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Structure-Guided Redesign of CYP153AM.aq for the Improved Terminal Hydroxylation of Fatty Acids

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JournalChemCatChem
DateE-pub ahead of print - 6 Sep 2016
Issue number20
Volume8
Number of pages6
Pages (from-to)3234–3239
Original languageEnglish

Abstract

The structure of a P450 ω-hydroxylase bound to its fatty acid product was determined, which revealed a narrow substrate tunnel that leads to the heme. The introduction of an arginine side chain in proximity to the carboxyl group of the fatty acid led to a reduced KM value for dodecanoic acid, which suggests the importance of an anchoring point in the active site. An increase in the flexibility of the substrate recognition region was also engineered, which resulted in a threefold improved product formation.

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© 2016, Wiley-VCH Verlag GmbH & Co. K. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

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