Sylwia Tarcz

Structure-function analysis of an enzymatic prenyl transfer reaction identifies a reaction chamber with modifiable specificity.

T. Stehle, G. Zocher, M. Jost, 2010, Journal of the American Chemical Society.

AstPT Catalyses both Reverse N1‐ and Regular C2 Prenylation of a Methylated Bisindolyl Benzoquinone

Shu‐Ming Li, L. Ludwig, Sylwia Tarcz, 2014, Chembiochem : a European journal of chemical biology.

Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase

Xiulan Xie, Shu‐Ming Li, Sylwia Tarcz, 2014 .

Mutation on Gly115 and Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 increases its catalytic activity toward hydroxynaphthalenes

Wei Zhao, Shu‐Ming Li, W. Yin, 2017, Applied Microbiology and Biotechnology.

Structure-function analysis of an enzymatic prenyl transfer reaction identifies a reaction chamber with modifiable specificity.

T. Stehle, G. Zocher, M. Jost, 2010, Journal of the American Chemical Society.