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Substrate Specificity in Ketosynthase Domains from trans‐ AT Polyketide Synthases
Author(s) -
Jenner Matthew,
Frank Sarah,
Kampa Annette,
Kohlhaas Christoph,
Pöplau Petra,
Briggs Geoff S.,
Piel Jörn,
Oldham Neil J.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201207690
Subject(s) - polyketide , steric effects , residue (chemistry) , stereochemistry , branching (polymer chemistry) , chemistry , substrate specificity , substrate (aquarium) , biochemistry , biology , biosynthesis , enzyme , organic chemistry , ecology
Branching out : The substrate specificity profiles for a range of ketosynthase (KS) domains from trans ‐AT PKSs are reported. Evidence is provided that a sterically demanding amino acid residue adjacent to the active‐site Cys residue confers specificity towards non‐β‐methyl‐branched substrates (see scheme).