caa a22 4500 605501289 CHVBK 20210128100600.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00253-015-6813-9 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6813-9 Impacts and perspectives of prenyltransferases of the DMATS superfamily for use in biotechnology [Elektronische Daten] [Aili Fan, Julia Winkelblech, Shu-Ming Li] Prenylated compounds are ubiquitously found in nature and demonstrate interesting biological and pharmacological activities. Prenyltransferases catalyze the attachment of prenyl moieties from different prenyl donors to various acceptors and contribute significantly to the structural and biological diversity of natural products. In the last decade, significant progress has been achieved for the prenyltransferases of the dimethylallyltryptophan synthase (DMATS) superfamily. More than 40 members of these soluble enzymes are identified in microorganisms and characterized biochemically. These enzymes were also successfully used for production of a large number of prenylated derivatives. N1-, C4-, C5-, C6-, and C7-prenylated tryptophan and N1-, C2-, C3-, C4-, and C7-prenylated tryptophan-containing peptides were obtained by using DMATS enzymes as biocatalysts. Tyrosine and xanthone prenyltransferases were used for production of prenylated derivatives of their analogs. More interestingly, the members of the DMATS superfamily demonstrated intriguing substrate and catalytic promiscuity and also used structurally quite different compounds as prenyl acceptors. Prenylated hydroxynaphthalenes, flavonoids, indolocarbazoles, and acylphloroglucinols, which are typical bacterial or plant metabolites, were produced by using several fungal DMATS enzymes. Furthermore, the potential usage of these enzymes was further expanded by using natural or unnatural DMAPP analogs as well as by coexpression with other genes like NRPS and by development of whole cell biocatalyst. Springer-Verlag Berlin Heidelberg, 2015 Biocatalyst nationallicence Chemoenzymatic synthesis nationallicence Dimethylallyltryptophan synthase nationallicence Friedel-Crafts alkylation nationallicence Prenylated compound nationallicence Prenyltransferase nationallicence Fan Aili Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut Winkelblech Julia Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut Li Shu-Ming Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/18(2015-09-01), 7399-7415 0175-7598 99:18<7399 2015 99 253 https://doi.org/10.1007/s00253-015-6813-9 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6813-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Fan Aili Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut NATIONALLICENCE 700 1- Winkelblech Julia Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut NATIONALLICENCE 700 1- Li Shu-Ming Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/18(2015-09-01), 7399-7415 0175-7598 99:18<7399 2015 99 253