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Cover Picture: Tailoring the S ‐Selectivity of 2‐Succinyl‐5‐enolpyruvyl‐6‐hydroxy‐3‐cyclohexene‐1‐carboxylate Synthase (MenD) from Escherichia coli (ChemCatChem 12/2013)
Author(s) -
Westphal Robert,
Hahn Doris,
Mackfeld Ursula,
Waltzer Simon,
Beigi Maryam,
Widmann Michael,
Vogel Constantin,
Pleiss Jürgen,
Müller Michael,
Rother Dörte,
Pohl Martina
Publication year - 2013
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.201390058
Subject(s) - chemistry , selectivity , steric effects , enzyme , stereochemistry , substrate (aquarium) , carboxylate , atp synthase , enantiomer , biocatalysis , escherichia coli , combinatorial chemistry , biochemistry , catalysis , gene , biology , reaction mechanism , ecology
Stereoselective traffic engineering The cover picture shows how engineered S ‐selective Ec MenD variants catalyze the carboligation of α‐ketoglutarate and benzaldehyde derivatives with excellent enantioselectivities of up to 99 % ee S , in contrast to the wild‐type enzyme, which produces R ‐enantiomers. In their Full Paper on p. 3587 ff. , M. Pohl et al. describe how they engineer S ‐selective Ec MenD variants by optimizing steric properties and stabilization of the acceptor substrate in the S ‐pocket. This method, inspired by the recently developed S ‐pocket concept, involves opening the S ‐pocket with simultaneous destabilization of the R ‐pathway to enhance the S ‐selectivity of thiamine diphosphate‐dependent enzymes.
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