Source:http://linkedlifedata.com/resource/pubmed/id/18421383
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2008-4-18
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pubmed:abstractText |
The straightforward synthesis of both enantiomers of cis-5'-hydroxythalidomide, a major metabolite of thalidomide, has been accomplished by enzymatic kinetic resolution of a racemic substrate catalyzed by Pseudomonas stutzeri lipase TL. cis-5'-Hydroxythalidomide shows resistance to racemization (and epimerization) at physiological pH. A tube formation assay to assess the ability to inhibit angiogenesis revealed that cis-5'-hydroxythalidomides are inactive.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1477-0520
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1540-3
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pubmed:meshHeading |
pubmed-meshheading:18421383-Catalysis,
pubmed-meshheading:18421383-Hydrogen-Ion Concentration,
pubmed-meshheading:18421383-Kinetics,
pubmed-meshheading:18421383-Lipase,
pubmed-meshheading:18421383-Molecular Conformation,
pubmed-meshheading:18421383-Pseudomonas stutzeri,
pubmed-meshheading:18421383-Stereoisomerism,
pubmed-meshheading:18421383-Thalidomide
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pubmed:year |
2008
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pubmed:articleTitle |
Enzymatic resolution and evaluation of enantiomers of cis-5'-hydroxythalidomide.
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pubmed:affiliation |
Department of Frontier Materials, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso, Showa-ku, Nagoya 466-8555, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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