Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17
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 spectrometr...
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| Veröffentlicht in: | Research in microbiology 2011-09, Vol.162 (7), p.724-728 |
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| creator | Yoo, Miyoun Kim, Dockyu Zylstra, Gerben J. Kang, Beom Sik Kim, Eungbin |
| description | 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. |
| doi_str_mv | 10.1016/j.resmic.2011.04.013 |
| format | Article |
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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
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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.</description><subject>Amino Acid Sequence</subject><subject>Aromatic hydroxylation</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biodegradation, Environmental</subject><subject>Biological and medical sciences</subject><subject>Biphenyl Compounds - chemistry</subject><subject>Biphenyl Compounds - metabolism</subject><subject>Dioxygenases - chemistry</subject><subject>Dioxygenases - genetics</subject><subject>Dioxygenases - metabolism</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Hydrophobic interactions</subject><subject>Hydroxylation</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Conformation</subject><subject>Molecular Sequence Data</subject><subject>Protein Engineering</subject><subject>Rhodococcus</subject><subject>Rhodococcus - enzymology</subject><subject>Rhodococcus - genetics</subject><subject>Rieske dioxygenase</subject><subject>Xylenes - metabolism</subject><issn>0923-2508</issn><issn>1769-7123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtv1DAQgC0EokvhHyDwBfWU4ImdOL4gQctLrYQE9Gx57cmuV0m8tbOI_Pt6laW9cfJ49M1D3xDyGlgJDJr3uzJiGrwtKwZQMlEy4E_ICmSjCgkVf0pWTFW8qGrWnpEXKe0Yg1pK8ZycVTmoJTQr0n3y-y2Oc0-3s4vh79ybyYeR4rg1o0VH1zM1x-_Gj4gxJ0KRIRyROp_xDY4mIe1iGOjPbXDBBmsPiaZ9SdMUjR_p1TXIl-RZZ_qEr07vObn98vn35bfi5sfX75cfbworhJwK3gFw12BrRc2ZtFwZI62yHFpgtqsV48Abpzg6WYEwiCbHa9aqtm551fJzcrH03cdwd8A06cEni31vRgyHpBUTQgmoRSbFQtoYUorY6X30g4mzBqaPgvVOL4L1UbBmQmfBuezNacBhPaB7KPpnNAPvToBJ1vRdzBp9euSE4ByaOnNvF64zQZtNzMztrzypyVeSkskqEx8WArOwPx6jTtbj8Sg-op20C_7_u94D23SkBA</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Yoo, Miyoun</creator><creator>Kim, Dockyu</creator><creator>Zylstra, Gerben J.</creator><creator>Kang, Beom Sik</creator><creator>Kim, Eungbin</creator><general>Elsevier Masson SAS</general><general>Elsevier Masson</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20110901</creationdate><title>Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17</title><author>Yoo, Miyoun ; Kim, Dockyu ; Zylstra, Gerben J. ; Kang, Beom Sik ; Kim, Eungbin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-3f113d6e8c45307c39aa7c9c31810cf5903136d93ed7214aeea93eb0898583283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Aromatic hydroxylation</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biodegradation, Environmental</topic><topic>Biological and medical sciences</topic><topic>Biphenyl Compounds - chemistry</topic><topic>Biphenyl Compounds - metabolism</topic><topic>Dioxygenases - chemistry</topic><topic>Dioxygenases - genetics</topic><topic>Dioxygenases - metabolism</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Fundamental and applied biological sciences. 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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
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| subjects | Amino Acid Sequence Aromatic hydroxylation Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biodegradation, Environmental Biological and medical sciences Biphenyl Compounds - chemistry Biphenyl Compounds - metabolism Dioxygenases - chemistry Dioxygenases - genetics Dioxygenases - metabolism Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Hydrophobic interactions Hydroxylation Microbiology Miscellaneous Molecular Conformation Molecular Sequence Data Protein Engineering Rhodococcus Rhodococcus - enzymology Rhodococcus - genetics Rieske dioxygenase Xylenes - metabolism |
| title | Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17 |
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