Engineered Cytochromes P 450 for Biocatalysis

Toward Kilogram-Scale Peroxygenase-Catalyzed Oxyfunctionalization of Cyclohexane

“…Selective enzyme catalysts may represent a solution to this selectivity issue. In the past, especially cytochrome P450 monooxygenases (P450 MOs) , have been considered as catalysts for the selective oxyfunctionalization of cycloalkanes. − Though excellent results with full conversion and high selectivity have been achieved, the space time yields tend to be low, in the range of a few millimolar product formations per hour and low final product titers generally in the range of 5–10 mM . Next, the complex molecular architecture of many P450 MOs and also their dependency on molecular oxygen challenge their practical application at scale. − So-called unspecific peroxygenases (UPOs, E.C.…”

Protein engineering for natural product biosynthesis: expanding diversity for therapeutic applications

“…After two more rounds of site-saturated mutagenesis, the stereoselectivity was reversed entirely, resulting in a P450 pravastatin synthase with a 21-fold lower Km value for compactin. [15] Furthermore, creating a highly effective mutant of P450sca-2 for pravastatin synthesis is a well-known case of semirational P450 design for commercial applications. [16]…”

“…Contrary to guided evolution, CPD can offer a clear transformation strategy and significantly reduce the labor involved in building and analyzing mutant libraries. [15] De novo protein designing, enzyme-substrate specificity, and thermal stability design have all made significant strides, and some of the created enzymes are being utilized for industrial and medical purposes. The summary of the conventional protein engineering techniques is listed in Table 1 Figure 1.…”