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- W4313260075 endingPage "214" @default.
- W4313260075 startingPage "214" @default.
- W4313260075 abstract "Cytochrome P450s are heme-containing enzymes capable of the oxidative transformation of a wide range of organic substrates. A protein scaffold that coordinates the heme iron, and the catalytic pocket residues, together, determine the reaction selectivity and regio- and stereo-selectivity of the P450 enzymes. Different substrates also affect the properties of P450s by binding to its catalytic pocket. Modulating the redox potential of the heme by substituting iron-coordinating residues changes the chemical reaction, the type of cofactor requirement, and the stereoselectivity of P450s. Around hundreds of P450s are experimentally characterized, therefore, a mechanistic understanding of the factors affecting their catalysis is increasingly vital in the age of synthetic biology and biotechnology. Engineering P450s can enable them to catalyze a variety of chemical reactions viz. oxygenation, peroxygenation, cyclopropanation, epoxidation, nitration, etc., to synthesize high-value chiral organic molecules with exceptionally high stereo- and regioselectivity and catalytic efficiency. This review will focus on recent studies of the mechanistic understandings of the modulation of heme redox potential in the engineered P450 variants, and the effect of small decoy molecules, dual function small molecules, and substrate mimetics on the type of chemical reaction and the catalytic cycle of the P450 enzymes." @default.
- W4313260075 created "2023-01-06" @default.
- W4313260075 creator A5001312801 @default.
- W4313260075 creator A5005438120 @default.
- W4313260075 creator A5006829613 @default.
- W4313260075 creator A5017855231 @default.
- W4313260075 creator A5049855626 @default.
- W4313260075 creator A5070350230 @default.
- W4313260075 date "2022-12-22" @default.
- W4313260075 modified "2023-09-25" @default.
- W4313260075 title "Hijacking Chemical Reactions of P450 Enzymes for Altered Chemical Reactions and Asymmetric Synthesis" @default.
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