Abstract
AbstractThe catalytic space of the P450 monooxygenase CYP153AM.aq was opened from a terminal (ω‐) fatty acid hydroxylase to a catalyst capable of performing ω‐hydroxylation of dodecylamine, which is a potent inhibitor for the wild‐type enzyme. A simple screening method named Rapid‐flow Analysis of Product Peaks (RAPP) was established and applied to measure saturation libraries directly from a 96‐deepwell plate in 36 seconds per sample. The obtained variants are less inhibited by the amine, although concurrently show less affinity towards the acid. Molecular modelling and molecular dynamics simulations showed significant effects of the mutations on the substrate tunnel architectures.
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