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Global Incorporation of Norleucine in Place of Methionine in Cytochrome P450
 

Summary: Global Incorporation of Norleucine in
Place of Methionine in Cytochrome P450
BM-3 Heme Domain Increases
Peroxygenase Activity
Patrick C. Cirino, Yi Tang, Katsuyuki Takahashi, David A. Tirrell,
Frances H. Arnold
Division of Chemistry and Chemical Engineering, California Institute
of Technology, Pasadena, California 91125, telephone: 626-395-4553;
fax: 626-568-8743; e-mail: frances@cheme.caltech.edu
Received 17 December 2002; accepted 24 March 2003
DOI: 10.1002/bit.10718
Abstract: In this study we have replaced all 13 methio-
nine residues in the cytochrome P450 BM-3 heme do-
main (463 amino acids) with the isosteric methionine
analog norleucine. This experiment has provided a
means of testing the functional limits of globally incor-
porating into an enzyme an unnatural amino acid in
place of its natural analog, and also an efficient way to
test whether inactivation during peroxide-driven P450
catalysis involves methionine oxidation. Although there

  

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

 

Collections: Chemistry; Biology and Medicine