Steady-state kinetic characterization of evolved biphenyl dioxygenase, which acquired novel degradation ability for benzene and toluene

Bioscience, Biotechnology, and Biochemistry
H SuenagaKensuke Furukawa

Abstract

Biphenyl dioxygenase (Bph Dox) catalyzes initial oxygenation in the bacterial biphenyl degradation pathway. Bph Dox in Pseudomonas pseudoalcaligenes KF707 is a Rieske type three-component enzyme in which a large subunit (encoded by the bphA1 gene) plays an important role in the substrate specificity of Bph Dox. Steady-state kinetic assays using purified enzyme components demonstrated that KF707 Bph Dox had a kcat/Km of 33.1 x 10(3) (M(-1) s(-1)) for biphenyl. Evolved 1072 Bph Dox generated by the process of DNA shuffling (Suenaga, H. et al., J. Bacteriol., 184, 3682-3688 (2002)) exhibited enhanced degradation activity not only for biphenyl (kcat/Km of 62.2 x 10(3) [M(-1) s(-1)]) but also for benzene and toluene, compounds that are rarely attacked by KF707 Bph Dox. These results suggest that evolved 1072 Bph Dox acquires higher affinities and catalytic efficiencies for various substrates than the original KF707 enzyme.

References

Jun 14, 2000·Current Opinion in Biotechnology·K Furukawa
Jun 12, 2002·Journal of Bacteriology·Hikaru SuenagaKensuke Furukawa
Nov 18, 2003·Journal of Bacteriology·Marco ZielinskiBernd Hofer
Aug 5, 2004·Journal of Bacteriology·Kensuke FurukawaMasatoshi Goto

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Citations

Apr 20, 2014·Nature Chemical Biology·Chad A Haynes, Ramon Gonzalez
Jun 19, 2008·Journal of Bioscience and Bioengineering·Kensuke Furukawa, Hidehiko Fujihara
Sep 24, 2018·Environmental Science and Pollution Research International·Jun Won YangHan S Kim

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