Linked Life Data

16095281

Source:http://linkedlifedata.com/resource/pubmed/id/16095281

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2005-8-12
pubmed:abstractText
The kinetic resolution of a range of methyl-substituted 1-oxaspiro[2.5]octanes by yeast epoxide hydrolase (YEH) from Rhodotorula glutinis has been investigated. The structural determinants of substrate specificity and stereoselectivity of YEH toward these substrates appeared to be the configuration of the epoxide ring and the substitution pattern of the cyclohexane ring. For all compounds tested, O-axial epoxides were hydrolyzed faster than the corresponding O-equatorial compounds. In concern of the ring substituents, YEH preferred methyl groups on the Re side of the ring. Placement of substituents close to the spiroepoxide carbon decreased the reaction rate but increased enantioselectivity. YEH-catalyzed kinetic resolutions of 4-methyl 1-oxaspiro[2.5]octane epimers were most enantioselective (E > 100).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-3263
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6639-46
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Stereoselectivity and substrate specificity in the kinetic resolution of methyl-substituted 1-oxaspiro[2.5]octanes by Rhodotorula glutinis epoxide hydrolase.
pubmed:affiliation
Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703HB Wageningen, The Netherlands.
pubmed:publicationType
Journal Article