Benzylic and aryl hydroxylations of m-xylene by o-xylene dioxygenase from Rhodococcus sp. strain DK17
Cited 8 time in
- Benzylic and aryl hydroxylations of m-xylene by o-xylene dioxygenase from Rhodococcus sp. strain DK17
- Other Titles
- Rhodococcus sp. strain DK17이 생산하는 o-xylene dioxygenase에 의한 m-xylene의 benzylic- 및 aryl-hydroxylation 반응
- Kim, Dockyu
Jung Nam Choi
Zylstra, Gerben J.
Kang, Beom Sik
Choong Hwan Lee
Ki Young Choi
- Biotechnology & Applied Microbiology
- Benzylic hydroxylation; Rhodococcus; meta Effect; o-Xylene dioxygenase
- Issue Date
- Springer Berlin / Heidelberg
- Kim, Dockyu, et al. 2010. "Benzylic and aryl hydroxylations of m-xylene by o-xylene dioxygenase from Rhodococcus sp. strain DK17". APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 86(6): 1841-1847.
- Escherichia coli cells expressing Rhodococcus DK17 o-xylene dioxygenase genes were used for bioconversion of m-xylene. Gas chromatography-mass spectrometry analysis of the oxidation products detected 3 methylbenzylalcohol and 2,4-dimethylphenol in the ratio 9:1. Molecular modeling suggests that o-xylene dioxygenase can hold xylene isomers at a kink region between α6 and α7 helices of the active site and α9 helix covers the substrates. m-Xylene is unlikely to locate at the active site with a methyl group facing the kink region because this configuration would not fit within the substrate-binding pocket. The m-xylene molecule can flip horizontally to expose the meta-position methyl group to the catalytic motif. In this configuration, 3 methylbenzylalcohol could be formed, presumably due to the meta effect. Alternatively, the m-xylene molecule can rotate counterclockwise, allowing the catalytic motif to hydroxylate at C-4 yielding 2,4-dimethylphenol. Site-directed mutagenesis combined with structural and functional analyses suggests that the alanine-218 and the aspartic acid-262 in the α7 and the α9 helices play an important role in positioning m-xylene, respectively
- Files in This Item
- Can archive pre-print and post-print or publisher's version/PDF
Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
Can archive pre-print (ie pre-refereeing)
Archiving not formally supported
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.