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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The front cover artwork for Issue 20/2016 is provided by researchers from the Universität Stuttgart (Germany) and the University of York (United Kingdom). The image shows a free fatty acid substrate which drops into the active site of a P450 enzyme in an aqueous solution. The fatty acid is kept in the splash through the specific structural elements of the enzyme. See the Full Paper itself at http://dx.doi.org/10.1002/cctc.201600680.

The Front Cover shows a free fatty acid substrate which drops into the active site of a P450 enzyme in an aqueous solution. The fatty acid is kept in the splash through the specific structural elements of the enzyme.In their Full Paper, S. M. Hoffmann et al. present the crystal structure of the fatty acid ω‐hydroxylase CYP153AM.aq and a structural based mutagenesis study. The narrow substrate binding pocket was found to be necessary for the selective terminal hydroxylation of fatty acids. Engineering the substrate recognition region a threefold improved product formation was achieved. The authors identified an anchoring point which resulted in an enzyme variant with better binding of the substrate carboxyl group in the active site. More information can be found in the Full Paper by S. M. Hoffmann et al. on page 3234 in Issue 20, 2016 (DOI: 10.1002/cctc.201600680).

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