Engineered Alkane-Hydroxylating Cytochrome P450BM3 Exhibiting Nativelike Catalytic Properties

Department of Chemistry and Chemical Engineering, California Institute of Technology, 1200 California Blvd. MC 210-41, Pasadena, CA 91125, USA.
Angewandte Chemie International Edition (Impact Factor: 11.26). 02/2007; 46(44):8414-8. DOI: 10.1002/anie.200702616
Source: PubMed

ABSTRACT (Figure Presented) Divide, evolve, and conquer: A domain-based strategy (see scheme) was used to engineer high catalytic and coupling efficiency for propane hydroxylation in a multidomain cytochrome P450 enzyme. The engineered enzymes exhibit high total activities in whole-cell bioconversions of propane to propanol under mild conditions, using air as oxidant.

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Available from: Rudi Fasan, Jul 28, 2015
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    • "Six mutants of the uncharged Ser72 and Ala74 residues that contained a negatively charged amino acid at these respective positions were selected. The Ser72 and Ala74 residues are located around the substrate binding channel (Li et al., 2001b; Otey et al., 2006; Dietrich et al., 2009) of the protein and have been shown to influence regioselectivity (Otey et al., 2006; Dietrich et al., 2009) and metabolic efficiency (Li et al., 2000, 2001b; Fasan et al., 2007) in previous studies. Two M01 mutants that contained mutations at the Ser72 position, MT43 (S72D) and MT44 (S72E), and one M01 mutant that contained a mutation at the Ala74 position (MT41; A74E) were selected. "
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