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
-
pcb-degrading
-
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
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General Information on EC 1.14.12.18 - biphenyl 2,3-dioxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
metabolism
physiological function
additional information
metabolism
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BPDO is one of the most potent biocatalysts of natural origin for the dioxygenation of chlorobiphenyls
metabolism
biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls
physiological function
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catalyzes critical steps of the bacterial polychlorinated biphenyl degrading pathway
physiological function
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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
additional information
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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
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the multicomponent enzyme consists of small and large subunits of the oxygenase component, and ferredoxin and reductase components
additional information
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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
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the alpha-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase directly influences catalytic activities and substrate specificity, three-dimensional model of LY402-BphA1, overview. The number and subposition of chlorine substituents influence the polychlorinated biphenyls binding ability of BphA1 significantly. Ser283, Val287, Gly321 and Tyr384 residues in the active site of LY402-BphA1 show high variability, and the space limitation of the active site of BphA1 have negative influence on the polychlorinated biphenyls binding affinity of the enzyme
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