1263380-19-3Relevant academic research and scientific papers
Combinatorial alanine substitution enables rapid optimization of cytochrome P450BM3 for selective hydroxylation of large substrates
Lewis, Jared C.,Mantovani, Simone M.,Fu, Yu,Snow, Christopher D.,Komor, Russell S.,Wong, Chi-Huey,Arnold, Frances H.
, p. 2502 - 2505 (2010)
Made for each other: Combinatorial alanine substitution of active site residues in a thermostable cytochrome P450BM3 variant was used to generate an enzyme that is active with large substrates. Selective hydroxylation of methoxymethylated monosaccharides, alkaloids, and steroids was thus made possible (see Scheme). This approach could be useful for improving the activity of enzymes that show only limited activity with larger substrates.
