Simon Waltzer

发表

Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C–C-bonding reactions

G. Sprenger, Michael Müller, Matthias Schapfl, 2018, Applied Microbiology and Biotechnology.

Elucidation of the Enantioselective Cyclohexane‐1,2‐dione Hydrolase Catalyzed Formation of (S)‐Acetoin

V. Brecht, Michael Müller, S. Loschonsky, 2014 .

Abstract 4858: LADR™: A novel linker activated drug release technology for drug delivery

F. Kratz, A. Warnecke, F. I. Nollmann, 2016 .

Tailoring the S‐Selectivity of 2‐Succinyl‐5‐enolpyruvyl‐6‐hydroxy‐3‐cyclohexene‐1‐carboxylate Synthase (MenD) from Escherichia coli

J. Pleiss, D. Rother, Michael Müller, 2013 .

Regio- and Stereoselective Aliphatic-Aromatic Cross-Benzoin Reaction: Enzymatic Divergent Catalysis.

Dörte Rother, Martina Pohl, Michael Müller, 2016, Chemistry.

Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.

S. Andrade, M. McLeish, Michael Müller, 2014, Angewandte Chemie.

TCA cycle involved enzymes SucA and Kgd, as well as MenD: efficient biocatalysts for asymmetric C-C bond formation.

L. Eggeling, G. Sprenger, Michael Müller, 2013, Organic letters.

New Stetter reactions catalyzed by thiamine diphosphate dependent MenD from E. coli.

Michael Müller, Mostafa Zarei, Michael Müller, 2014, Journal of biotechnology.

Catalytic Scope of the Thiamine‐Dependent Multifunctional Enzyme Cyclohexane‐1,2‐dione Hydrolase

S. Andrade, P. Kroneck, Michael Müller, 2014, Chembiochem : a European journal of chemical biology.

Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C–C-bonding reactions

G. Sprenger, Michael Müller, Matthias Schapfl, 2018, Applied Microbiology and Biotechnology.