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Enzyme Nomenclature
Information on EC 1.1.1.404 - tetrachlorobenzoquinone reductase
for references in articles please use BRENDA:EC1.1.1.404
Word Map on EC 1.1.1.404
- 1.1.1.404
- chlorophenolicum
-
sphingobium
- pentachlorophenol
- pcp
-
biodegradation
-
pollutant
- flavin
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The expected taxonomic range for this enzyme is: Sphingobium chlorophenolicum
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EC NUMBER 
COMMENTARY 
1.1.1.404
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RECOMMENDED NAME
GeneOntology No.
tetrachlorobenzoquinone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2,3,5,6-tetrachlorohydroquinone:NAD+ oxidoreductase
Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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the enzyme participates in the degradation of pentachlorophenol
physiological function
physiological function
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a mutant strain lacking functional PcpD has an impaired ability to remove pentachlorophenol from the medium but removes tetrachlorophenol from the medium at the same rate as does the wild-type strain
physiological function
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TCBQ reductase is the second enzyme in the pentachlorophenol degradation pathway. It rescues the nonproductive diradical complex generated by pentachlorophenol hydroxylase via two fast sequential one-electron transfers
physiological function
tetrachlorohydroquinone reductase PcpD catalyzes the reduction of tetrachlorohydroquinone to tetrachlorohydroquinone. In the presence of PcpD, tetrachlorohydroquinone formed by pentachlorophenol hydroxylase PcpB is sequestered until it is reduced to the less toxic tetrachlorohydroquinone, protecting the bacterium from the toxic effects of tetrachlorohydroquinone and maintaining flux through the pathway. Deletion of pcpD results in increased sensitivity to phenols that are degraded via a benzoquinone intermediate
physiological function
-
a mutant strain lacking functional PcpD has an impaired ability to remove pentachlorophenol from the medium but removes tetrachlorophenol from the medium at the same rate as does the wild-type strain
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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
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
-
-
-
?
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
the enzyme participates in the degradation of pentachlorophenol
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
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-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
-
-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
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-
-
?
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
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-
-
?
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
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-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
M9WIZ7
-
-
-
?
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
M9WIZ7
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
the enzyme participates in the degradation of pentachlorophenol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
FMN
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the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
[2Fe-2S]-center
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
[2Fe-2S]-center
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the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pentachlorophenol
competitive, 55% loss of activity at 0.1 mM
tetrachlorohydroquinone
activity of PcpD is stimulated by tetrachlorohydroquinone at low concentrations but inhibited at high concentrations. 83% increase in activity at 0.1 mM tetrachlorohydroquinone, 60% loss of activity at 0.2 mM tetrachlorohydroquinone
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrachlorohydroquinone
activity of PcpD is stimulated by tetrachlorohydroquinone at low concentrations but inhibited at high concentrations. 83% increase in activity at 0.1 mM tetrachlorohydroquinone, 60% loss of activity at 0.2 mM tetrachlorohydroquinone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
additional information
protein exists as trimer, dynamic light scattering
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
homotrimer
3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
homotrimer
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3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The active site is slightly positively charged and situated in a deep pit on the surface. The putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster. It is formed mainly by residues Ser78, Arg79, Phe225, Gly226, Ala227, Ala228, Leu229, Gln275 and the cofactor FMN
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein, golden-brown enzyme with a spectrum consistent with the presence of both a flavin and an iron-sulfur cluster
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of PcpD is induced in the presence of pentachlorophenol
expression of PcpD is induced in the presence of pentachlorophenol
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expression of PcpD is induced in the presence of pentachlorophenol
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.404)
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