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Enzyme Nomenclature
Information on EC 1.14.12.18 - biphenyl 2,3-dioxygenase
for references in articles please use BRENDA:EC1.14.12.18
Word Map on EC 1.14.12.18
- 1.14.12.18
- biphenyls
-
polychlorinated
- burkholderia
- pseudoalcaligenes
- xenovorans
-
chlorobiphenyls
-
bpdos
-
pcb-degrading
- testosteroni
-
rieske-type
- comamonas
-
dihydrodiols
-
cis-dihydrodiols
- dibenzofuran
- 2,3-dihydroxybiphenyls
-
ring-hydroxylating
-
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
-
pcb-contaminated
- yanoikuyae
-
biphenyl-degrading
- globerulus
- beijerinckia
- synthesis
-
biphenyl-utilizing
-
biphenyl-induced
-
pandoraea
-
2,2\',5,5\'-tetrachlorobiphenyl
- jostii
-
2,2\'-dichlorobiphenyl
- pnomenusa
-
polychlorobiphenyls
-
chlorobenzoates
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.12.18
-
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RECOMMENDED NAME
GeneOntology No.
biphenyl 2,3-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biphenyl + NADH + H+ + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
with chlorinated biphenyls the product is 2,3-dihydroxybiphenyl and HCl
-
biphenyl + NADH + H+ + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
with chlorinated biphenyls the product is 2,3-dihydroxybiphenyl and HCl
-
-
biphenyl + NADH + H+ + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating)
Requires Fe2+. The enzyme from Burkholderia fungorum LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).
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CAS REGISTRY NUMBER
COMMENTARY
103289-55-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large subunit fragment; uncultured soil bacterium
A5YWJ0, A5YWJ1, A5YWJ2, A5YWJ3, A5YWJ4, A5YWJ5, A5YWJ6, A5YWJ7, A5YWJ8, A5YWJ9, A5YWK0, A5YWK1, A5YWK2, A5YWK3, A5YWK4, A5YWK5, A5YWK6
UniProt
strain LB400, hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain LB400 bphA with the homologous gene of Comamonas testosteroni B-356
-
-
strain B-356, hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain LB400 bphA with the homologous gene of Comamonas testosteroni B-356
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls; biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls
metabolism
-
BPDO is one of the most potent biocatalysts of natural origin for the dioxygenation of chlorobiphenyls
physiological function
-
catalyzes critical steps of the bacterial polychlorinated biphenyl degrading pathway. Transgenic plants cotransformed with pGreenbphA + bphE + bphG + pGreen-bphF do not produce the three enzyme components simultaneously. Frequency of viable plants among transformants is low, thus simultaneous expression of all four BPDO genes in transgenic tobacco is hampered by genetic or physiological reasons
physiological function
-
catalyzes critical steps of the bacterial polychlorinated biphenyl degrading pathway
additional information
-
the multicomponent enzyme consists of small and large subunits of the oxygenase component, and ferredoxin and reductase components
additional information
-
the multicomponent enzyme consists of small and large subunits of the oxygenase component, and ferredoxin and reductase components forming a redox chain in the overall reaction, overview
additional information
-
the alpha-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase directly influences catalytic activities and substrate specificity, three-dimensional model of LY402-BphA1, overview. The number and subposition of chlorine substituents influence the polychlorinated biphenyls binding ability of BphA1 significantly. Ser283, Val287, Gly321 and Tyr384 residues in the active site of LY402-BphA1 show high variability, and the space limitation of the active site of BphA1 have negative influence on the polychlorinated biphenyls binding affinity of the enzyme
additional information
-
the alpha-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase directly influences catalytic activities and substrate specificity, three-dimensional model of LY402-BphA1, overview. The number and subposition of chlorine substituents influence the polychlorinated biphenyls binding ability of BphA1 significantly. Ser283, Val287, Gly321 and Tyr384 residues in the active site of LY402-BphA1 show high variability, and the space limitation of the active site of BphA1 have negative influence on the polychlorinated biphenyls binding affinity of the enzyme
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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
(3R,4R)-cis-isoflavan-4-ol + NADH + H+ + O2
(3R,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
(3R,4S)-trans-isoflavan-4-ol + NADH + H+ + O2
(3R,4S)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
(3S,4R)-trans-isoflavan-4-ol + NADH + H+ + O2
(3S,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
(3S,4S)-cis-isoflavan-4-ol + NADH + H+ + O2
(3S,4S)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
2,2',3,3'-tetrachlorobiphenyl + NADH + H+ + O2
5,6-dihydro-5,6-dihydroxy-2,2',3,3'-tetrachlorobiphenyl + 4,5-dihydro-4,5-dihydroxy-2,2',3,3'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,2',5,5'-tetrachlorobiphenyl + NADH + H+ + O2
3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + cis-3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + NAD+
-
poor substrate
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
2,2'-difluorobiphenyl + NADH + O2
2,3-dihydroxy-2'-fluorobiphenyl + 5,6-dihydroxy-2,2'-difluorobiphenyl + NAD+ + HF
2,3'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 4-chloro-3-(3-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 5-chloro-3-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol
2,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-3'-chlorobiphenyl + 5',6'-dihydroxy-1'-phenylcyclohexa-1',3'-diene + NAD+ + HCl
-
-
-
-
?
2,3,2',3'-tetrachlorobiphenyl + NADH + H+ + O2
4,5-dihydro-4,5-dihydroxy-2,3,2',3'-tetrachlorobiphenyl + NAD+
-
oxygenated onto meta-para carbons 4 and 5
-
-
?
2,3,2',3'-tetrachlorobiphenyl + NADH + H+ + O2
cis-4,5-dihydro-4,5-dihydroxy-2,3,2',3'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,4',5-trichlorobiphenyl + NADH + H+ + O2
3,4-dihydro-3,4-dihydroxy-2,5,4'-trichlorobiphenyl + 2',3'-dihydro-2',3'-dihydroxy-2,5,4'-trichlorobiphenyl + NAD+
-
-
-
-
?
2,4,2',4'-tetrachlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+ + HCl
-
oxygenated principally onto vicinal ortho-meta carbons 2 and 3
-
-
?
2,4,4'-trichlorobiphenyl + NADH + H+ + O2
2,3-dihydro-2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+
2,5,2',5'-tetrachlorobiphenyl + NADH + O2
cis-3,4-dihydroxy-2,5-dichloro-1-[2',5'-dichlorophenyl]-cyclohexa-1,5-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
2,5,2'-trichlorobiphenyl + NADH + O2
cis-3,4-dihydroxy-2,5-dichloro-1-[2'-chlorophenyl]-cyclohexa-1,5-diene + 2',3'-dihydroxy-2,5-dichlorobiphenyl + 5',6'-dihydrodiol + NAD+ + HCl
-
-
-
-
?
2,5,3'-trichlorobiphenyl + NADH + O2
3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + 5',6'-dihydroxy-1'-phenylcyclohexa-1',3'-diene + 2,3-catechol + NAD+ + HCl
-
-
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
2,6-dichlorobiphenyl + NADH + H+ + O2
2,6-dichloro-2',3'-dihydro-2',3'-dihydroxybiphenyl + ?
2-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2-chlorophenyl)-cyclohexa-4',6'-diene + catechol + NAD+
2-hydroxy-3-chlorobiphenyl + NADH + H+ + O2
5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one + NAD+
2-hydroxy-5-chlorobiphenyl + NADH + H+ + O2
cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl + 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-one + 2,2'-dihydroxy-5-chlorobiphenyl + 2,3'-dihydroxy-5-chlorobiphenyl + NAD+
3,3'-dichlorobiphenyl + NADH + H+ + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
3,4'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(4-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 3-chloro-6-(3-chlorophenyl)cyclohexa-3,4-diene-1,2-diol
3-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(3-chlorophenyl)-cyclohexa-4',6'-diene + NAD+
4,4'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD+
-
-
-
?
4-methylbiphenyl + NADH + O2
2-hydroxy-6-oxo-6-[4-methylphenyl]-hexa-2,4-dienoic acid + NAD+
5,7-dihydroxyflavone + NADH + H+ + O2
2-(2,3-dihydroxyphenyl)-5,7-dihydroxy-chromen-4-one + NAD+
6,7-dihydro-5H-benzocycloheptene + NAD(P)H + O2
(-)-cis-(1R,2S)-dihydroxybenzocycloheptane + NAD(P)+
benzene + ?
?
-
benzene is only a substrate for Pseudomonas pseudoalcaligenes strain 1072
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ + ?
-
-
-
-
?
biphenyl + NADH + H+ + O2
cis-(2R,3S)-dihydroxy-1-phenylcyclohexa-4,6-diene + NAD+
-
-
-
-
?
dibenzo-p-dioxine + NADH + O2
2,3,2'-trihydroxy-diphenylether + dibenzo-p-dioxine-dihydrodiol + NAD+
-
-
-
-
?
dibenzofuran + NADH + O2
?
-
dibenzofuran is a poor substrate
-
-
?
dibenzofurane + NADH + O2
2,2',3-trihydroxybiphenyl + dihydro-dihydroxy-dibenzofuran + NAD+
dibenzofurane + NADH + O2
monohydroxydibenzofuran + 2,3,2'-trihydroxybiphenyl + dibenzofuran-1,2-dihydrodiol + dibenzofuran-3,4-dihydrodiol + NAD+
-
-
-
-
?
flavone + O2 + NAD(P)H
cis-flavone-2',3'-dihydrodiol + ?
-
-
-
-
?
isoflavone + NADH + H+ + O2
isoflavone-cis-(2'R,3'S)-dihydrodiol + NAD+
-
-
-
-
?
toluene + NAD(P)H + O2
?
-
toluene is only a substrate for Pseudomonas pseudoalcaligenes strain 1072
-
-
?
(3R,4R)-cis-isoflavan-4-ol + NADH + H+ + O2
(3R,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
(3R,4R)-cis-isoflavan-4-ol + NADH + H+ + O2
(3R,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
(3R,4S)-trans-isoflavan-4-ol + NADH + H+ + O2
(3R,4S)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
(3R,4S)-trans-isoflavan-4-ol + NADH + H+ + O2
(3R,4S)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
(3S,4R)-trans-isoflavan-4-ol + NADH + H+ + O2
(3S,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
(3S,4R)-trans-isoflavan-4-ol + NADH + H+ + O2
(3S,4R)-3-(7-oxabicyclo[4.1.0]hepta-1,3,5-trien-2-yl)-3,4-dihydro-2H-chromen-4-ol + NAD+
-
-
-
-
?
2,2'-dibromobiphenyl + NADH + O2
2,3-dihydroxy-2'-bromobiphenyl + NAD+ + HBr
-
-
-
-
?
2,2'-dibromobiphenyl + NADH + O2
2,3-dihydroxy-2'-bromobiphenyl + NAD+ + HBr
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
-
-
the ratio of 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme, 40/60 for the mutant enzymes T335A/F336M, T335A/F336L/I341V and T335A/F336I,80/20 for mutant enzyme T335G, 85/15 for the mutant enzymes T335A and T335A/F336L
-
?
2,2'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-difluorobiphenyl + NADH + O2
2,3-dihydroxy-2'-fluorobiphenyl + 5,6-dihydroxy-2,2'-difluorobiphenyl + NAD+ + HF
-
-
-
-
?
2,2'-difluorobiphenyl + NADH + O2
2,3-dihydroxy-2'-fluorobiphenyl + 5,6-dihydroxy-2,2'-difluorobiphenyl + NAD+ + HF
-
-
-
-
?
2,2'-dihydroxybiphenyl + NADH + O2
2,3,2'-trihydroxybiphenyl + trihydroxybiphenyl + NAD+
-
-
-
-
?
2,2'-dihydroxybiphenyl + NADH + O2
2,3,2'-trihydroxybiphenyl + trihydroxybiphenyl + NAD+
-
-
-
-
?
2,2'-dinitrobiphenyl + NADH + O2
2,3-dihydroxy-2'-nitrobiphenyl + NAD+ + NO2
-
-
-
-
?
2,2'-dinitrobiphenyl + NADH + O2
2,3-dihydroxy-2'-nitrobiphenyl + NAD+ + NO2
-
-
-
-
?
2,3'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 4-chloro-3-(3-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 5-chloro-3-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol
-
-
-
-
?
2,3'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 4-chloro-3-(3-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 5-chloro-3-(2-chlorophenyl)cyclohexa-3,5-diene-1,2-diol
-
-
-
-
?
2,4'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-4'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,4'-dichlorobiphenyl + NADH + O2
2,3-dihydroxy-4'-chlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,4,4'-trichlorobiphenyl + NADH + H+ + O2
2,3-dihydro-2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+
-
-
-
-
?
2,4,4'-trichlorobiphenyl + NADH + H+ + O2
2,3-dihydro-2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+
-
-
-
-
?
2,5,2',5'-tetrachlorobiphenyl + NADH + O2
cis-3,4-dihydroxy-2,5-dichloro-1-[2',5'-dichlorophenyl]-cyclohexa-1,5-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,5,2',5'-tetrachlorobiphenyl + NADH + O2
cis-3,4-dihydroxy-2,5-dichloro-1-[2',5'-dichlorophenyl]-cyclohexa-1,5-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
no 3,4-dihydrodiol as product
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,5-dichlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2,5-dichlorophenyl)-cyclohexa-4',6'-diene + 3,4-dihydroxy-1-phenylcyclohexa-1,5-diene + NAD+ + HCl
-
-
-
-
?
2,6-dichlorobiphenyl + NADH + H+ + O2
2,6-dichloro-2',3'-dihydro-2',3'-dihydroxybiphenyl + ?
-
-
-
-
?
2,6-dichlorobiphenyl + NADH + H+ + O2
2,6-dichloro-2',3'-dihydro-2',3'-dihydroxybiphenyl + ?
-
-
-
-
?
2-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2-chlorophenyl)-cyclohexa-4',6'-diene + catechol + NAD+
-
-
-
-
?
2-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2-chlorophenyl)-cyclohexa-4',6'-diene + catechol + NAD+
-
-
-
-
?
2-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2-chlorophenyl)-cyclohexa-4',6'-diene + catechol + NAD+
-
no catechol formation
-
-
?
2-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(2-chlorophenyl)-cyclohexa-4',6'-diene + catechol + NAD+
-
no catechol formation
-
-
?
2-hydroxy-3,5-dichlorobiphenyl + NADH + H+ + O2
?
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
-
-
?
2-hydroxy-3,5-dichlorobiphenyl + NADH + H+ + O2
?
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
-
-
?
2-hydroxy-3,5-dichlorobiphenyl + NADH + H+ + O2
?
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
-
-
?
2-hydroxy-3-chlorobiphenyl + NADH + H+ + O2
5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
+ minor amounts of dihydroxybiphenyl, generated by the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and 2-hydroxy-3-chloro-2',3'-dihydroxybiphenyl. 5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one is likely generated from the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl
-
?
2-hydroxy-3-chlorobiphenyl + NADH + H+ + O2
5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
+ minor amounts of dihydroxybiphenyl, generated by the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and 2-hydroxy-3-chloro-2',3'-dihydroxybiphenyl. 5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one is likely generated from the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl
-
?
2-hydroxy-3-chlorobiphenyl + NADH + H+ + O2
5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
+ minor amounts of dihydroxybiphenyl, generated by the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl and 2-hydroxy-3-chloro-2',3'-dihydroxybiphenyl. 5-(3-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexen-1-one is likely generated from the rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-3'-chlorobiphenyl
-
?
2-hydroxy-5-chlorobiphenyl + NADH + H+ + O2
cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl + 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-one + 2,2'-dihydroxy-5-chlorobiphenyl + 2,3'-dihydroxy-5-chlorobiphenyl + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl are also found as well as 2-hydroxy-5-chloro-2',3'-dihydroxybiphenyl which is most likely generated by spontaneous rearrangement and dehydrogenation of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-oneis likely to be generated from rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 2,2'-Dihydroxy-5-chlorobiphenyl and 2,3'-dihydroxy-5-chlorobiphenyl are also generated by the loss of OH and rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl
-
?
2-hydroxy-5-chlorobiphenyl + NADH + H+ + O2
cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl + 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-one + 2,2'-dihydroxy-5-chlorobiphenyl + 2,3'-dihydroxy-5-chlorobiphenyl + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl are also found as well as 2-hydroxy-5-chloro-2',3'-dihydroxybiphenyl which is most likely generated by spontaneous rearrangement and dehydrogenation of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-oneis likely to be generated from rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 2,2'-Dihydroxy-5-chlorobiphenyl and 2,3'-dihydroxy-5-chlorobiphenyl are also generated by the loss of OH and rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl
-
?
2-hydroxy-5-chlorobiphenyl + NADH + H+ + O2
cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl + 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-one + 2,2'-dihydroxy-5-chlorobiphenyl + 2,3'-dihydroxy-5-chlorobiphenyl + NAD+
-
ortho-meta-oxygenation, hydroxylation on the non-substituted ring
minor amounts of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl are also found as well as 2-hydroxy-5-chloro-2',3'-dihydroxybiphenyl which is most likely generated by spontaneous rearrangement and dehydrogenation of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 5-(5-chloro-2-hydroxyphenyl)-6-hydroxy-3-cyclohexene-1-oneis likely to be generated from rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl. 2,2'-Dihydroxy-5-chlorobiphenyl and 2,3'-dihydroxy-5-chlorobiphenyl are also generated by the loss of OH and rearrangement of cis-2,3-dihydro-2,3-dihydroxy-2'-hydroxy-5'-chlorobiphenyl
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
poor substrate
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
3,4'-dichlorobiphenyl + NAD(P)H + O2
5,6-dihydroxy-3,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
3,4'-dichlorobiphenyl + NAD(P)H + O2
5,6-dihydroxy-3,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
3,4'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(4-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 3-chloro-6-(3-chlorophenyl)cyclohexa-3,4-diene-1,2-diol
-
-
-
-
?
3,4'-dichlorobiphenyl + NADH + H+ + O2
3-chloro-5-(4-chlorophenyl)cyclohexa-3,5-diene-1,2-diol + 3-chloro-6-(3-chlorophenyl)cyclohexa-3,4-diene-1,2-diol
-
-
-
-
?
3-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(3-chlorophenyl)-cyclohexa-4',6'-diene + NAD+
-
-
-
-
?
3-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(3-chlorophenyl)-cyclohexa-4',6'-diene + NAD+
-
-
-
-
?
3-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(3-chlorophenyl)-cyclohexa-4',6'-diene + NAD+
-
-
-
-
?
3-chlorobiphenyl + NADH + O2
cis-2',3'-dihydroxy-1'-(3-chlorophenyl)-cyclohexa-4',6'-diene + NAD+
-
-
-
-
?
4,4'-dichlorobiphenyl + NAD(P)H + O2
2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
4,4'-dichlorobiphenyl + NAD(P)H + O2
2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
4,4'-dichlorobiphenyl + NAD(P)H + O2
2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
4,4'-dichlorobiphenyl + NAD(P)H + O2
2,3-dihydroxy-4,4'-dichlorobiphenyl + NAD(P)+
-
-
-
-
?
4-chlorobiphenyl + NADH + O2
2',3'-dihydrodiol-4-chlorobiphenyl + NAD+
-
-
-
-
?
4-chlorobiphenyl + NADH + O2
2',3'-dihydrodiol-4-chlorobiphenyl + NAD+
-
-
-
-
?
4-chlorobiphenyl + NADH + O2
2',3'-dihydrodiol-4-chlorobiphenyl + NAD+
-
-
-
-
?
4-chlorobiphenyl + NADH + O2
2',3'-dihydrodiol-4-chlorobiphenyl + NAD+
-
-
-
-
?
4-methylbiphenyl + NADH + O2
2-hydroxy-6-oxo-6-[4-methylphenyl]-hexa-2,4-dienoic acid + NAD+
-
-
-
-
?
4-methylbiphenyl + NADH + O2
2-hydroxy-6-oxo-6-[4-methylphenyl]-hexa-2,4-dienoic acid + NAD+
-
-
-
-
?
5,7-dihydroxyflavone + NADH + H+ + O2
2-(2,3-dihydroxyphenyl)-5,7-dihydroxy-chromen-4-one + NAD+
-
BphA1 (1-22) and BphA1 (2-2), expression of the mutants in together with bphA2A3A4B from strain KF707
-
-
?
5,7-dihydroxyflavone + NADH + H+ + O2
2-(2,3-dihydroxyphenyl)-5,7-dihydroxy-chromen-4-one + NAD+
-
BphA1 (1-22) and BphA1 (2-2), expression of the mutants in together with bphA2A3A4B from strain KF707
-
-
?
6,7-dihydro-5H-benzocycloheptene + NAD(P)H + O2
(-)-cis-(1R,2S)-dihydroxybenzocycloheptane + NAD(P)+
-
-
-
-
?
6,7-dihydro-5H-benzocycloheptene + NAD(P)H + O2
(-)-cis-(1R,2S)-dihydroxybenzocycloheptane + NAD(P)+
-
-
-
-
?
7-hydroxyflavone + NADH + H+ + O2
2-(2,3-dihydroxyphenyl)-7-hydroxy-chromen-4-one + NAD+
-
BphA1 (1-22) and BphA1 (2-2), expression of the mutants together with bphA2A3A4B from strain KF707
-
-
?
7-hydroxyflavone + NADH + H+ + O2
2-(2,3-dihydroxyphenyl)-7-hydroxy-chromen-4-one + NAD+
-
BphA1 (1-22) and BphA1 (2-2), expression of the mutants together with bphA2A3A4B from strain KF707
-
-
?
biphenyl + NAD(P)H + O2
(1S,2R)-dihydroxy-3-phenylcyclohexa-3,5-diene + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
(1S,2R)-dihydroxy-3-phenylcyclohexa-3,5-diene + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
2,3-dihydro-dihydroxybiphenyl + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
2,3-dihydro-dihydroxybiphenyl + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
2,3-dihydro-dihydroxybiphenyl + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
-
?
biphenyl + NADH + O2
cis-biphenyl 2,3-dihydrodiol + NAD+
-
-
-
-
?
carbazole + NADH + O2
3-hydroxycarbazole + NAD+
-
no products with carbazole detected
-
-
-
carbazole + NADH + O2
3-hydroxycarbazole + NAD+
-
no products with carbazole detected
-
-
-
carbazole + NADH + O2
3-hydroxycarbazole + NAD+
-
formation of an unstable cis-carbazole-3,4-dihydrodiol is proposed
-
-
?
carbazole + NADH + O2
3-hydroxycarbazole + NAD+
-
formation of an unstable cis-carbazole-3,4-dihydrodiol is proposed
-
-
?
dibenzo-p-dioxin + NADH + O2
2,2',3-trihydroxybiphenyl ether + NAD+
-
-
-
-
?
dibenzo-p-dioxin + NADH + O2
2,2',3-trihydroxybiphenyl ether + NAD+
-
-
-
-
?
dibenzofurane + NADH + O2
2,2',3-trihydroxybiphenyl + dihydro-dihydroxy-dibenzofuran + NAD+
-
-
+ small amounts of 2,2',3-trihydroxybiphenyl. 2,2',3-dihydroxybiphenyl results from angular oxygenation, dihydro-dihydroxy-dibenzofuran results from lateral oxygenation
-
?
dibenzofurane + NADH + O2
2,2',3-trihydroxybiphenyl + dihydro-dihydroxy-dibenzofuran + NAD+
-
-
+ small amounts of 2,2',3-trihydroxybiphenyl. 2,2',3-dihydroxybiphenyl results from angular oxygenation, dihydro-dihydroxy-dibenzofuran results from lateral oxygenation
-
?
flavone + O2 + NADH + H+
cis-flavone-2',3'-dihydrodiol + ?
-
the flavone metabolite is 2-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-4H-chromen-4-one
-
-
?
flavone + O2 + NADH + H+
cis-flavone-2',3'-dihydrodiol + ?
-
the flavone metabolite is 2-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-4H-chromen-4-one
-
-
?
isoflavone + O2 + NADH + H+
2',3'-dihydro-2',3'-cis-dihydroxyflavone + NAD+
-
biphenyl dioxygenase induces 2',3'-cis-dihydroxylation of the B-ring of isoflavone, the isoflavone metabolite is 3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-4H-chromen-4-one
-
-
?
isoflavone + O2 + NADH + H+
2',3'-dihydro-2',3'-cis-dihydroxyflavone + NAD+
-
biphenyl dioxygenase induces 2',3'-cis-dihydroxylation of the B-ring of isoflavone, the isoflavone metabolite is 3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-4H-chromen-4-one
-
-
?
naphthalene + NADPH + O2
cis-naphthalene 1,2-dihydrodiol + NADP+
-
poor substrate
-
-
?
naphthalene + NADPH + O2
cis-naphthalene 1,2-dihydrodiol + NADP+
-
poor substrate
-
-
?
phenazine + NADH + H+ + O2
1,2-dihydro-1,2-dihydroxyphenazine + NAD+
-
-
-
-
?
phenazine + NADH + H+ + O2
1,2-dihydro-1,2-dihydroxyphenazine + NAD+
-
-
-
-
?
additional information
?
-
-
enzyme of biphenyl catabolic pathway
-
-
-
additional information
?
-
-
no activity with 4,4'-dichlorobiphenyl and 2,2',5,5'-tetrachlorobiphenyl
-
-
-
additional information
?
-
-
the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview
-
-
-
additional information
?
-
-
the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview
-
-
-
additional information
?
-
-
no activity on toluene and benzene
-
-
-
additional information
?
-
-
biphenyl pathway of strain LB400 oxidizes an unusually wide range of polychlorinated biphenyl congeners and BphA is able to dihydroxylate from mono-chlorobiphenyls to 2,3,4,5,2',5'-hexachlorobiphenyl, is able to oxidize other substituted biphenyls, unsubstituted dibenzofuran and dibenzodioxin and is also able to transform different isoflavonoids. A hybrid BphA based on the LB400 enzyme but harboring the core segment of an oxygenase from Pseudomonas sp. strain B4-Magdeburg shows (depending on the congener considered) complementing or improved degradative properties. BphA mutants with increased catalytic turnover on polychlorinated biphenyls, that are recalcitrant for the parental BphA from strain LB400
-
-
-
additional information
?
-
-
overview on polychlorinated biphenyls
-
-
-
additional information
?
-
-
the enzyme also shows monooxygenase activity by converting 2(R)- and 2(S)-flavanone to their corresponding epoxides, whereby the epoxide bond is formed between C2' and C3' on the B ring of the flavanone
-
-
-
additional information
?
-
-
the enzyme does not produce metabolites from 2'-hydroxyflavanone, 3'-hydroxyflavanone, and naringenin
-
-
?
additional information
?
-
-
BDO shows stereoselective preference to the stereoisomers of isoflavan-4-ol in the order (3S,4S)-cis-isoflavan-4-ol > (3R,4S)-transisoflavan-4-ol > (3S,4R)-trans-isoflavan-4-ol > (3R,4R)-cisisoflavan-4-ol
-
-
-
additional information
?
-
-
overview on polychlorinated biphenyls
-
-
-
additional information
?
-
-
the enzyme also shows monooxygenase activity by converting 2(R)- and 2(S)-flavanone to their corresponding epoxides, whereby the epoxide bond is formed between C2' and C3' on the B ring of the flavanone
-
-
-
additional information
?
-
-
the enzyme does not produce metabolites from 2'-hydroxyflavanone, 3'-hydroxyflavanone, and naringenin
-
-
?
additional information
?
-
-
BDO shows stereoselective preference to the stereoisomers of isoflavan-4-ol in the order (3S,4S)-cis-isoflavan-4-ol > (3R,4S)-transisoflavan-4-ol > (3S,4R)-trans-isoflavan-4-ol > (3R,4R)-cisisoflavan-4-ol
-
-
-
additional information
?
-
-
trans-chalcone is converted into 3-(2,3-dihydroxyphenyl)-1-phenylpropan-1-one and further into 1,3-bis-(2,3-dihydroxyphenyl)-propan-1-one
-
-
-
additional information
?
-
-
trans-chalcone is converted into 3-(2,3-dihydroxyphenyl)-1-phenylpropan-1-one and further into 1,3-bis-(2,3-dihydroxyphenyl)-propan-1-one
-
-
-
additional information
?
-
-
no substrates are benzene, toluene, 2,5-dichlorotoluene, carbazole and dibenzothiophene
-
-
-
additional information
?
-
-
overview on polychlorinated biphenyls
-
-
-
additional information
?
-
-
overview on polychlorinated biphenyls
-
-
-
additional information
?
-
-
no substrates are benzene, toluene, 2,5-dichlorotoluene, carbazole and dibenzothiophene
-
-
-
additional information
?
-
-
overview on polychlorinated biphenyls
-
-
-
additional information
?
-
-
Phe378 and Phe384 are near the substrate inside the catalytic pocket and thus likely interact with it
-
-
-
additional information
?
-
-
biphenyl 2,3-dioxygenase is responsible for the ability of Sphingobium yanoikuyae strain B1 to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene
-
-
-
additional information
?
-
-
a single multicomponent dioxygenase enzyme is involved in the initial oxidation of both biphenyl and naphthalene in Sphingobium yanoikuyae strain B1
-
-
-
additional information
?
-
-
biphenyl 2,3-dioxygenase is responsible for the ability of Sphingobium yanoikuyae strain B1 to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene
-
-
-
additional information
?
-
-
a single multicomponent dioxygenase enzyme is involved in the initial oxidation of both biphenyl and naphthalene in Sphingobium yanoikuyae strain B1
-
-
-
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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
biphenyl + NADH + H+ + O2
cis-(2R,3S)-dihydroxy-1-phenylcyclohexa-4,6-diene + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
P37333, P37334
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
S5GDK5
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
P37333, P37334
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
-
?
additional information
?
-
-
enzyme of biphenyl catabolic pathway
-
-
-
additional information
?
-
-
the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview
-
-
-
additional information
?
-
-
the strain LY402 shows polychlorinated biphenyls degradation abilities of BphA1, molecular simulation and ligand docking studies, overview
-
-
-
additional information
?
-
-
biphenyl 2,3-dioxygenase is responsible for the ability of Sphingobium yanoikuyae strain B1 to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene
-
-
-
additional information
?
-
-
biphenyl 2,3-dioxygenase is responsible for the ability of Sphingobium yanoikuyae strain B1 to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
-
exogenous ferrous iron is required for maximal activity, the oxygenase component contains 2.43 g/mol iron, the ferredoxin component contains 2.1 g/mol iron
Fe2+
-
contains a [2Fe-2S] Rieske-type center carrying a mononuclear Fe2+
Fe2+
coordination geometry of Fe-ion along with the oxygen and different polychlorinated biphenyl congeners
Fe2+
-
omission of ferrous ammonium sulfate reduces specific activity of purified ISP 7.4fold
Fe2+
-
one Fe+ and one [Fe2-S2] cluster in the large subunit, as well as one [Fe2-S2] cluster in the small subunit of the enzyme complex
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different bacterial community structures and abundance of BPH genes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.156
NADPH
-
recombinant, purified NADH: ferredoxin oxidoreductase component
0.0108
ethylbenzene
-
Pseudomonas pseudoalcaligenes strain 1072
0.0236
ethylbenzene
-
Pseudomonas pseudoalcaligenes strain KF707
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0497
ethylbenzene
-
Pseudomonas pseudoalcaligenes strain KF707
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.15
-
referred to iron sulfur protein (terminal oxygenase) after purification
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
from second most abundant taxon present in the horseradish rhizosphere
additional information
-
indigenous bacteria from polychlorinated biphenyl-contaminated River Raisin sediment. 31.8 kb cosmid clone, detected by aromatic dioxygenase primers, contains genes of biphenyl dioxygenase subunits bphAE, while the rest of the clone's sequence is similar to that of an unknown member of the Gammaproteobacteria
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
additional information
-
from bacterium, that dominates biphenyl metabolism in the horseradish rhizosphere soil
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
additional information
-
from predominant biphenyl-utilizing bacteria in the initial bulk soil
additional information
microbial community of a polychlorinated biphenyl-polluted soil
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
-
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
-
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
-
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
additional information
-
from bacterium present in the horseradish rhizosphere
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
-
native, recombinant and purified alpha subunit with His-tag, HPLC gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterohexamer
heterotetramer
heterotrimer
additional information
?
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
construction of a three-dimensional model of alpha-subunit of biphenyl dioxygenase (BphA). BphA active site is composed of two domains, the catalytic domain (residues 1-58 and 176-457) and the Rieske domain (residues 59–166). The active site pocket, which is lined mostly by hydrophobic residues (Phe227, Trp390, Phe 376, Asp386, Phe382 and Ala234) is located between the core beta-sheet and alpha-helices in the catalytic domain of the alpha-subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
?
-
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
-
?
A5YWJ0, A5YWJ1, A5YWJ2, A5YWJ3, A5YWJ4, A5YWJ5, A5YWJ6, A5YWJ7, A5YWJ8, A5YWJ9, A5YWK0, A5YWK1, A5YWK2, A5YWK3, A5YWK4, A5YWK5, A5YWK6
diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit; diversity of the C-terminal portion of the biphenyl dioxygenase large subunit
heterohexamer
-
alpha3,beta3, 3 * 53600 + 3 * 25200, SDS-PAGE and gel filtration
heterohexamer
-
alpha3,beta3, 3 * 53000 + 3 * 27300, measurement of molecular weight and Stokes' radius with gel filtration
heterohexamer
-
alpha3,beta3, 3 * 53000 + 3 * 27300, measurement of molecular weight and Stokes' radius with gel filtration
-
heterotetramer
-
BphA1 (iron-sulfur protein large alpha subunit), BphA2 (iron-sulfur protein small beta subunit), BphA3 (ferredoxin) and BphA4 (ferredoxin reductase).
heterotetramer
-
BphA1 (iron-sulfur protein large alpha subunit), BphA2 (iron-sulfur protein small beta subunit), BphA3 (ferredoxin) and BphA4 (ferredoxin reductase).
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the BPDOB356–2,6-dichlorobiphenyl complex is determined at 2.4 A resolution
-
crystal structure of the BPDOB356/2,6-dichlorobiphenyl complex is determined at 2.4 A resolution
-
purified recombinant BPDOLB400, sitting drop vapour diffusion method, anaerobic conditions, method optimization, 0.002 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.3, containing 0.25 mM ferrous ammonium sulfate, and 2 mM dithiothreitol, is mixed with 0.002 ml of reservoir solution containing 20-25% w/v PEG 8000 or PEG 5000 MME, 50 mM PIPES, pH 6.5, 100 mM ammonium acetate, 5% v/v glycerol, and 0.2% w/v agarose, successful crystallization only occurs at pH 6.5, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution; purified recombinant BPDOLB400, sitting drop vapour diffusion method, anaerobic conditions, method optimization, 0.002 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.3, containing 0.25 mM ferrous ammonium sulfate, and 2 mM dithiothreitol, is mixed with 0.002 ml of reservoir solution containing 20-25% w/v PEG 8000 or PEG 5000 MME, 50 mM PIPES, pH 6.5, 100 mM ammonium acetate, 5% v/v glycerol, and 0.2% w/v agarose, successful crystallization only occurs at pH 6.5, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution; sitting drop vapor diffusion method, using 20-25% (w/v) PEG 8000 or PEG 5000 MME, 50 mM PIPES pH 6.5, 100 mM ammonium acetate, 5% (v/v) glycerol and 0.2% (w/v) agarose
sitting drop vapor diffusion method, using 20–25% (w/v) PEG 8000 or PEG 5000 MME, 50 mM PIPES (pH 6.5), 100 mM ammonium acetate, 5% (v/v) glycerol, and 0.2% (w/v) agarose
-
terminal oxygenase component of the biphenyl dioxygenase, BphA1A2 in substrate-free and biphenyl complex forms, cocrystallization method
hanging drop vapour diffusion method using 20% (w/v) polyethylene glycol 3350, 1 M NaCl and 0.1 M ZnCl2 at 6°C
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 55
-
NADH: ferredoxin oxidoreductase component: no activity at 5 or 55°C, 15.2% of control activity at 50°C
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
20 min preincubation of His-tagged enzyme with 5 mM dithiothreitol on ice can restore activity of older preparations
-
285287
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant His-tagged subunits alpha and beta and mutant variants from Escherichia coli strain C41 (DE3) by affinity chromatography, the tag is cleaved off by thrombin; recombinant His-tagged subunits alpha and beta and mutant variants from Escherichia coli strain C41(DE3) by affinity chromatography, the tag is cleaved off by thrombin
active BphAE and BphG copurified from Nicotiana benthamiana leaves
-
butyl-Sepharose XK26/40 column chromatography, Q-Sepharose column chromatography, and hydroxyapatite column chromatography
-
His-tagged ISP, expressed in Escherichia coli and Pseudomonas putida
-
purification from heterologous expression in Pseudomonas putida KT2442
-
Q-Sepharose FF column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
A central part (amino acid position 268-397 of 458 residues) of the biphenyl dioxygenase large alpha subunit, BphA1, from Pseudomonas pseudoalcaligenes (strain KF707) is exchanged with the corresponding part of BphA1 from Pseudomonas putida strain KF715, to construct hybrid BphA1, BphA1 (amino acid 715-707). When expressed in Escherichia coli together with the bphA2A3A4BC genes from strain KF707, this enzyme is shown to possess activity for degrading both 1-phenylnaphthalene and 2-phenylnaphthalene.
-
based on analyses with Nicotiana benthamiana plants transiently expressing the biphenyl dioxygenase genes (the two subunit oxygenase (BphAE) containing a Rieske-type iron–sulfur cluster and a mononuclear iron center, the Rieske-type ferredoxin (BphF), and the FAD-containing ferredoxin reductase (BphG)) from Burkholderia xenovorans LB400 and transgenic Nicotiana tabacum plants transformed with each of these four genes, it can be shown that each of the three biphenyl dioxygenase components can be produced individually as active protein in tobacco plants
-
expressed in Escherichia coli
expressed in Escherichia coli C41 (DE3) cells; expression of His-tagged subunits alpha and beta and mutant variants in Escherichia coli strain C41 (DE3); expression of His-tagged subunits alpha and beta and mutant variants in Escherichia coli strain C41(DE3)
expressed in Escherichia coli Top10F cells
expression in Escherichia coli
gene cluster bphAaAbAcAd, genetic organization, the multicomponent enzyme components cannot be expressed in Escherichia coli actively due to lack of activity of the ferredoxin component in Escherichia coli involving codon usage bias. Therefore hybrid BphA gene derivatives are constructed by replacing ferredoxin and/or reductase components of RHA1 with those of Pseudomonas pseudoalcaligenes strain KF707. Expression of ferredoxin encoding gene bphAc in Escherichia coli strain Rosetta (DE3) pLacI resulting in an active protein
-
genes bphAaAbAcAd, encoding the large and small subunits of the terminal oxygenase component and the ferredoxin and reductase subunits responsible for electron transfer from NADH to the large subunit. Functional expression Burkholderia sp. strain NK8 is only successful by combining the bphAaAbAcAd genes of RHA1 and bphA3A4 of Pseudomonas pseudoalcaligenes KF707, introduction of a plasmid containing the RHA1 bphAaAb and KF707 bphA3A4 genes plus the RHA1 bphB2C1D1 genes into strain NK8. The remaining enzyme genes involved in the transformation of biphenyl to benzoate, bphB2C1D1, which encodes dehydrogenase, ring-cleavage dioxygenase and hydrolase, confer activities to NK8, installation of the polychlorinated biphenyls degradation pathway, overview
-
in Escherichia coli strain M15 and SG13009; in Pseudomonas putida strain KT2442
-
in Pseudomonas putida strain KT2442
pET101[L11E10-bphAE] and pDB31[LB400-bphFGBC] cotransformed into Escherichia coli BL21 Star(DE3)
-
pET101[LB400-bphAE] and pDB31[LB400-bphFGBC] cotransformed into Escherichia coli BL21 Star(DE3)
-
the construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
the evolved bphA1 gene, in which nine amino acids from the Pseudomonas pseudoalcaligenes KF707 BphA1 are changed to those from the Burkholderia xenovorans LB400 BphA1 (M247I/H255Q/V258I/G268A/D303E/-313G/S324T/V325I/T376N), is expressed in Escherichia coli along with the bphA2A3A4 and bphB genes derived from strain KF707. This recombinant Escherichia coli cells convert biphenyl and several heterocyclic aromatic compounds into the highly hydroxylated products such as biphenyl-2,3,2',3'-tetraol (from biphenyl), 2-(2,3-dihydroxyphenyl)benzoxazole-4,5-diol (from 2-phenylbenzoxazole), and 2-(2,5-dihydroxyphenyl)benzoxazole-4,5-diol (from 2-(2-hydroxyphenyl)benzoxazole)
-
the construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
-
the construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bph gene cluster bphAaAbAcAdCB is localized on the linear plasmid pRHL1, which is followed by bphS and bphT genes which encode a two-component signal transduction system composed of a BphT response regulator and a BpdS sensor kinase and promote transcriptional induction by aromatic compounds biphenyl, benzene, alkylbenzene and chlorinated benzene
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
exposure to polychlorinated biphenyl and Aroclor 1242 results in a marked increase of two out of the four BPH genes. Exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
bph gene cluster bphAaAbAcAdCB is localized on the linear plasmid pRHL1, which is followed by bphS and bphT genes which encode a two-component signal transduction system composed of a BphT response regulator and a BpdS sensor kinase and promote transcriptional induction by aromatic compounds biphenyl, benzene, alkylbenzene and chlorinated benzene
-
bph gene cluster bphAaAbAcAdCB is localized on the linear plasmid pRHL1, which is followed by bphS and bphT genes which encode a two-component signal transduction system composed of a BphT response regulator and a BpdS sensor kinase and promote transcriptional induction by aromatic compounds biphenyl, benzene, alkylbenzene and chlorinated benzene
-
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
exposure of soil microcosms to different polychlorinated biphenyl congeners results in different expression patterns of biphenyl dioxygenase genes
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A234S
-
significant change in regiospecificity of substrate dioxygenation, factor 2.3
F378A
-
very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
F384A
-
very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
M231A
-
very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
T335G/F336I/N338T/I341T
-
relaxation of the enzyme towards polychlorinated biphenyls. Wild-type enzyme shows less than 10% degradation with 2,6-dichlorobiphenyl, 3,3'-dichlorobiphenyl, 4,4'-dichlorobiphenyl, 2,3',4'-trichlorobiphenyl - the mutant enzyme enzyme shows 45 to 99% depletion depending on the substrate. Wild-type enzyme shows no degradation of 2,4,4'-trichlorobiphenyl, mutant enzyme shows 44% depletion
A234S
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significant change in regiospecificity of substrate dioxygenation, factor 2.3
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M231A
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very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
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T335G/F336I/N338T/I341T
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relaxation of the enzyme towards polychlorinated biphenyls. Wild-type enzyme shows less than 10% degradation with 2,6-dichlorobiphenyl, 3,3'-dichlorobiphenyl, 4,4'-dichlorobiphenyl, 2,3',4'-trichlorobiphenyl - the mutant enzyme enzyme shows 45 to 99% depletion depending on the substrate. Wild-type enzyme shows no degradation of 2,4,4'-trichlorobiphenyl, mutant enzyme shows 44% depletion
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N348H
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wild-type enzyme shows less than 10% activity with 2,6-dichlorobiphenyl, 4,4'-dichlorobiphenyl - mutant enzyme shows about 55% depletion. Wild-type enzyme shows no degradation of 2,4,4'-trichlorobiphenyl and 2,2',5,5'-tetrachlorobiphenyl - mutant enzyme shows 50% and 92% depletion
N348H/A404V
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wild-type enzyme shows less than 10% activity with 2,6-dichlorobiphenyl, 4,4'-dichlorobiphenyl - mutant enzyme shows about 55% depletion. Wild-type enzyme shows no degradation of 2,4,4'-trichlorobiphenyl and 2,2',5,5'-tetrachlorobiphenyl - mutant enzyme shows 29% and 84% depletion
T375N
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conversion of sequence to corresponding sequence of Pseudomonas sp. strain LB400
F336M
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the mutant produces principally 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl from 2,2'-dichlorobiphenyl
F370Y
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lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
L283S
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lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
M237T
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lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
S238T
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lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
T335A
T335A/F336I
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336L
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 85/15 for the mutant enzymes
T335A/F336L/I341V
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336M
T335G
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 80/20 for the mutant enzymes
T377N
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lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
H255Q/V258I/G268A/F277Y
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mutant of the bphA1 gene encoding the large subunit, that is responsible for substrate specificity, extremely enhanced benzene-, toluene-, and alkylbenzene-degrading ability
I335F/T376N
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does not show any significant difference in the oxidation of biphenyl compared with wild type Bph Dox, and exhibits 2,3-dioxygenase activity for 2,2'-dichlorobiphenyl and 3,4-dioxygenase activity for 2,5,4'-trichlorobiphenyl
T376F
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376K
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376N
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376V
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
H255Q/V258I/G268A/F277Y
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mutant of the bphA1 gene encoding the large subunit, that is responsible for substrate specificity, extremely enhanced benzene-, toluene-, and alkylbenzene-degrading ability
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T376F
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
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T376K
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
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T376N
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
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T376V
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shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
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T335A/F336T/N338T/I341T
additional information
T335A
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 85/15 for the mutant enzymes
T335A
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the mutant yields 2,3-dihydroxy-2,2'chlorobiphenyl as the major metabolite from 2,2'-dichlorobiphenyl
T335A/F336M
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the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336M
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the mutant metabolizes 2,2'-dichlorobiphenyl better than the wild type enzyme to generate principally 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl instead of 2,3-dihydroxy-2'-chlorobiphenyl as produced by the wild type enzyme, the mutant produces 3',4'-dihydroxy-3',4'-dihydro-2,6-dichlorobiphenyl as a major metabolite from 2,6-dichlorobiphenyl
T335A/F336T/N338T/I341T
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conversion of sequence to corresponding sequence of Pseudomonas pseudoalcaligenes strain KF707
T335A/F336T/N338T/I341T
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conversion of sequence to corresponding sequence of Pseudomonas pseudoalcaligenes strain KF707
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additional information
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characterization of hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain Comamonas testosteroni LB400 bphA with the homologous gene of Comamonas testosteroni B-356. The C-terminal portion of Burkholderia sp. LB400 alpha-subunit can withstand extensive structural modifications, and that these modifications can change the catalytic properties of the enzyme. Exchanging the C-terminal portion of Comamonas testosteroni B-356 BPDO alpha-subunit with that of Burkholderia sp. LB400 alpha-subunit generates inactive chimeras
additional information
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generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
additional information
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generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
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additional information
-
characterization of hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain Comamonas testosteroni LB400 bphA with the homologous gene of Comamonas testosteroni B-356. The C-terminal portion of Burkholderia sp. LB400 alpha-subunit can withstand extensive structural modifications, and that these modifications can change the catalytic properties of the enzyme. Exchanging the C-terminal portion of Comamonas testosteroni B-356 BPDO alpha-subunit with that of Burkholderia sp. LB400 alpha-subunit generates inactive chimeras
additional information
-
generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
additional information
-
generation of 8 chimeric enzyme systems that each consists of a hybrid hydroxylase alpha subunit (BphA1) containing segments from Burkholderia sp. strain LB400 and Rhodococcus globerulus P6, and of a hydroxylase beta subunit (BphA2), a ferredoxin (BphA3) and a ferredoxin reductase (BphA4) from strain LB400. All hybrid bphA1 genes are expressed at high levels. Seven of the resulting fusion subunits functionally interacts with the other polypeptides of the dioxygenase system to yield catalytically active enzymes.The construction of appropriate hybrid genes may be used as a general strategy to overcome problems in obtaining heterologous biphenyl dioxygenase activities in Escherichia coli or other host organisms
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additional information
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construction of sets of BphA genes by combining the bphAaAbAcAd genes of RHA1 and bphA3A4 of Pseudomonas pseudoalcaligenes KF707, encoding the ferredoxin and reductase subunits, to obtain the BphA activity of RHA1 in chlorobenzoate-degrading Burkholderia sp. strain NK8, which has an insertion in the cbeA gene to inactivate CBA dioxygenase. Hybrid derivatives of BphA containing the KF707 bphA3 confer BphA activity to NK8, and a derivative containing the RHA1 bphAaAb and KF707 bphA3A4 genes exhibit the highest BphA activity. A plasmid containing the RHA1 bphAaAb and KF707 bphA3A4 genes plus the RHA1 bphB2C1D1 genes is constructed and introduced into strain NK8
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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cis-2',3'-dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
synthesis
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cis-2',3'-dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
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