Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2006-10-26
pubmed:abstractText
This paper outlines the design and execution of the first mini-evolution of cyclopentanone monooxygenase (CPMO). The methodology described is a relatively inexpensive and rapid way to obtain mutant enzymes with the desired characteristics. Several successful mutants with enhanced enantioselectivities were identified. For example, mutant-catalyzed oxidation of 4-methoxycyclohexanone gave the corresponding lactone with 92% entantiometric excess (ee) compared to the 46% ee achieved with wild-type cyclohexanone monoxygenase (WT-CHMO). The original design of the mini-evolution and the following evaluation of mutants can provide valuable insights into the active site's construction and dynamics and can suggest other catalytically profitable mutations within the putative active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-3263
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8431-7
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Designing new Baeyer-Villiger monooxygenases using restricted CASTing.
pubmed:affiliation
Department of Physical Sciences, University of New Brunswick, Saint John, New Brunswick, E2L 4L5 Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't