Source:http://linkedlifedata.com/resource/pubmed/id/17665136
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-11-29
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pubmed:abstractText |
Enantio-convergent hydrolysis of racemic styrene oxides was achieved to prepare enantiopure (R)-phenyl-1,2-ethanediol by using two recombinant epoxide hydrolases (EHs) of a bacterium, Caulobacter crescentus, and a marine fish, Mugil cephalus. The recombinant C. crescentus EH primarily attacked the benzylic carbon of (S)-styrene oxide, while the M. cephalus EH preferentially attacked the terminal carbon of (R)-styrene oxide, thus leading to the formation of (R)-phenyl-1,2-ethanediol as the main product. (R)-Phenyl-1,2-ethanediol was obtained with 90% enantiomeric excess and yield as high as 94% from 50 mM racemic styrene oxides in a one-pot process.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epoxy Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/styrene glycol,
http://linkedlifedata.com/resource/pubmed/chemical/styrene oxide
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1573-6776
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-33
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pubmed:dateRevised |
2008-10-7
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pubmed:meshHeading |
pubmed-meshheading:17665136-Animals,
pubmed-meshheading:17665136-Caulobacter crescentus,
pubmed-meshheading:17665136-Epoxy Compounds,
pubmed-meshheading:17665136-Ethylene Glycols,
pubmed-meshheading:17665136-Fishes,
pubmed-meshheading:17665136-Hydrolases,
pubmed-meshheading:17665136-Marine Biology,
pubmed-meshheading:17665136-Recombinant Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Biosynthesis of (R)-phenyl-1,2-ethanediol from racemic styrene oxide by using bacterial and marine fish epoxide hydrolases.
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pubmed:affiliation |
Department of Food Science and Biotechnology, Kyungsung University, Busan 608-736, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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