1.14.12.18: biphenyl 2,3-dioxygenase
This is an abbreviated version!
For detailed information about biphenyl 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.18
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1.14.12.18
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biphenyls
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polychlorinated
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pseudoalcaligenes
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xenovorans
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chlorobiphenyls
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dihydrodiols
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comamonas
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rieske-type
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testosteroni
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pcb-degrading
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bpdos
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pcb-contaminated
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yanoikuyae
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
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2,3-dihydroxybiphenyls
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biphenyl-degrading
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cis-dihydrodiols
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globerulus
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ring-hydroxylating
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pnomenusa
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2,2\'-dichlorobiphenyl
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pandoraea
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polychlorobiphenyls
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biphenyl-utilizing
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synthesis
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beijerinckia
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chlorobenzoates
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biphenyl-induced
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2,2\',5,5\'-tetrachlorobiphenyl
- 1.14.12.18
- biphenyls
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polychlorinated
- pseudoalcaligenes
- xenovorans
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chlorobiphenyls
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dihydrodiols
- comamonas
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rieske-type
- testosteroni
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pcb-degrading
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bpdos
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pcb-contaminated
- yanoikuyae
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
- 2,3-dihydroxybiphenyls
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biphenyl-degrading
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cis-dihydrodiols
- globerulus
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ring-hydroxylating
- pnomenusa
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2,2\'-dichlorobiphenyl
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pandoraea
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polychlorobiphenyls
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biphenyl-utilizing
- synthesis
- beijerinckia
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chlorobenzoates
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biphenyl-induced
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2,2\',5,5\'-tetrachlorobiphenyl
Reaction
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, BPH, BPH dox, BphA, BphA1, BphA1A2, BphABC, BphABCD, BphAE, BPO, ThebphA1fA2f
ECTree
1.14.12.18 biphenyl 2,3-dioxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.12.18 - biphenyl 2,3-dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A234S
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significant change in regiospecificity of substrate dioxygenation, factor 2.3
F378A
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very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
F384A
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very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
M231A
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very strong change in regiospecificity of substrate dioxygenation, factor higher than 7
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
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
Pseudomonas oleovorans KF707
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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
Pseudomonas oleovorans KF707
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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
Pseudomonas oleovorans KF707
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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
Pseudomonas oleovorans KF707
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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
Pseudomonas oleovorans KF707
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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
-
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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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
