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Cover Picture: Structure‐Guided Redesign of CYP153A M.aq for the Improved Terminal Hydroxylation of Fatty Acids (ChemCatChem 20/2016)
Author(s) -
Hoffmann Sara M.,
DaneshAzari HamidReza,
Spandolf Claudia,
Weissenborn Martin J.,
Grogan Gideon,
Hauer Bernhard
Publication year - 2016
Publication title -
chemcatchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201601209
Subject(s) - substrate (aquarium) , chemistry , active site , fatty acid , hydroxylation , stereochemistry , enzyme , protein engineering , mutagenesis , organic chemistry , biochemistry , biology , ecology , gene , mutation
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 CYP153A M.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).