Online citations, reference lists, and bibliographies.
Please confirm you are human
(Sign Up for free to never see this)
← Back to Search

Characterization Of Hybrid Biphenyl Dioxygenases Obtained By Recombining Burkholderia Sp. Strain LB400 BphA With The Homologous Gene Of Comamonas Testosteroni B-356.

D. Barriault, Claire Simard, H. Chatel, M. Sylvestre
Published 2001 · Biology, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy
The bacterial degradation of polychlorinated biphenyls depends on the ability of the enzyme biphenyl 2,3-dioxygenase (BPDO) to catalyze their oxygenation. Analysis of hybrid BPDOs obtained using common restriction sites to exchange large DNA fragments between LB400 bphA and B-356 bphA showed that the C-terminal portion of LB400 alpha subunit can withstand extensive structural modifications, and that these modifications can change the catalytic properties of the enzyme. On the other hand, exchanging the C-terminal portion of B-356 BPDO alpha subunit with that of LB400 alpha subunit generated inactive chimeras. Data encourage an enzyme engineering approach, consisting of introducing extensive modifications of the C-terminal portion of LB400 bphA to extend BPDO catalytic properties toward polychlorinated biphenyls.
This paper references
Phenotypic and Phylogenetic Characterization of Burkholderia (Pseudomonas) sp. Strain LB400
Matthew G. Fain (2001)
Purification and properties of ferredoxinBPH, a component of biphenyl 2,3-dioxygenase of Pseudomonas sp strain LB400
J. Haddock (1997)
Characterization of Active Recombinant His-tagged Oxygenase Component of Comamonas testosteroni B-356 Biphenyl Dioxygenase (*)
Y. Hurtubise (1996)
Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase
T. Kumamaru (1998)
Tuning biphenyl dioxygenase for extended substrate specificity.
F. Brühlmann (1999)
Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
Richard M Broadus (1998)
Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme.
R. Parales (2000)
Steady-state Kinetic Characterization and Crystallization of a Polychlorinated Biphenyl-transforming Dioxygenase*
N. Imbeault (2000)
Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400.
B. D. Erickson (1992)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
U. Laemmli (1970)
Rapid assay for screening and characterizing microorganisms for the ability to degrade polychlorinated biphenyls.
D. Bedard (1986)
Cloning and expression of genes involved in 4-chlorobiphenyl transformation by Pseudomonas testosteroni: homology to polychlorobiphenyl-degrading genes in other bacteria.
D. Ahmad (1990)
Mouse limb muscle is determined in the absence of the earliest myogenic factor myf-5.
S. Tajbakhsh (1994)
Heterologous expression and characterization of the purified oxygenase component of Rhodococcus globerulus P6 biphenyl dioxygenase and of chimeras derived from it.
H. Chebrou (1999)
Analysis of bph operon from the polychlorinated biphenyl-degrading strain of Pseudomonas pseudoalcaligenes KF707.
K. Taira (1992)
Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components.
Y. Hurtubise (1995)
DH11S: an Escherichia coli strain for preparation of single-stranded DNA from phagemid vectors.
J. Lin (1992)
Engineering a hybrid pseudomonad to acquire 3,4-dioxygenase activity for polychlorinated biphenyls.
H. Suenaga (1999)
Site-directed mutagenesis for large insertions by oligonucleotide primers in optimized molar ratios.
D. Wang (1997)
Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships among Gram-negative bacterial biphenyl dioxygenases.
M. Sylvestre (1996)
DNA shuffling of a family of genes from diverse species accelerates directed evolution
A. Crameri (1998)
Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400.
J. Haddock (1995)
Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.
B. Kauppi (1998)
Involvement of the terminal oxygenase beta subunit in the biphenyl dioxygenase reactivity pattern toward chlorobiphenyls.
Y. Hurtubise (1998)
Functional analyses of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally.
N. Kimura (1997)
Protein measurement with the Folin phenol reagent.
O. H. Lowry (1951)

This paper is referenced by
Substrate specificity and expression of three 2,3-dihydroxybiphenyl 1,2-dioxygenases from Rhodococcus globerulus strain P6.
D. B. Mckay (2003)
Diversity of microbial toluene degradation pathways.
R. Parales (2008)
Subtle Difference between Benzene and Toluene Dioxygenases of Pseudomonas putida
C. Bagnéris (2005)
Proteomic Strategy for the Analysis of the Polychlorobiphenyl-Degrading Cyanobacterium Anabaena PD-1 Exposed to Aroclor 1254
Hangjun Zhang (2014)
Family shuffling of a targeted bphA region to engineer biphenyl dioxygenase.
D. Barriault (2002)
Directed evolution of the dioxygenase complex for the synthesis of furanone flavor compounds
L. M. Newman (2004)
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.
K. Frančová (2004)
MINIREVIEWS Biphenyl Dioxygenases: Functional Versatilities and Directed Evolution
K. Furukawa (2004)
putida Pseudomonas Toluene Dioxygenases of Subtle Difference between Benzene and
Claire Bagnéris (2004)
Aromatic Ring Hydroxylating Dioxygenases
R. Parales (2006)
34. Aromatic Oxidations
D. Leak (2012)
Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls
B. Cámara (2007)
Microbial degradation of polychlorinated biphenyls: biochemical and molecular features.
K. Furukawa (2008)
The principal determinants for the structure of the substrate-binding pocket are located within a central core of a biphenyl dioxygenase alpha subunit.
M. Zielinski (2002)
Biphenyl dioxygenases: functional versatilities and directed evolution.
K. Furukawa (2004)
Benzoate Dioxygenases Characterization of Hybrid Toluate and
Yong Ge (2003)
Substrate Specificity and Expression of Three 2 , 3-Dihydroxybiphenyl 1 , 2-Dioxygenases from Rhodococcus globerulus Strain P 6
D. B. Mckay (2003)
Aromatic Hydrocarbon Dioxygenases
R. Parales (2004)
Characterization of hybrid toluate and benzoate dioxygenases.
Yong Ge (2003)
Characterization of the molecular basis for polychlorinated biphenyls (PCBs) transformation by biphenyl dioxygenase
L. Gil (2006)
Semantic Scholar Logo Some data provided by SemanticScholar