCE reductase is the final enzyme of the perchloroethene respiratory chain that catalyzes the reductive cleavage of a carbon chlorine bond
-
-
?
additional information
?
-
trichlofluoroethene, tetrachloromethane, hexachloroethane, tetrachloroethane, trichloroethane, and 1,1,1-trichloro-2,2,2-trifluoroethane cause an enzyme dependent oxidation of reduced methyl viologen
-
-
?
additional information
?
-
-
trichlofluoroethene, tetrachloromethane, hexachloroethane, tetrachloroethane, trichloroethane, and 1,1,1-trichloro-2,2,2-trifluoroethane cause an enzyme dependent oxidation of reduced methyl viologen
-
-
?
additional information
?
-
-
no activity with trichloroethene, TCE, cis-dichloroethene, cis-DCE, or vinyl chloride
-
-
?
additional information
?
-
-
very low activity with reduced benzyl viologen
-
-
?
additional information
?
-
-
no activity with 3-chloro-4-hydroxyphenylacetate and other ortho-chlorophenolic compounds, 2-chlorophenol, 3-chlorophenol, 4-chlorophenol, 2,3-dichlorophenol, 2,4-dichlorophenol, 2,5-dichlorophenol, 2,6-dichlorophenol, cis-dichloroethene
-
-
?
additional information
?
-
-
very high substrate specificity
-
-
?
additional information
?
-
-
no activity with other chloroethenes or chloromethanes or chlorinated aromatic compounds, no activity with carbon tetrachloride, 1,1-dichloroethene, trans-1,2-dichloroethene, cis-1,2-dichloroethene, 3-chlorobenzoate, 3-chloro-4-hydroxyphenol, pentachlorophenol, 2,4,6-trichlorophenol, 2,4,5-trichlorophenol
-
-
?
additional information
?
-
no substrates: 2,6-dichlorophenol, 3,4-dichlorophenol
-
-
?
additional information
?
-
no substrates: 2,6-dichlorophenol, 3,4-dichlorophenol
-
-
?
additional information
?
-
-
no substrates: 2,6-dichlorophenol, 3,4-dichlorophenol
-
-
?
additional information
?
-
-
the enzyme shows no dihaloelimination activity towards 1,1,2-trichloroethane or 1,1,1-trichloroethane
-
-
?
additional information
?
-
no substrates: 2,6-dichlorophenol, 3,4-dichlorophenol
-
-
?
additional information
?
-
-
no activity with 3-chloro-4-hydroxyphenylacetate and other ortho-chlorophenolic compounds, 2-chlorophenol, 3-chlorophenol, 4-chlorophenol, 2,3-dichlorophenol, 2,4-dichlorophenol, 2,5-dichlorophenol, 2,6-dichlorophenol, cis-dichloroethene
-
-
?
additional information
?
-
-
the enzyme shows no dihaloelimination activity towards 1,1,2-trichloroethane or 1,1,1-trichloroethane
-
-
?
additional information
?
-
-
no activity with 3-chloro-4-hydroxyphenylacetate and other ortho-chlorophenolic compounds, 2-chlorophenol, 3-chlorophenol, 4-chlorophenol, 2,3-dichlorophenol, 2,4-dichlorophenol, 2,5-dichlorophenol, 2,6-dichlorophenol, cis-dichloroethene
-
-
?
additional information
?
-
-
broad substrate specificity, degrades various chlorinated aliphatic compounds
-
-
?
additional information
?
-
-
broad substrate specificity, degrades various chlorinated aliphatic compounds
-
-
?
additional information
?
-
-
physiological electron donor is not known
-
-
?
additional information
?
-
-
no activity with other chloroethenes, chloroethanes or chloromethanes, no activity with 1,1-dichloroethene, trans-1,2-dichloroethene, 1,1,1-trichloroethane, 1,1,1-trichloroacetone, hexachloroethane, and the chlorinated aromatic compounds 3-chlorobenzoate, 4-chlorophenol, and 3,4-dichlorobenzoate
-
-
?
additional information
?
-
-
no activity with dichloroethene, 1-chloropropene, 2-chloropropene, 3-chloropropene, 1,1-dichloropropene, 1,2-dichloropropane, 1,3-dichloropropane, and 1,2,3-trichloropropane
-
-
?
additional information
?
-
-
anaerobic growth in presence of dimethylbenzimidazole leads to replacement of the adenine moiety in the nucleotide loop of cofoactor norpseudo-B12 by dimethylbenzimidazole. The formation of the dimethylbenzimidazole-containing nor-B12 severely affects tetrachloroethene-dependent growth and the PceA activity. In dimethylbenzimidazole-treated cells processing of the cytoplasmic PceA precursor is impeded. PceA enriched from cells cultivated with dimethylbenzimidazole contains nor-B12. Nor-B12 purified from cells grown in the presence of dimethylbenzimidazole mediates the abiotic reductive dehalogenation of trichloroacetate to dichloroacetate at a 25fold lower rate in comparison with norpseudo-B12
-
-
?
additional information
?
-
-
dehalogenation of tetrachloroethene results in a similar extent of C and Cl isotope fractionation, and in similar dual element isotope slopes for PceA enzyme and for abiotic dehylogenation by corrinoids. Catalytic dehalogenation by enzymes and different corrinoids display mechanistic and/or kinetic differences
-
-
?
additional information
?
-
-
anaerobic growth in presence of dimethylbenzimidazole leads to replacement of the adenine moiety in the nucleotide loop of cofoactor norpseudo-B12 by dimethylbenzimidazole. The formation of the dimethylbenzimidazole-containing nor-B12 severely affects tetrachloroethene-dependent growth and the PceA activity. In dimethylbenzimidazole-treated cells processing of the cytoplasmic PceA precursor is impeded. PceA enriched from cells cultivated with dimethylbenzimidazole contains nor-B12. Nor-B12 purified from cells grown in the presence of dimethylbenzimidazole mediates the abiotic reductive dehalogenation of trichloroacetate to dichloroacetate at a 25fold lower rate in comparison with norpseudo-B12
-
-
?
additional information
?
-
-
dehalogenation of tetrachloroethene results in a similar extent of C and Cl isotope fractionation, and in similar dual element isotope slopes for PceA enzyme and for abiotic dehylogenation by corrinoids. Catalytic dehalogenation by enzymes and different corrinoids display mechanistic and/or kinetic differences
-
-
?
additional information
?
-
no substrate: trichloroethene
-
-
?
additional information
?
-
-
in homogeneous aqueous solution containing titanium(III) citrate or titanium(III)-nitrilotriacetic acid as bulk electron donor, cobalamin, cobinamide, and cobamide are effective electron transfer mediators for the reduction of tetrachloroethene, trichloroethene, and trichlorofluoroethene. For a given chlorinated ethene, the reaction rate varies only slightly with pH and type of corrinoid present and is about 5 and 50 times faster for tetrachloroethene as compared to trichlorofluoroethene and trichloroethene, respectively. The first and rate-limiting step of the reduction of tetrachloroethene, trichloroethene, and trichlorofluoroethene by super-reduced corrinoids is a dissociative one-electron transfer yielding the corresponding vinyl radicals
-
-
?
additional information
?
-
using pull-down assays PceA1 interacts with DnaK (Hsp70)
-
-
?
additional information
?
-
using pull-down assays PceA1 interacts with DnaK (Hsp70)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2,4,5-tetrachlorobenzene + reduced acceptor
1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + acceptor
-
-
-
-
?
1,2,4-trichlorobenzene + reduced acceptor
1,3-dichlorobenzene + 1,4-dichlorobenzene + chloride + acceptor
-
-
-
-
?
chloroethene + reduced acceptor
ethene + chloride + acceptor
-
-
-
-
?
cis-1,2-dichloroethene + reduced acceptor
monochloroethene + chloride + acceptor
-
-
-
-
?
dichloroethene + reduced acceptor
chloroethene + chloride + acceptor
-
-
-
-
?
monochloroethene + reduced acceptor
ethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + 2 H2
cis-1,2-dichloroethene + 2 chloride + 2 H+
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
trichloroethene + reduced acceptor
dichloroethene + chloride + acceptor
-
-
-
-
?
2,2',3,4,4',5,5'-heptachlorobiphenyl + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
2,2',3,4,4',5,5'-heptachlorobiphenyl + reduced acceptor
? + chloride + acceptor
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
terminal component of the respiratory chain
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
terminal component of the respiratory chain
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
-
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
-
via trichloroethene, enables growth on tetrachloroethene as sole energy source
-
-
?
tetrachloroethene + 2 reduced acceptor
cis-1,2-dichloroethene + 2 chloride + 2 acceptor + 2 H+
Sulfurospirillum multivorans DSMZ 12446
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
PCE reductase is the final enzyme of the perchloroethene respiratory chain that catalyzes the reductive cleavage of a carbon chlorine bond
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
-
-
-
?
tetrachloroethene + reduced acceptor
trichloroethene + chloride + acceptor
-
PCE, physiological electron donor is not known
-
-
?
trichloroethene + chloride + acceptor
tetrachloroethene + reduced acceptor
-
-
-
-
?
trichloroethene + chloride + acceptor
tetrachloroethene + reduced acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
-
-
-
?
trichloroethene + reduced acceptor
cis-1,2-dichloroethene + chloride + acceptor
-
physiological electron donor is not known
-
-
?
additional information
?
-
-
PCE reductase is the final enzyme of the perchloroethene respiratory chain that catalyzes the reductive cleavage of a carbon chlorine bond
-
-
?
additional information
?
-
using pull-down assays PceA1 interacts with DnaK (Hsp70)
-
-
?
additional information
?
-
using pull-down assays PceA1 interacts with DnaK (Hsp70)
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
corrinoid
-
one mol of dehalogenase contains 1.0 mol of corrinoid
corrinoid
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
corrinoid
-
cofactor is absent in strain N and therefore the strain is unable to dechlorinate tetrachloroethene
vitamin B12
-
corrinoid cofactor is norpseudo-B12, adenine instead of 5,6-dimethylbenzimidazole serves as lower ligand base of the central cobalt ion
vitamin B12
-
PceA dehalogenase harbors either norpseudo-B12 as cofactor when Sulfurospirillum multivorans has been cultivated in the absence - or nor-B12 when Sulfurospirillum multivorans has been cultivated in its presence of 4,6-dimethylbenzimidazole. Dehalogenation rates with norpseudo-B12 reductive dehalogenase are faster than with nor-B12
additional information
-
anaerobic growth in presence of dimethylbenzimidazole leads to replacement of the adenine moiety in the nucleotide loop of norpseudo-B12 by dimethylbenzimidazole. The formation of the dimethylbenzimidazole-containing nor-B12 severely affects tetrachloroethene-dependent growth and the PceA activity. In dimethylbenzimidazole-treated cells processing of the cytoplasmic PceA precursor is impeded. PceA enriched from cells cultivated with dimethylbenzimidazole contains nor-B12. Nor-B12 purified from cells grown in the presence of dimethylbenzimidazole mediates the abiotic reductive dehalogenation of trichloroacetate to dichloroacetate at a 25fold lower rate in comparison with norpseudo-B12
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cobalamin
Cobalt
Fe2+
Iron
Iron-sulfur cluster
iron-sulfur clusters
NH4+
NH4Cl
-
activation of dechlorination of perchloroethene, 4 mM: 2fold activation
sulfur
additional information
Cobalt
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
Cobalt
-
cobalt of the cofactor vitamin B12 appears to be subjected to a change in its redox state in the course of the halogenation
Fe2+
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
Fe2+
-
one mol of dehalogenase contains 9.8 mol of iron, and 8.0 mol of acid-labile sulfur
Iron-sulfur cluster
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
Iron-sulfur cluster
-
iron-sulfur clusters are present as additional cofactors, one mol of dehalogenase contains 9.8 mol of iron, and 8.0 mol of acid-labile sulfur
iron-sulfur clusters
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
iron-sulfur clusters
-
iron-sulfur clusters are present as additional cofactors, one mol of dehalogenase contains 9.8 mol of iron, and 8.0 mol of acid-labile sulfur
S
-
contains 0.7 mol corrinoid, 1.0 mol cobalt, 7.8 mol iron, and 10.3 mol acid-labile sulfur per mol subunit
S
-
one mol of dehalogenase contains 9.8 mol of iron, and 8.0 mol of acid-labile sulfur
additional information
-
indicates the presence of a second transition metal
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chloroform
-
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
Iodoethane
-
in the presence of titanium(III)citrate: 85% inhibition; light-reversible inhibition
propyliodide
-
25 mM, 13% residual activity. When exposed to light, the activity is restored to 59% after 6 h and 90% after 24 h
cis-1,2-dichloroethene
-
significant growth inhibition of strain in presence of cis-1,2-dichloroethene, during growth in presence of cis-1,2-dichloroethene, the enzyme gene cluster is deleted with high frequency
cis-1,2-dichloroethene
-
slight inhibition at high concentrations, 14 mM: 50% inhibition
N2O
-
dinitrogen oxide; N2O, 100%, present in the gas phase: complete inhibition
Propyl iodide
-
1-iodopropane; 1-iodopropane, photoreversible inactivation
Propyl iodide
-
no inhibition in the presence of 1-iodopropane and titanium(III)citrate
Propyl iodide
-
1-iodopropane; 1-iodopropane, photoreversible inactivation
Propyl iodide
-
0.05 mM 1-iodopropane: 3fold inhibition, completely reversed by light, light-reversible inhibition; 1-iodopropane
Propyl iodide
-
1-iodopropane; 90% inhibition by mixture of propyl iodide and titanium citrate in the dark, light restores about 95% of initial activity; light-reversible inactivation in the presence of titanium(III)citrate as electron donor
Propyl iodide
-
1-iodopropane; light-reversible inactivation in the presence of titanium(III)citrate as electron donor
Propyl iodide
-
1-iodopropane; 1-iodopropane, photoreversible inactivation; light-reversible inactivation in the presence of titanium(III)citrate as electron donor
trichloroethene
-
substrate inhibition, higher concentrations of trichloroethene: inhibition of PCE dehalogenase, Ki: 1.3 mM
additional information
-
no inhibition by 2 mM sodium sulfate, sodium selenate, sodium sulfide, or 100% carbon monoxide; no inhibition by 5 mM EDTA, bathophenanthroline disulfonate, and 2,2-dipyridyl
-
additional information
-
cis-1,2-dichloroethene is not inhibitory, previous findings of inhibition were due to contamination of cis-1,2-dichloroethene by chloroform. Carbon dichloride does not inhibit growth up to 1 mM
-
additional information
-
no inhibition by 1,1-dichloroethene, trans-1,2-dichloroethene, 1,1,1-trichloroethane, 1,1,1-trichloroacetone, hexachloroethane, and the chlorinated aromatic compounds 3-chlorobenzoate, 4-chlorophenol, and 3,4-dichlorobenzoate
-
additional information
-
no inhibition by 1-chloropropene, 2-chloropropene, 3-chloropropene, 1,1-dichloropropene, 1,2-dichloropropane, 1,3-dichloropropane, and 1,2,3-trichloropropane
-
additional information
-
no inhibition by carbon monoxide, azide, hydroxylamine, nitrate, cis-1,2-dichloroethene, trans-1,2-dichloroethene or 1,1-dichloroethene
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
vitamin B12
-
tetrachloroethene dehalogenase formation in fumarate-grown cells is influenced by vitamin B12
additional information
dechlorination activity occurs only in cell extracts from anaerobically grown cultures. Dechlorination activity requires that vitamin B12 was present in the growth medium of the cells
-
additional information
-
dechlorination activity occurs only in cell extracts from anaerobically grown cultures. Dechlorination activity requires that vitamin B12 was present in the growth medium of the cells
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.25
trans-1,3-dichloropropene
-
reduced 1.6 mM methyl viologen as electron donor
0.28
methyl viologen
-
at a tetrachloroethene concentration of 1 mM
0.3
methyl viologen
-
at a tetrachloroethene concentration of 1 mM
0.1 - 2
tetrachloroethene
pH 8.0, temperature not specified in the publication
0.2
tetrachloroethene
-
reduced 1.6 mM methyl viologen as electron donor
0.24
trichloroethene
-
reduced 1.6 mM methyl viologen as electron donor
additional information
additional information
-
enzyme kinetics and kinetic parameters
-
additional information
additional information
-
enzyme kinetics and kinetic parameters
-
additional information
additional information
-
enzyme kinetics and kinetic parameters
-
additional information
additional information
-
enzyme kinetics and kinetic parameters
-
additional information
additional information
-
enzyme kinetics and kinetic parameters
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
tetrachloroethene
-
titanium(III)citrate as sole electron donor
20.4
tetrachloroethene
-
methyl viologen as artificial electron donor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
8.1
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain TCE1, DSMZ 12704, formerly Desulfitobacterium frappieri strain TCE1
SwissProt
brenda
strain N, DSM 15119, non-dechlorinating, strain K, DSM 12446, dechlorinating
-
-
brenda
strictly anaerobic, gram-negative bacterium
-
-
brenda
tetrachloroethene-utilizing anaerobic bacterium
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
studies on cellular localization indicates presence of a cytoplasmic and a membrane-bound, periplasmic PCE dehalogenase
brenda
-
in cells grown on pyruvate plus fumarate, a major part of the enzyme is either localized in the cytoplasm or membrane associated facing the cytoplasm
brenda
-
cytoplasmic side of membrane, mainly associated with the membrane
-
brenda
-
not an integral membrane protein but a peripheral membrane protein
-
brenda
-
not an integral membrane protein but a peripheral membrane protein
-
-
brenda
-
studies on cellular localization indicates presence of a cytoplasmic and a membrane-bound, periplasmic PCE dehalogenase
-
brenda
-
membrane-associated, periplasmic hydrogenase
-
brenda
-
in cells grown on pyruvate plus fumarate, a major part of the enzyme is either localized in the cytoplasm or membrane associated facing the cytoplasm. In cells grown on pyruvate or formate as electron donors and tetrachloroethene as electron acceptor, most of the enzyme is at the periplasmic side of the cytoplasmic membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
according to a model for the maturation of PceA, the pce genes are transcribed in tetrachloroethene-grown cells and the PceA cofactor-free precursor is formed and binds to the PceT chaperone. When corrinoid cofactor is provided by de novo biosynthesis, it is incorporated into prePceA. After incorporation of this cofactor and assembly and incorporation of the iron-sulfur clusters, the precursor protein is correctly folded and exported to the exoplasm by the Tat machinery. After cleavage of the signal peptide, the protein is bound to PceB, which may serve as a membrane anchor for PceA. In cells subcultivated for a few steps with fumarate instead of tetrachloroethene, corrinoid biosynthesis is impeded. This causes aggregation of the prePceA together with PceT and other proteins inside the cells. Excision of the pce gene cluster occurs upon longterm cultivation with fumarate. The loss of the gene cluster is delayed in the presence of exogenous vitamin B12
metabolism
-
according to a model for the maturation of PceA, the pce genes are transcribed in tetrachloroethene-grown cells and the PceA cofactor-free precursor is formed and binds to the PceT chaperone. When corrinoid cofactor is provided by de novo biosynthesis, it is incorporated into prePceA. After incorporation of this cofactor and assembly and incorporation of the iron-sulfur clusters, the precursor protein is correctly folded and exported to the exoplasm by the Tat machinery. After cleavage of the signal peptide, the protein is bound to PceB, which may serve as a membrane anchor for PceA. In cells subcultivated for a few steps with fumarate instead of tetrachloroethene, corrinoid biosynthesis is impeded. This causes aggregation of the prePceA together with PceT and other proteins inside the cells. Excision of the pce gene cluster occurs upon longterm cultivation with fumarate. The loss of the gene cluster is delayed in the presence of exogenous vitamin B12
-
physiological function
-
overview on dehalorespiration with H2 as electron donor and tetrachloroethene as electron acceptor. Tetrachloroethene reducing organisms include Desulfitobacterium sp., Dehalobacter restrictus as well as Dehalospirillum multivorans, Desulfuromonas chloroethenica, Dehalococcoides ethenogenes, and the facultative anaerobes Enterobacter strain MS-1 and Enterobacter agglomerans
physiological function
the strain shows a close coupling of cell growth and chlorine removal during tetrachloroethene dechlorination
physiological function
-
the strain shows a close coupling of cell growth and chlorine removal during tetrachloroethene dechlorination
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PCEA_DEHRP
Dehalobacter restrictus (strain DSM 9455 / PER-K23)
551
0
61202
Swiss-Prot
-
PCEA_DESHY
Desulfitobacterium hafniense (strain Y51)
551
0
61285
Swiss-Prot
-
A0A160V9J1_9ZZZZ
424
0
47836
TrEMBL
other Location (Reliability: 1)
A0A142VC48_9CHLR
498
0
55199
TrEMBL
Secretory Pathway (Reliability: 2)
B8FVX4_DESHD
Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)
550
0
61174
TrEMBL
-
U3MYW0_9PROT
500
0
55532
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
56000
57000
58000
59000
59430
enzyme mass + cobalamin cofactor + iron-sulfur clusters, calculated from deduced amino acid sequence
60000
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
monomer
1 * 60000, SDS-PAGE, native mass of 71000 determined by gel filtration
monomer
-
1 * 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 of 65000 Da in vivo, probably a monomeric 65-kDa protein, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
x * 61000 Da, unprocessed protein, x * 58000, mature protein
proteolytic modification
-
x * 61000 Da, unprocessed protein, x * 58000, mature protein
-
proteolytic modification
-
modified by truncation of the first 30 amino acids
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the expression of catalytically active PceA enzyme in Shimwellia blattae is significantly enhanced when its dedicated PceT chaperone is coproduced and when 5,6-dimethylbenzimidazole and hydroxocobalamin are added to the cultures
synthesis
-
the expression of catalytically active PceA enzyme in Shimwellia blattae is significantly enhanced when its dedicated PceT chaperone is coproduced and when 5,6-dimethylbenzimidazole and hydroxocobalamin are added to the cultures
-
synthesis
-
the expression of catalytically active PceA enzyme in Shimwellia blattae is significantly enhanced when its dedicated PceT chaperone is coproduced and when 5,6-dimethylbenzimidazole and hydroxocobalamin are added to the cultures
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to oxygen exposure, half-life of 280 h upon exposure to air
657587
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha
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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
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
-
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
-
-
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
-
reductive dehalogenation assay can be used for the sensitive and rapid quantification of the corrinoid cofactor
agriculture
-
degradation of lipophilic solvent tetrachloroethene, one of the most abundant halogenated xenobiotic pollutants in the environment
agriculture
-
degradation of lipophilic solvent tetrachloroethene, one of the most abundant halogenated xenobiotic pollutants in the environment
agriculture
-
uesd to decontaminate environment polluntant, tetrachloroethene, by tetrachloroethene bioremediation
agriculture
-
can play important role in breakdown of perchloroethene and other chlorinated aliphatic compounds in sites contaminated with mixtures of halogenated substances
agriculture
-
bioremediation of chloroethylenes, multiple chlorinated aliphatic molecules, in contaminated sites and water, anaerobic reductive dehalogenation of toxic xenobiotic
agriculture
-
can play important role in breakdown of perchloroethene and other chlorinated aliphatic compounds in sites contaminated with mixtures of halogenated substances
-
agriculture
-
bioremediation of chloroethylenes, multiple chlorinated aliphatic molecules, in contaminated sites and water, anaerobic reductive dehalogenation of toxic xenobiotic
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Neumann, A.; Wohlfarth, G.; Diekert, G.
Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans
J. Biol. Chem.
271
16515-16519
1996
Sulfurospirillum multivorans
brenda
Schumacher, W.; Holliger, C.; Zehnder, A.J.B.; Hagen, W.R.
Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus
FEBS Lett.
409
421-425
1997
Dehalobacter restrictus
brenda
Schumacher, W.; Holliger, C.
The proton/electron ratio of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in "Dehalobacter restrictus"
J. Bacteriol.
178
2328-2333
1996
Dehalobacter restrictus
brenda
Magnuson, J.K.; Stern, R.V.; Gossett, J.M.; Zinder, S.H.; Burris, D.R.
Reductive dechlorination of tetrachloroethene to ethene by a two-component enzyme pathway
Appl. Environ. Microbiol.
64
1270-1275
1998
Dehalococcoides mccartyi
brenda
Neumann, A.; Siebert, A.; Trescher, T.; Reinhardt, S.; Wohlfarth, G.; Diekert, G.
Tetrachloroethene reductive dehalogenase of Dehalospirillum multivorans: substrate specificity of the native enzyme and its corrinoid cofactor
Arch. Microbiol.
177
420-426
2002
Sulfurospirillum multivorans
brenda
Van de Pas, B.A.; Gerritse, J.; De Vos, W.M.; Schraa, G.; Stams, A.J.M.
Two distinct enzyme systems are responsible for tetrachloroethene and chlorophenol reductive dehalogenation in Desulfitobacterium strain PCE1
Arch. Microbiol.
176
165-169
2001
Desulfitobacterium hafniense, Desulfitobacterium sp. PCE1, Desulfitobacterium hafniense TCE1
brenda
Miller, E.; Wohlfarth, G.; Diekert, G.
Purification and characterization of the tetrachloroethene reductive dehalogenase of strain PCE-S
Arch. Microbiol.
169
497-502
1998
Desulfitobacterium hafniense
brenda
Neumann, A.; Wohlfarth, G.; Diekert, G.
Properties of tetrachloroethene and trichloroethene dehalogenase of Dehalospirillum multivorans
Arch. Microbiol.
163
276-281
1995
Sulfurospirillum multivorans
-
brenda
Neumann, A.; Wohlfarth, G.; Diekert, G.
Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli
J. Bacteriol.
180
4140-4145
1998
Sulfurospirillum multivorans
brenda
Okeke, B.C.; Chang, Y.C.; Hatsu, M.; Suzuki, T.; Takamizawa, K.
Purification, cloning, and sequencing of an enzyme mediating the reductive dechlorination of tetrachloroethylene (PCE) from Clostridium bifermentans DPH-1
Can. J. Microbiol.
47
448-456
2001
Paraclostridium bifermentans, Paraclostridium bifermentans DPH-1
brenda
Maillard, J.; Schumacher, W.; Vazquez, F.; Regeard, C.; Hagen, W.R.; Holliger, C.
Characterization of the corrinoid iron-sulfur protein tetrachloroethene reductive dehalogenase of Dehalobacter restrictus
Appl. Environ. Microbiol.
69
4628-4638
2003
Dehalobacter restrictus (Q8GJ27), Dehalobacter restrictus, Desulfitobacterium hafniense (Q8GJ31), Desulfitobacterium hafniense
brenda
Nijenhuis, I.; Zinder, S.H.
Characterization of hydrogenase and reductive dehalogenase activities of Dehalococcoides ethenogenes strain 195
Appl. Environ. Microbiol.
71
1664-1667
2005
Dehalococcoides mccartyi
brenda
Siebert, A.; Neumann, A.; Schubert, T.; Diekert, G.
A non-dechlorinating strain of Dehalospirillum multivorans: evidence for a key role of the corrinoid cofactor in the synthesis of an active tetrachloroethene dehalogenase
Arch. Microbiol.
178
443-449
2002
Sulfurospirillum multivorans
brenda
Futagami, T.; Yamaguchi, T.; Nakayama, S.; Goto, M.; Furukawa, K.
Effects of chloromethanes on growth of and deletion of the pce gene cluster in dehalorespiring Desulfitobacterium hafniense strain Y51
Appl. Environ. Microbiol.
72
5998-6003
2006
Desulfitobacterium hafniense, Desulfitobacterium hafniense Y51
brenda
John, M.; Schmitz, R.P.; Westermann, M.; Richter, W.; Diekert, G.
Growth substrate dependent localization of tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans
Arch. Microbiol.
186
99-106
2006
Sulfurospirillum multivorans
brenda
Costentin, C.; Robert, M.; Saveant, J.
Does catalysis of reductive dechlorination of tetra- and trichloroethylenes by vitamin B12 and corrinoid-based dehalogenases follow an electron transfer mechanism?
J. Am. Chem. Soc.
127
12154-12155
2005
synthetic construct
brenda
Diekert, G.; Gugova, D.; Limoges, B.; Robert, M.; Saveant, J.M.
Electroenzymatic reactions. Investigation of a reductive dehalogenase by means of electrogenerated redox cosubstrates
J. Am. Chem. Soc.
127
13583-13588
2005
Sulfurospirillum multivorans
brenda
Furukawa, K.; Suyama, A.; Tsuboi, Y.; Futagami, T.; Goto, M.
Biochemical and molecular characterization of a tetrachloroethene dechlorinating Desulfitobacterium sp. strain Y51: a review
J. Ind. Microbiol. Biotechnol.
32
534-541
2005
Desulfitobacterium sp., Desulfitobacterium sp. Y51
brenda
Schmitz, R.P.; Wolf, J.; Habel, A.; Neumann, A.; Ploss, K.; Svatos, A.; Boland, W.; Diekert, G.
Evidence for a radical mechanism of the dechlorination of chlorinated propenes mediated by the tetrachloroethene reductive dehalogenase of Sulfurospirillum multivorans
Environ. Sci. Technol.
41
7370-7375
2007
Sulfurospirillum multivorans
brenda
Kimoto, H.; Suye, S.; Makishima, H.; Arai, J.; Yamaguchi, S.; Fujii, Y.; Yoshioka, T.; Taketo, A.
Cloning of a novel dehalogenase from environmental DNA
Biosci. Biotechnol. Biochem.
74
1290-1292
2010
uncultured bacterium (D6RU53), uncultured bacterium (D6RU55)
brenda
Chow, W.L.; Cheng, D.; Wang, S.; He, J.
Identification and transcriptional analysis of trans-DCE-producing reductive dehalogenases in Dehalococcoides species
ISME J.
4
1020-1030
2010
Dehalococcoides sp. (D6MZ08), Dehalococcoides sp. MB (D6MZ08)
brenda
Reinhold, A.; Westermann, M.; Seifert, J.; von Bergen, M.; Schubert, T.; Diekert, G.
Impact of vitamin B12 on formation of the tetrachloroethene reductive dehalogenase in Desulfitobacterium hafniense strain Y51
Appl. Environ. Microbiol.
78
8025-8032
2012
Desulfitobacterium hafniense, Desulfitobacterium hafniense Y51
brenda
Buttet, G.F.; Holliger, C.; Maillard, J.
Functional genotyping of Sulfurospirillum spp. in mixed cultures allowed the identification of a new tetrachloroethene reductive dehalogenase
Appl. Environ. Microbiol.
79
6941-6947
2013
Sulfurospirillum sp. mixed culture SL2 (U3MYW0)
brenda
Keller, S.; Ruetz, M.; Kunze, C.; Kraeutler, B.; Diekert, G.; Schubert, T.
Exogenous 5,6-dimethylbenzimidazole caused production of a non-functional tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans
Environ. Microbiol.
16
3361-3369
2014
Sulfurospirillum multivorans, Sulfurospirillum multivorans DSM 12446
brenda
Lohner, S.; Spormann, A.
Identification of a reductive tetrachloroethene dehalogenase in Shewanella sediminis
Philos. Trans. R. Soc. Lond. B Biol. Sci.
368
20120326
2013
Shewanella sediminis (A8FZV0), Shewanella sediminis
brenda
Mac Nelly, A.; Kai, M.; Svatos, A.; Diekert, G.; Schubert, T.
Functional heterologous production of reductive dehalogenases from Desulfitobacterium hafniense strains
Appl. Environ. Microbiol.
80
4313-4322
2014
Desulfitobacterium hafniense (B8FVX4), Desulfitobacterium hafniense (Q8L172), Desulfitobacterium hafniense, Desulfitobacterium hafniense DSM 10664 (B8FVX4), Desulfitobacterium hafniense Y51 (Q8L172), Desulfitobacterium hafniense Y51
brenda
Glod, G.; Angst, W.; Holliger, C.; Schwarzenbach, R.P.
Corrinoid-mediated reduction of tetrachloroethene, trichloroethene, and trichlorofluoroethene in homogeneous aqueous solution: Reaction kinetics and reaction mechanisms
Environ. Sci. Technol.
31
253-260
1997
synthetic construct
-
brenda
Renpenning, J.; Keller, S.; Cretnik, S.; Shouakar-Stash, O.; Elsner, M.; Schubert, T.; Nijenhuis, I.
Combined C and Cl isotope effects indicate differences between corrinoids and enzyme (Sulfurospirillum multivorans PceA) in reductive dehalogenation of tetrachloroethene, but not trichloroethene
Environ. Sci. Technol.
48
11837-11845
2014
Sulfurospirillum multivorans, Sulfurospirillum multivorans DSM 12446
brenda
Zhao, S.; Ding, C.; He, J.
Genomic characterization of Dehalococcoides mccartyi strain 11a5 reveals a circular extrachromosomal genetic element and a new tetrachloroethene reductive dehalogenase gene
FEMS Microbiol. Ecol.
93
fiw235
2016
Dehalococcoides mccartyi (A0A142VC48), Dehalococcoides mccartyi, Dehalococcoides mccartyi 11a5 (A0A142VC48)
brenda
Holliger, C.; Wohlfarth, G.; Diekert, G.
Reductive dechlorination in the energy metabolism of anaerobic bacteria
FEMS Microbiol. Rev.
22
383-398
1999
uncultured bacterium
-
brenda
Zhao, S.; Rogers, M.J.; He, J.
Microbial reductive dehalogenation of trihalomethanes by a Dehalobacter-containing co-culture
Appl. Microbiol. Biotechnol.
101
5481-5492
2017
Dehalobacter sp. THM1 (A0A1I9LHM9)
brenda
Ismaeil, M.; Yoshida, N.; Katayama, A.
Identification of multiple dehalogenase genes involved in tetrachloroethene-to-ethene dechlorination in a Dehalococcoides-dominated enrichment culture
BioMed Res. Int.
2017
9191086
2017
Dehalococcoides sp. YN3
brenda
Kranzioch, I.; Ganz, S.; Tiehm, A.
Chloroethene degradation and expression of Dehalococcoides dehalogenase genes in cultures originating from Yangtze sediments
Environ. Sci. Pollut. Res. Int.
22
3138-3148
2015
Dehalococcoides sp.
brenda
Wang, S.; Chng, K.R.; Chen, C.; Bedard, D.L.; He, J.
Genomic Ccharacterization of Dehalococcoides mccartyi strain JNA that reductively dechlorinates tetrachloroethene and polychlorinated biphenyls
Environ. Sci. Technol.
49
14319-14325
2015
Dehalococcoides mccartyi, Dehalococcoides mccartyi JNA
brenda
Kunze, C.; Diekert, G.; Schubert, T.
Subtle changes in the active site architecture untangled overlapping substrate ranges and mechanistic differences of two reductive dehalogenases
FEBS J.
284
3520-3535
2017
Desulfitobacterium hafniense, Desulfitobacterium hafniense Y51
brenda
Gadkari, J.; Goris, T.; Schiffmann, C.L.; Rubick, R.; Adrian, L.; Schubert, T.; Diekert, G.
Reductive tetrachloroethene dehalogenation in the presence of oxygen by Sulfurospirillum multivorans physiological studies and proteome analysis
FEMS Microbiol. Ecol.
94
fix176
2018
Sulfurospirillum multivorans, Sulfurospirillum multivorans DSMZ 12446
brenda
Gadkari, J.; Goris, T.; Schiffmann, C.L.; Rubick, R.; Adrian, L.; Schubert, T.; Diekert, G.
Reductive tetrachloroethene dehalogenation in the presence of oxygen by Sulfurospirillum multivorans physiological studies and proteome analysis
FEMS Microbiol. Ecol.
94
doi: 10.1093/femsec/fix176
2018
Desulfitobacterium hafniense, Desulfitobacterium hafniense Y51
brenda
Alfan-Guzman, R.; Ertan, H.; Manefield, M.; Lee, M.
Isolation and characterization of Dehalobacter sp. strain TeCB1 including identification of TcbA a novel tetra- and trichlorobenzene reductive dehalogenase
Front. Microbiol.
8
558
2017
Dehalobacter sp. TeCB1
brenda
Matturro, B.; Presta, E.; Rossetti, S.
Reductive dechlorination of tetrachloroethene in marine sediments Biodiversity and dehalorespiring capabilities of the indigenous microbes
Sci. Total Environ.
545-546
445-452
2016
Dehalococcoides mccartyi
brenda
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