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Characterization and engineering of an o-xylene dioxygenase for biocatalytic applications.

Cited 2 time in scopus
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Title
Characterization and engineering of an o-xylene dioxygenase for biocatalytic applications.
Other Titles
생물촉매효소 o-xylene dioxygenase의 응용을 위한 효소반응특성 연구 및 개량
Authors
Choi, Ki Young
Yoo, Miyoun
Kim, Dockyu
Kim, Eungbin
Kang, Beom Sik
Subject
Biotechnology & Applied Microbiology; Energy & Fuels
Keywords
Aromatic dioxygenases; Biocatalysis; Regioselective hydroxylation; Rhodococcus; cis-Dihydrodiols; Agriculture
Issue Date
2013
Publisher
Elsevier
Citation
Choi, Ki Young, et al. 2013. "Characterization and engineering of an o-xylene dioxygenase for biocatalytic applications.". Bioresource Technology, 145(1): 123-127.
Abstract
The o-xylene dioxygenase from Rhodococcus sp. strain DK17 possesses the unique ability to perform distinct regioselective hydroxylations depending on the size and position of the substituent groups on the aromatic ring. Molecular modeling studies predicted that the substrate-binding pocket of the DK17 o-xylene dioxygenase is large enough to accommodate bicyclics and can be divided into three regions (distal, central, and proximal), and hydrophobic interactions in the distal position are important in substrate binding. Subsequent sitedirected mutagenesis experiments combined with metabolite analysis confirmed these predictions, and further showed that the different positioning of substrates in the active site of the enzyme results in the generation of different products. This review specifically summarizes molecular functional mechanisms that enable this enzyme to catalyze the respective hydroxylation reactions.tudies predicted that the substrate-binding pocket of the DK17 o-xylene dioxygenase is large enough to accommodate bicyclics and can be divided into three regions (distal, central, and proximal), and hydrophobic interactions in the distal position are important in substrate binding. Subsequent sitedirected mutagenesis experiments combined with metabolite analysis confirmed these predictions, and further showed that the different positioning of substrates in the active site of the enzyme results in the generation of different products. This review specifically summarizes molecular functional mechanisms that enable this enzyme to catalyze the respective hydroxylation reactions.
URI
http://repository.kopri.re.kr/handle/201206/6219
DOI
http://dx.doi.org/10.1016/j.biortech.2013.03.034
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