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APPLIED AND ENVIRONMENTAL MICROBIOLOGY, Jan. 2009, p. 337344 Vol. 75, No. 2 0099-2240/09/$08.00 0 doi:10.1128/AEM.01758-08
 

Summary: APPLIED AND ENVIRONMENTAL MICROBIOLOGY, Jan. 2009, p. 337­344 Vol. 75, No. 2
0099-2240/09/$08.00 0 doi:10.1128/AEM.01758-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
In Vivo Evolution of Butane Oxidation by Terminal Alkane
Hydroxylases AlkB and CYP153A6
Daniel J. Koch,1
Mike M. Chen,1
Jan B. van Beilen,2
and Frances H. Arnold1
*
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125,1
and
De´partement de Biologie Mole´culaire Ve´ge´tale, Universite´ de Lausanne, Lausanne, Switzerland2
Received 30 July 2008/Accepted 8 November 2008
Enzymes of the AlkB and CYP153 families catalyze the first step in the catabolism of medium-chain-length
alkanes, selective oxidation of the alkane to the 1-alkanol, and enable their host organisms to utilize alkanes
as carbon sources. Small, gaseous alkanes, however, are converted to alkanols by evolutionarily unrelated
methane monooxygenases. Propane and butane can be oxidized by CYP enzymes engineered in the laboratory,
but these produce predominantly the 2-alkanols. Here we report the in vivo-directed evolution of two medium-
chain-length terminal alkane hydroxylases, the integral membrane di-iron enzyme AlkB from Pseudomonas

  

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

 

Collections: Chemistry; Biology and Medicine