Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
Laboratory Evolution of Cytochrome P450 BM-3 Monooxygenase for
 

Summary: Laboratory Evolution of Cytochrome
P450 BM-3 Monooxygenase for
Organic Cosolvents
Tuck Seng Wong,* Frances H. Arnold, Ulrich Schwaneberg*
Division of Chemistry and Chemical Engineering 210-41, California Institute
of Technology, Pasadena, California 91125; telephone: (626) 395-4162;
fax: (626) 568-8743; e-mail: frances@cheme.caltech.edu
Received 17 March 2003; accepted 29 September 2003
Published online 31 December 2003 in Wiley InterScience (www.interscience.wiley.com). DOI: 10.1002/bit.10896
Abstract: CytochromeP450BM-3(EC1.14.14.1)catalyzes
the hydroxylation and/or epoxidation of a broad range of
substrates, including alkanes, alkenes, alcohols, fatty acids,
amides, polyaromatic hydrocarbons, and heterocycles. For
many of these notoriously water-insoluble compounds,
P450 BM-3's Km values are in the millimolar range. Polar
organiccosolvents are thereforeaddedto increasesubstrate
solubility and achieve high catalytic efficiency. Using P450
BM-3 as a catalyst for these important transformations
requires that we improve its ability to tolerate the cosol-
vents. By directed evolution, we improved the activity of

  

Source: Arnold, Frances H. - Division of Chemistry and Chemical Engineering, California Institute of Technology

 

Collections: Chemistry; Biology and Medicine