Information on EC 1.1.1.404 - tetrachlorobenzoquinone reductase

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The expected taxonomic range for this enzyme is: Sphingobium chlorophenolicum

EC NUMBER
COMMENTARY hide
1.1.1.404
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RECOMMENDED NAME
GeneOntology No.
tetrachlorobenzoquinone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Chlorocyclohexane and chlorobenzene degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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pentachlorophenol degradation
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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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
show the reaction diagram
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
show the reaction diagram
2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
show the reaction diagram
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
show the reaction diagram
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
show the reaction diagram
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
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
show the reaction diagram
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
poor activity with NADPH
[2Fe-2S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
protein contains 1.7 mol of iron per mol
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0383
2,6-dichloroindophenol
pH 7.6, 22C
0.0176
cytochrome c
pH 7.6, 22C
0.0115
NADH
pH 7.6, 22C
1.21
NADPH
pH 7.6, 22C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.1
2,6-dichloroindophenol
pH 7.6, 22C
9.1
cytochrome c
pH 7.6, 22C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12000
2,3,5,6-tetrachloro-1,4-benzoquinone
pH 7.6, 22C
368
2,6-dichloroindophenol
pH 7.6, 22C
510
cytochrome c
pH 7.6, 22C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
70% of maximum activity
8
20% of maximum activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
protein exists as trimer, dynamic light scattering
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
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
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
recombinant protein,. Purified enzyme is colorless
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Eshcerichia coli
expression in Pseudomonas aeruginosa
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of PcpD is induced in the presence of pentachlorophenol