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 | |
| Publication status | Published - 2011 Sep 1 |
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All Science Journal Classification (ASJC) codes
- Microbiology
- Molecular Biology
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Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17. / Yoo, Miyoun; Kim, Dockyu; Zylstra, Gerben J.; Kang, Beom Sik; Kim, Eungbin.
In: Research in Microbiology, Vol. 162, No. 7, 01.09.2011, p. 724-728.Research output: Contribution to journal › Article
TY - JOUR
T1 - Biphenyl hydroxylation enhanced by an engineered o-xylene dioxygenase from Rhodococcus sp. strain DK17
AU - Yoo, Miyoun
AU - Kim, Dockyu
AU - Zylstra, Gerben J.
AU - Kang, Beom Sik
AU - Kim, Eungbin
PY - 2011/9/1
Y1 - 2011/9/1
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.
UR - http://www.scopus.com/inward/record.url?scp=80955180488&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80955180488&partnerID=8YFLogxK
U2 - 10.1016/j.resmic.2011.04.013
DO - 10.1016/j.resmic.2011.04.013
M3 - Article
C2 - 21575716
AN - SCOPUS:80955180488
VL - 162
SP - 724
EP - 728
JO - Research in Microbiology
JF - Research in Microbiology
SN - 0923-2508
IS - 7
ER -