Inverting the enantioselectivity of P450pyr monooxygenase by directed evolutionwz
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منابع مشابه
Inverting the enantioselectivity of P450pyr monooxygenase by directed evolution.
We report the first example of directed evolution of a P450 monooxygenase with inverted enantioselectivity for asymmetric biohydroxylation. The biohydroxylation product of the best mutant 1AF4A has an ee of 83% (R) compared to the wild type's ee of 43% (S).
متن کاملEngineered P450pyr monooxygenase for asymmetric epoxidation of alkenes with unique and high enantioselectivity.
A triple mutant of P450pyr monooxygenase (P450pyrTM) catalysed the epoxidation of several para-substituted styrenes as the first enzyme showing high (R)-enantioselectivity and high conversion, demonstrated a broad substrate range, and showed high enantioselectivity for the epoxidation of an unconjugated 1,1-disubstituted alkene, 2-methyl-3-phenyl-1-propene, and a cyclic alkene, N-phenoxycarbony...
متن کاملEvolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.
Directed evolution of a monooxygenase to achieve very high enantioselectivity for hydroxylation at non-activated carbon atoms is demonstrated for the first time, where a triple mutant of P450pyr hydroxylase is obtained via determination of enzyme structure, iterative saturation mutagenesis, and high-throughput screening with a MS-based ee assay to increase the product ee from 53% to 98% for the...
متن کاملEvolving P450pyr monooxygenase for highly regioselective terminal hydroxylation of n-butanol to 1,4-butanediol.
Directed evolution of P450pyr created I83M/I82T mutant for highly regioselective terminal hydroxylation of n-butanol to 1,4-butanediol, representing the first achievement of this hydroxylation reaction by chemical or enzymatic methods and an unique example of evolving a hydroxylase to switch the substrate acceptance from a hydrophobic to hydrophilic compound.
متن کاملInduced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase.
The molecular basis of allosteric effects, known to be caused by an effector docking to an enzyme at a site distal from the binding pocket, has been studied recently by applying directed evolution. Here, we utilize laboratory evolution in a different way, namely to induce allostery by introducing appropriate distal mutations that cause domain movements with concomitant reshaping of the binding ...
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تاریخ انتشار 2010