Premium
Structure‐Guided Redesign of CYP153A M.aq for the Improved Terminal Hydroxylation of Fatty Acids
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 - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201600680
Subject(s) - hydroxylation , substrate (aquarium) , chemistry , fatty acid , terminal (telecommunication) , stereochemistry , heme , side chain , arginine , combinatorial chemistry , biochemistry , enzyme , amino acid , organic chemistry , biology , computer science , ecology , telecommunications , polymer
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 K M 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.