Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17

Miyoun Yoo; Dockyu Kim; Gerben J. Zylstra; Beom Sik Kang; Eungbin Kim

doi:10.1016/j.resmic.2011.04.013

Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17

Miyoun Yoo, Dockyu Kim, Gerben J. Zylstra, Beom Sik Kang, Eungbin Kim

Department of Systems Biology

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.

Original language	English
Pages (from-to)	724-728
Number of pages	5
Journal	Research in Microbiology
Volume	162
Issue number	7
DOIs	https://doi.org/10.1016/j.resmic.2011.04.013
Publication status	Published - 2011 Sep

Bibliographical note

Funding Information:
This work was supported by a grant to the 21C Frontier Microbial Genomics and Applications Center Program and by grant 2009-0079296 to the Basic Science Research Program through the National Research Foundation of Korea . Both are funded by the Ministry of Education, Science, and Technology of the Republic of Korea . DK is supported by the Korea Polar Research Institute under projects PE10050 and PE11060. GJZ acknowledges the support of NIEHS grant P42-ES004911 under the Superfund Basic Science Program. MY is a recipient of the Brain Korea 21 scholarship.

All Science Journal Classification (ASJC) codes

Microbiology
Molecular Biology

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10.1016/j.resmic.2011.04.013

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title = "Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17",

abstract = "Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.",

author = "Miyoun Yoo and Dockyu Kim and Zylstra, {Gerben J.} and Kang, {Beom Sik} and Eungbin Kim",

note = "Funding Information: This work was supported by a grant to the 21C Frontier Microbial Genomics and Applications Center Program and by grant 2009-0079296 to the Basic Science Research Program through the National Research Foundation of Korea . Both are funded by the Ministry of Education, Science, and Technology of the Republic of Korea . DK is supported by the Korea Polar Research Institute under projects PE10050 and PE11060. GJZ acknowledges the support of NIEHS grant P42-ES004911 under the Superfund Basic Science Program. MY is a recipient of the Brain Korea 21 scholarship.",

year = "2011",

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doi = "10.1016/j.resmic.2011.04.013",

language = "English",

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AU - Kim, Dockyu

AU - Zylstra, Gerben J.

AU - Kang, Beom Sik

AU - Kim, Eungbin

N1 - Funding Information: This work was supported by a grant to the 21C Frontier Microbial Genomics and Applications Center Program and by grant 2009-0079296 to the Basic Science Research Program through the National Research Foundation of Korea . Both are funded by the Ministry of Education, Science, and Technology of the Republic of Korea . DK is supported by the Korea Polar Research Institute under projects PE10050 and PE11060. GJZ acknowledges the support of NIEHS grant P42-ES004911 under the Superfund Basic Science Program. MY is a recipient of the Brain Korea 21 scholarship.

PY - 2011/9

Y1 - 2011/9

N2 - Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.

AB - Hydroxylation of the non-growth substrate biphenyl by recombinant o-xylene dioxygenases from Rhodococcus sp. strain DK17 was studied through bioconversion experiments. The metabolites from the biphenyl hydroxylation by each enzyme were identified and quantified by gas chromatography-mass spectrometry. The L266F mutant enzyme produced much more 2-hydroxybiphenyl (2.43 vs. 0.1 μg/L) and 3-hydroxybiphenyl (1.97 vs. 0.03 μg/L) than the wild-type. Site-directed mutagenesis combined with structural and functional analyses indicated that hydrophobic interactions and shielding effects against water are important factors in the hydroxylation of biphenyl by the o-xylene dioxygenase. The residue at position 266 plays a key role in coordinating the reaction.

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Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17

Abstract

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