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Information on EC 1.14.12.18 - biphenyl 2,3-dioxygenase
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1.14.12.18 biphenyl 2,3-dioxygenaseIUBMB Comments
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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Word Map
- 1.14.12.18
- biphenyls
-
polychlorinated
- pseudoalcaligenes
- xenovorans
-
dioxygenation
- testosteroni
-
rieske-type
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chlorobiphenyls
-
pcb-degrading
-
bpdos
- comamonas
-
dihydrodiols
-
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
- yanoikuyae
-
biphenyl-degrading
- 2,3-dihydroxybiphenyls
- globerulus
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cis-dihydrodiols
-
pcb-contaminated
-
ring-hydroxylating
-
biphenyl-utilizing
-
chlorobenzoates
-
biphenyl-induced
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polychlorobiphenyls
- beijerinckia
- pnomenusa
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2,2\'-dichlorobiphenyl
-
pandoraea
- synthesis
-
2,2\',5,5\'-tetrachlorobiphenyl
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2,3-biphenyl dioxygenase, BDO, biphenyl 2, 3-dioxygenase, Biphenyl 2,3-dioxygenase, biphenyl dioxygenase, biphenyl-2,3-dioxygenase, BPDO, BPDOB356, BPDOCam-1, BPDOLB400, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-biphenyl dioxygenase
BDO
biphenyl 2, 3-dioxygenase
Biphenyl 2,3-dioxygenase
biphenyl dioxygenase
BPDO
BPDOB356
BPDOLB400
BPH
BPH dox
BphA
BphA1
BphABC
BphABCD
BphAE
BPO
-
-
-
-
ThebphA1fA2f
BDO
-
-
-
-
Biphenyl 2,3-dioxygenase
-
-
-
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biphenyl dioxygenase
-
-
-
-
biphenyl dioxygenase
-
-
biphenyl dioxygenase
-
the enzyme is composed of BphA1, BphA2 [large (alpha) and small (beta) subunits of an iron-sulfur protein, respectively], BphA3 (ferredoxin), and BphA4 (ferredoxin reductase)
biphenyl dioxygenase
-
the enzyme is composed of BphA1, BphA2 [large (alpha) and small (beta) subunits of an iron-sulfur protein, respectively], BphA3 (ferredoxin), and BphA4 (ferredoxin reductase)
-
biphenyl dioxygenase
A5YWJ0, A5YWJ1, A5YWJ2, A5YWJ3, A5YWJ4, A5YWJ5, A5YWJ6, A5YWJ7, A5YWJ8, A5YWJ9, A5YWK0, A5YWK1, A5YWK2, A5YWK3, A5YWK4, A5YWK5, A5YWK6
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BPDO
-
-
-
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BPDO
A5YWJ0, A5YWJ1, A5YWJ2, A5YWJ3, A5YWJ4, A5YWJ5, A5YWJ6, A5YWJ7, A5YWJ8, A5YWJ9, A5YWK0, A5YWK1, A5YWK2, A5YWK3, A5YWK4, A5YWK5, A5YWK6
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BPH dox
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-
-
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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+
-
-
-
-
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
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
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redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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 + 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 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
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+
-
-
-
?
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+
-
-
-
-
?
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
brenda
strain LB400, hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain LB400 bphA with the homologous gene of Comamonas testosteroni B-356
-
-
brenda
strain B-356, hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain LB400 bphA with the homologous gene of Comamonas testosteroni B-356
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
from second most abundant taxon present in the horseradish rhizosphere
brenda
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
brenda
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
brenda
additional information
-
from bacterium, that dominates biphenyl metabolism in the horseradish rhizosphere soil
brenda
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
brenda
additional information
-
from bacterium present in the horseradish rhizosphere
brenda
additional information
-
from predominant biphenyl-utilizing bacteria in the initial bulk soil
brenda
additional information
microbial community of a polychlorinated biphenyl-polluted soil
brenda
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
brenda
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
-
brenda
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
brenda
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
-
brenda
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
brenda
additional information
-
microbial community of a polychlorinated biphenyl-polluted soil
-
brenda
additional information
-
from bacteria in the rhizosphere of horseradish and bulk soil contaminated by polychlorinated biphenyls
brenda
additional information
-
from bacterium present in the horseradish rhizosphere
brenda
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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
-
Show AA Sequence and Transmembrane Helices (373 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Paraburkholderia xenovorans (strain LB400)
Rhodococcus jostii (strain RHA1)
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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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SUBUNIT
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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PROTEIN VARIANTS
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
-
significant change in regiospecificity of substrate dioxygenation, factor 2.3
-
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
-
N348H
-
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
-
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
-
conversion of sequence to corresponding sequence of Pseudomonas sp. strain LB400
F336M
-
the mutant produces principally 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl from 2,2'-dichlorobiphenyl
F370Y
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
L283S
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
M237T
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
S238T
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
T335A
T335A/F336I
-
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
-
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
-
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
-
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
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
H255Q/V258I/G268A/F277Y
-
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
-
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
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376K
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376N
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
T376V
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
H255Q/V258I/G268A/F277Y
-
mutant of the bphA1 gene encoding the large subunit, that is responsible for substrate specificity, extremely enhanced benzene-, toluene-, and alkylbenzene-degrading ability
-
T376F
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
-
T376K
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
-
T376N
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
-
T376V
-
shows novel degradation activity for dibenzofuran, which is a poor substrate for the wild type enzyme
-
T335A/F336T/N338T/I341T
additional information
T335A
-
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
-
the mutant yields 2,3-dihydroxy-2,2'chlorobiphenyl as the major metabolite from 2,2'-dichlorobiphenyl
T335A/F336M
-
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
-
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
-
conversion of sequence to corresponding sequence of Pseudomonas pseudoalcaligenes strain KF707
T335A/F336T/N338T/I341T
-
conversion of sequence to corresponding sequence of Pseudomonas pseudoalcaligenes strain KF707
-
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
-
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
-
additional information
-
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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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
cis-2',3'-dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
synthesis
-
cis-2',3'-dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Resnick, S.M.; Torok, D.S.; Gibson, D.T.
Oxidation of carbazole to 3-hydroxycarbazole by naphthalene 1,2-dioxygenase and biphenyl 2,3-dioxygenase
FEMS Microbiol. Lett.
113
297-302
1993
Sphingobium yanoikuyae, Sphingobium yanoikuyae B8/36
brenda
Erickson, B.D.; Mondello, F.J.
Enhanced biodegradation of polychlorated biphenyls after site-directed mutagenesis of a biphenyl dioxygenase gene
Appl. Environ. Microbiol.
59
3858-3862
1993
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707, Pseudomonas sp., Pseudomonas sp. LB400
brenda
Haddock, J.D.; Horton, J.R.; Gibson, D.T.
Dihydroxylation and dechlorination of chlorinated biphenyls by purified biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
J. Bacteriol.
177
20-26
1995
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Seeger, M.; Timmis, K.N.; Hofer, B.
Degradation of chlorobiphenyls catalyzed by the bph-encoded biphenyl-2,3-dioxygenase and biphenyl-2,3-dihydrodiol-2,3-dehydrogenase of Pseudomonas sp. LB400
FEMS Microbiol. Lett.
133
259-264
1995
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Haddock, J.D.; Gibson, D.T.
Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
J. Bacteriol.
177
5834-5839
1995
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Hurtubise, Y.; Barriault, D.; Sylvestre, M.
Characterization of active recombinant His-tagged oxygenase component of Comamonas testosteroni B-356 biphenyl dioxygenase
J. Biol. Chem.
271
8152-8156
1996
Comamonas testosteroni
brenda
Resnick, S.M.; Gibson, D.T.
Oxidation of 6,7-dihydro-5H-benzocycloheptene by bacterial strains expressing naphthalene dioxygenase, biphenyl dioxygenase, and toluene dioxygenase yields homochiral mono-ol or cis-diol enantiomers as major products
Appl. Environ. Microbiol.
62
1364-1368
1996
Sphingobium yanoikuyae, Sphingobium yanoikuyae B8/36
brenda
McKay, D.B.; Seeger, M.; Zielinski, M.; Hofer, B.; Timmis, K.N.
Heterologous expression of biphenyl dioxygenase-encoding genes from a gram-positive broad-spectrum polychlorinated biphenyl degrader and characterization of chlorobiphenyl oxidation by the gene products
J. Bacteriol.
179
1924-1930
1997
Rhodococcus globerulus, Rhodococcus globerulus P6
brenda
Broadus, R.M.; Haddock, J.D.
Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
Arch. Microbiol.
170
106-112
1998
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Hurtubise, Y.; Barriault, D.; Sylvestre, M.
Involvement of the terminal oxygenase beta subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls
J. Bacteriol.
180
5828-5835
1998
Comamonas testosteroni, Pseudomonas sp., Pseudomonas sp. LB400
brenda
Chebrou, H.; Hurtubise, Y.; Barriault, D.; Sylvestre, M.
Heterologous expression and characterization of the purified oxygenase component of Rhodococcus globerulus P6 biphenyl dioxygenase and of chimeras derived from it
J. Bacteriol.
181
4805-4811
1999
Rhodococcus globerulus, Rhodococcus globerulus P6
brenda
Arnett, C.M.; Parales, J.V.; Haddock, J.D.
Influence of chlorine substituents on rates of oxidation of chlorinated biphenyls by the biphenyl dioxygenase of Burkholderia sp. strain LB400
Appl. Environ. Microbiol.
66
2928-2933
2000
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Seeger, M.; Camara, B.; Hofer, B.
Dehalogenation, denitration, dehydroxylation, and angular attack on substituted biphenyls and related compounds by a biphenyl dioxygenase
J. Bacteriol.
183
3548-3555
2001
Burkholderia sp., Burkholderia sp. LB400, Pseudomonas sp., Pseudomonas sp. LB400
brenda
Imbeault, N.Y.; Powlowski, J.B.; Colbert, C.L.; Bolin, J.T.; Eltis, L.D.
Steady-state kinetic characterization and crystallization of a polychlorinated biphenyl-transforming dioxygenase
J. Biol. Chem.
275
12430-12437
2000
Comamonas testosteroni
brenda
Kim, S.Y.; Jung, J.; Lim, Y.; Ahn, J.H.; Kim, S.I.; Hur, H.G.
cis-2', 3'-Dihydrodiol production on flavone B-ring by biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 expressed in Escherichia coli
Antonie van Leeuwenhoek
84
261-268
2003
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
L'Abbee J.B.; Barriault, D.; Sylvestre, M.
Metabolism of dibenzofuran and dibenzo-p-dioxin by the biphenyl dioxygenase of Burkholderia xenovorans LB400 and Comamonas testosteroni B-356
Appl. Microbiol. Biotechnol.
67
506-514
2005
Comamonas testosteroni, Paraburkholderia xenovorans
brenda
Barriault, D.; Simard, C.; Chatel, H.; Sylvestre, M.
Characterization of hybrid biphenyl dioxygenases obtained by recombining Burkholderia sp. strain LB400 bphA with the homologous gene of Comamonas testosteroni B-356
Can. J. Microbiol.
47
1025-1032
2001
Burkholderia sp., Comamonas testosteroni
brenda
Francova, K.; Mackova, M.; Macek, T.; Sylvestre, M.
Ability of bacterial biphenyl dioxygenases from Burkholderia sp. LB400 and Comamonas testosteroni B-356 to catalyse oxygenation of ortho-hydroxychlorobiphenyls formed from PCBs by plants
Environ. Pollut.
127
41-48
2004
Burkholderia sp., Burkholderia sp. LB400, Comamonas testosteroni
brenda
Suenaga, H.; Mitsuoka, M.; Ura, Y.; Watanabe, T.; Furukawa, K.
Directed evolution of biphenyl dioxygenase: emergence of enhanced degradation capacity for benzene, toluene, and alkylbenzenes
J. Bacteriol.
183
5441-5444
2001
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
Barriault, D.; Plante, M.M.; Sylvestre, M.
Family shuffling of a targeted bphA region to engineer biphenyl dioxygenase
J. Bacteriol.
184
3794-3800
2002
Burkholderia sp., Burkholderia sp. LB4000, Comamonas testosteroni
brenda
Zielinski, M.; Kahl, S.; Hecht, H.J.; Hofer, B.
Pinpointing biphenyl dioxygenase residues that are crucial for substrate interaction
J. Bacteriol.
185
6976-6980
2003
Burkholderia sp., Burkholderia sp. LB400
brenda
Barriault, D.; Sylvestre, M.
Evolution of the biphenyl dioxygenase BphA from Burkholderia xenovorans LB400 by random mutagenesis of multiple sites in region III
J. Biol. Chem.
279
47480-47488
2004
Paraburkholderia xenovorans
brenda
Barriault, D.; Lepine, F.; Mohammadi, M.; Milot, S.; Leberre, N.; Sylvestre, M.
Revisiting the regiospecificity of Burkholderia xenovorans LB400 biphenyl dioxygenase toward 2,2'-dichlorobiphenyl and 2,3,2',3'-tetrachlorobiphenyl
J. Biol. Chem.
279
47489-47496
2004
Paraburkholderia xenovorans
brenda
Furusawa, Y.; Nagarajan, V.; Tanokura, M.; Masai, E.; Fukuda, M.; Senda, T.
Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1
J. Mol. Biol.
342
1041-1052
2004
Rhodococcus sp. (Q53122), Rhodococcus sp. RHA1 (Q53122)
brenda
Zielinski, M.; Backhaus, S.; Hofer, B.
The principal determinants for the structure of the substrate-binding pocket are located within a central core of a biphenyl dioxygenase alpha subunit
Microbiology
148
2439-2448
2002
Burkholderia sp., Burkholderia sp. LB400, Rhodococcus globerulus, Rhodococcus globerulus P6
brenda
Han, J.; Kim, S.Y.; Jung, J.; Lim, Y.; Ahn, J.H.; Kim, S.I.; Hur, H.G.
Epoxide formation on the aromatic B ring of flavanone by biphenyl dioxygenase of Pseudomonas pseudoalcaligenes KF707
Appl. Environ. Microbiol.
71
5354-5361
2005
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
Zielinski, M.; Kahl, S.; Standfuss-Gabisch, C.; Camara, B.; Seeger, M.; Hofer, B.
Generation of novel-substrate-accepting biphenyl dioxygenases through segmental random mutagenesis and identification of residues involved in enzyme specificity
Appl. Environ. Microbiol.
72
2191-2199
2006
Paraburkholderia xenovorans
brenda
Witzig, R.; Junca, H.; Hecht, H.J.; Pieper, D.H.
Assessment of toluene/biphenyl dioxygenase gene diversity in benzene-polluted soils: links between benzene biodegradation and genes similar to those encoding isopropylbenzene dioxygenases
Appl. Environ. Microbiol.
72
3504-3514
2006
Burkholderia sp. (O86136), Comamonas testosteroni (Q46372), Comamonas testosteroni (Q8KZP9), Paraburkholderia xenovorans (P37333), Pseudomonas aeruginosa, Pseudomonas aeruginosa JI104, Pseudomonas pseudoalcaligenes (Q52028), Pseudomonas pseudoalcaligenes KF707 (Q52028), Pseudomonas sp. (Q52438), Rhodococcus erythropolis (Q79EP8), Rhodococcus erythropolis TA421 (Q79EP8), Rhodococcus globerulus (Q52757), Rhodococcus globerulus P6 (Q52757), Rhodococcus sp. (Q53122)
brenda
Suenaga, H.; Goto, M.; Furukawa, K.
Active-site engineering of biphenyl dioxygenase: effect of substituted amino acids on substrate specificity and regiospecificity
Appl. Microbiol. Biotechnol.
71
168-176
2006
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
Suenaga, H.; Sato, M.; Goto, M.; Takeshita, M.; Furukawa, K.
Steady-state kinetic characterization of evolved biphenyl dioxygenase, which acquired novel degradation ability for benzene and toluene
Biosci. Biotechnol. Biochem.
70
1021-1025
2006
Paraburkholderia xenovorans, Pseudomonas pseudoalcaligenes
brenda
Vezina, J.; Barriault, D.; Sylvestre, M.
Family shuffling of soil DNA to change the regiospecificity of Burkholderia xenovorans LB400 biphenyl dioxygenase
J. Bacteriol.
189
779-788
2007
Paraburkholderia xenovorans
brenda
Yu, C.L.; Liu, W.; Ferraro, D.J.; Brown, E.N.; Parales, J.V.; Ramaswamy, S.; Zylstra, G.J.; Gibson, D.T.; Parales, R.E.
Purification, characterization, and crystallization of the components of a biphenyl dioxygenase system from Sphingobium yanoikuyae B1
J. Ind. Microbiol. Biotechnol.
34
311-324
2007
Sphingobium yanoikuyae, Sphingobium yanoikuyae B1
brenda
Shindo, K.; Nakamura, R.; Osawa, A.; Kagami, O.; Kanoh, K.; Furukawa, K.; Misawa, N.
Biocatalytic synthesis of monocyclic arene-dihydrodiols and -diols by Escherichia coli cells expressing hybrid toluene/biphenyl dioxygenase and dihydrodiol dehydrogenase genes
J. Mol. Catal. B
35
134-141
2005
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
-
brenda
Master, E.R.; Agar, N.Y.; Gomez-Gil, L.; Powlowski, J.B.; Mohn, W.W.; Eltis, L.D.
Biphenyl dioxygenase from an arctic isolate is not cold adapted
Appl. Environ. Microbiol.
74
3908-3911
2008
Pseudomonas sp.
brenda
Shindo, K.; Shindo, Y.; Hasegawa, T.; Osawa, A.; Kagami, O.; Furukawa, K.; Misawa, N.
Synthesis of highly hydroxylated aromatics by evolved biphenyl dioxygenase and subsequent dihydrodiol dehydrogenase
Appl. Microbiol. Biotechnol.
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2007
Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
Mohammadi, M.; Chalavi, V.; Novakova-Sura, M.; Laliberte, J.; Sylvestre, M.
Expression of bacterial biphenyl-chlorobiphenyl dioxygenase genes in tobacco plants
Biotechnol. Bioeng.
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2007
Paraburkholderia xenovorans
brenda
Ferraro, D.J.; Brown, E.N.; Yu, C.; Parales, R.E.; Gibson, D.T.; Ramaswamy, S.
Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1
BMC Struct. Biol.
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2007
Sphingobium yanoikuyae, Sphingobium yanoikuyae B1
brenda
Yang, X.; Liu, X.; Song, L.; Xie, F.; Zhang, G.; Qian, S.
Characterization and functional analysis of a novel gene cluster involved in biphenyl degradation in Rhodococcus sp. strain R04
J. Appl. Microbiol.
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Rhodococcus sp., Rhodococcus sp. R04
brenda
Gomez-Gil, L.; Kumar, P.; Barriault, D.; Bolin, J.T.; Sylvestre, M.; Eltis, L.D.
Characterization of biphenyl dioxygenase of Pandoraea pnomenusa B-356 as a potent polychlorinated biphenyl-degrading enzyme
J. Bacteriol.
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Pandoraea pnomenusa, Pandoraea pnomenusa B-356, Paraburkholderia xenovorans
brenda
Chadhain, S.M.; Moritz, E.M.; Kim, E.; Zylstra, G.J.
Identification, cloning, and characterization of a multicomponent biphenyl dioxygenase from Sphingobium yanoikuyae B1
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2007
Sphingobium yanoikuyae, Sphingobium yanoikuyae B1
brenda
Kagami, O.; Shindo, K.; Kyojima, A.; Takeda, K.; Ikenaga, H.; Furukawa, K.; Misawa, N.
Protein engineering on biphenyl dioxygenase for conferring activity to convert 7-hydroxyflavone and 5,7-dihydroxyflavone (chrysin)
J. Biosci. Bioeng.
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2008
Pseudomonas putida, Pseudomonas putida KF715
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Seo, J.; Kang, S.I.; Kim, M.; Won, D.; Takahashi, H.; Ahn, J.H.; Chong, Y.; Lee, E.; Lim, Y.; Kanaly, R.A.; Han, J.; Hur, H.G.
TD-DFT-assisted absolute configuration determination of cis-dihydrodiol metabolite produced from isoflavone by biphenyl dioxygenase
Anal. Biochem.
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Pseudomonas pseudoalcaligenes, Pseudomonas pseudoalcaligenes KF707
brenda
Sul, W.J.; Park, J.; Quensen, J.F.; Rodrigues, J.L.; Seliger, L.; Tsoi, T.V.; Zylstra, G.J.; Tiedje, J.M.
DNA-stable isotope probing integrated with metagenomics for retrieval of biphenyl dioxygenase genes from polychlorinated biphenyl-contaminated river sediment
Appl. Environ. Microbiol.
75
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Bacteria, Paraburkholderia xenovorans LB400
brenda