caa a22 4500 605502919 CHVBK 20210128100608.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00253-015-6452-1 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6452-1 Tyrosine O -prenyltransferases TyrPT and SirD displaying similar behavior toward unnatural alkyl or benzyl diphosphate as their natural prenyl donor dimethylallyl diphosphate [Elektronische Daten] [Huili Yu, Mike Liebhold, Xiulan Xie, Shu-Ming Li] Prenyltransferases of the dimethylallyltryptophan synthase (DMATS) superfamily are involved in the biosynthesis of secondary metabolites and contribute as modification enzymes significantly to structural diversity of natural products. They show usually broad specificity toward their aromatic substrates with regiospecific prenylations on aromatic rings. However, most members of this superfamily exhibit a high specificity toward their prenyl donors and usually accept exclusively dimethylallyl diphosphate (DMAPP). Recently, several indole prenyltransferases from this family were also demonstrated to accept unnatural DMAPP analogs such as methylallyl, 2-pentenyl and benzyl diphosphate for alkylation, or benzylation of the indole ring. Partial or complete shift of the substitution position was observed for these enzymes. In this study, we report the acceptance of these DMAPP analogs by two tyrosine O-prenyltransferases TyrPT from Aspergillus niger and SirD from Leptosphaeria maculans for alkylation or benzylation of tyrosine and derivatives. NMR and mass spectrometry (MS) analyses of nine isolated enzyme products confirmed the regiospecific O- or N-alkylation or benzylation at position C-4 of the aromatic ring, which is the same prenylation position of these enzymes in the presence of DMAPP. Springer-Verlag Berlin Heidelberg, 2015 DMATS superfamily nationallicence Unnatural alkyl donors nationallicence Tyrosine and derivatives nationallicence Enzyme catalysis nationallicence Yu Huili Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut Liebhold Mike Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut Xie Xiulan Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany aut Li Shu-Ming Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/17(2015-09-01), 7115-7124 0175-7598 99:17<7115 2015 99 253 https://doi.org/10.1007/s00253-015-6452-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6452-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yu Huili Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut NATIONALLICENCE 700 1- Liebhold Mike Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut NATIONALLICENCE 700 1- Xie Xiulan Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany aut NATIONALLICENCE 700 1- Li Shu-Ming Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, 35037, Marburg, Germany aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/17(2015-09-01), 7115-7124 0175-7598 99:17<7115 2015 99 253