S
Simon Waltzer
Researcher at University of Freiburg
Publications - 11
Citations - 164
Simon Waltzer is an academic researcher from University of Freiburg. The author has contributed to research in topics: Hydrolase & Biocatalysis. The author has an hindex of 8, co-authored 11 publications receiving 151 citations.
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Journal ArticleDOI
Regio- and Stereoselective Aliphatic-Aromatic Cross-Benzoin Reaction: Enzymatic Divergent Catalysis.
Maryam Beigi,Ekaterina Gauchenova,Lydia Walter,Simon Waltzer,Fabrizio Bonina,Thomas Stillger,Dörte Rother,Martina Pohl,Michael Müller +8 more
TL;DR: The regio- and stereochemistry of the product in the asymmetric aliphatic-aromatic cross-benzoin reaction can be controlled solely by choice of the appropriate enzyme or enzyme variant.
Journal ArticleDOI
TCA Cycle Involved Enzymes SucA and Kgd, as well as MenD: Efficient Biocatalysts for Asymmetric C–C Bond Formation
TL;DR: Asymmetric mixed carboligation reactions of α-ketoglutarate with different aldehydes were explored with the thiamine diphosphate dependent enzymes SucA, Kgd and MenD to selectively deliver chiral δ-hydroxy-γ-keto acids with moderate to excellent stereoselectivity.
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(S)-Selective MenD variants from Escherichia coli provide access to new functionalized chiral α-hydroxy ketones
Robert Westphal,Simon Waltzer,Ursula Mackfeld,Michael Widmann,Jürgen Pleiss,Maryam Beigi,Michael Müller,Dörte Rother,Martina Pohl +8 more
TL;DR: It is reported the first rationally designed (S)-selective MenD from E. coli for the synthesis of functionalized α-hydroxy ketones by mutation of two amino acids in the active site stereoselectivity of the (R)- selective EcMenD.
Journal ArticleDOI
Tailoring the S‐Selectivity of 2‐Succinyl‐5‐enolpyruvyl‐6‐hydroxy‐3‐cyclohexene‐1‐carboxylate Synthase (MenD) from Escherichia coli
Robert Westphal,Doris Hahn,Ursula Mackfeld,Simon Waltzer,Maryam Beigi,Michael Widmann,Constantin Vogel,Jürgen Pleiss,Michael Müller,Dörte Rother,Martina Pohl +10 more
TL;DR: Opening the S‐pocket and simultaneous destabilization of the R‐pathway provides a potential general new strategy to enhance the S-selectivity of ThDP‐dependent enzymes.
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New Stetter reactions catalyzed by thiamine diphosphate dependent MenD from E. coli.
TL;DR: The unexpected activity of MenD with short-chain α,β-unsaturated acids and derivatives as substrates in Stetter reactions is described, which provides biocatalytic access to new types of products which are not related to the products currently accessible by thiamine diphosphate dependent enzyme catalysis.