Linked Life Data

16190688

Source:http://linkedlifedata.com/resource/pubmed/id/16190688

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2005-9-29
pubmed:abstractText
Lipases (EC 3.1.1.3) play an important role in asymmetric biocatalysis. Tailoring these enzymes to novel, unnatural substrates is one of the primary challenges of protein engineering. We have used circular permutation, the intramolecular relocation of a protein's N- and C-termini, to explore the effects of altered active site accessibility and protein backbone flexibility on the catalytic performance of lipase B from Candida antarctica (CALB). Our combinatorial approach identified 63 unique functional protein permutants of CALB, and kinetic analysis of selected candidates indicated that a majority of enzyme variants either retained or surpassed wild-type CALB activity on a series of standard substrates. Beyond the potential benefits of these tailor-made lipases as new catalysts for unnatural substrates, our study validates circular permutation as a promising general method for lipase engineering.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13466-7
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Improving the catalytic activity of Candida antarctica lipase B by circular permutation.
pubmed:affiliation
Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.