Linked Life Data

20049759

Source:http://linkedlifedata.com/resource/pubmed/id/20049759

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-2-15
pubmed:abstractText
The size of the stereoselectivity pocket of Candida antarctica lipase B limits the range of alcohols that can be resolved with this enzyme. These steric constrains have been changed by increasing the size of the pocket by the mutation W104A. The mutated enzyme has good activity and enantioselectivity toward bulky secondary alcohols, such as 1-phenylalkanols, with alkyl chains up to eight carbon atoms. The S enantiomer was preferred in contrast to the wild-type enzyme, which has R selectivity. The magnitude of the enantioselectivity changes in an interesting way with the chain length of the alkyl moiety. It is governed by interplay between entropic and enthalpic contributions and substrates with long alkyl chains are resolved best with E values higher than 100. The enantioselectivity increases with temperature for the small substrates, but decreases for the long ones.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1439-7633
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
411-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Mutant lipase-catalyzed kinetic resolution of bulky phenyl alkyl sec-alcohols: a thermodynamic analysis of enantioselectivity.
pubmed:affiliation
Department of Biochemistry, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Center, 10691 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't