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

Sara Hoffmann, Hamid-Reza Danesh-Azari, Claudia Spandolf, Martin Weissenborn, Gideon James Grogan, Bernhard Hauer

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)3234–3239
Number of pages6
Issue number20
Publication statusE-pub ahead of print - 6 Sept 2016

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