Linked Life Data

16001257

Source:http://linkedlifedata.com/resource/pubmed/id/16001257

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-2-13
pubmed:abstractText
Wild-type cytochrome P450 monooxygenase from Bacillus megaterium (P450 BM-3) has a low hydroxylation activity for beta-ionone (<1 min(-1)). Substitution of phenylalanine by valine at position 87 led to a more than 100-fold increase in beta-ionone hydroxylation activity (115 min(-1)). Enzyme activity could be further increased by both site-directed and random mutagenesis. The mutant R47L Y51F F87V, designed by site-directed mutagenesis, and the mutant A74E F87V P386S, obtained after two rounds of error-prone polymerase chain reaction, exhibited an increase in activity of up to 300-fold compared to the wild-type enzyme. The triple mutant R47 LY51F F87V exhibited moderate enantioselectivity, forming (R)-4-hydroxy-beta-ionone with an optical purity of 39%. All mutants regioselectively converted beta-ionone into 4-hydroxy-beta-ionone. The regioselectivity is determined amongst others by the absolute configuration of the substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0175-7598
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Biotransformation of beta-ionone by engineered cytochrome P450 BM-3.
pubmed:affiliation
Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. itbvur@itb.uni-stuttgart.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't