caa a22 4500 605501297 CHVBK 20210128100600.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00253-015-6811-y doi (NATIONALLICENCE)springer-10.1007/s00253-015-6811-y Prenyltransferases as key enzymes in primary and secondary metabolism [Elektronische Daten] [Julia Winkelblech, Aili Fan, Shu-Ming Li] Attachment of isoprene units to various acceptors by prenylation plays an important role in primary and secondary metabolism of living organisms. Protein prenylation belongs to posttranslational modification and is involved in cellular regulation process. Prenylated secondary metabolites usually demonstrate promising biological and pharmacological activities. Prenyl transfer reactions catalyzed by prenyltransferases represent the key steps in the biosynthesis and contribute significantly to the structural and biological diversity of these compounds. In the last decade, remarkable progress has been achieved in the biochemical, molecular, and structural biological investigations of prenyltransferases, especially on those of the members of the dimethylallyltryptophan synthase (DMATS) superfamily. Until now, more than 40 of such soluble enzymes are identified and characterized biochemically. They catalyze usually regioselective and stereoselective prenylations of a series of aromatic substances including tryptophan, tryptophan-containing peptides, and other indole derivatives as well as tyrosine or even nitrogen-free substrates. Crystal structures of a number of prenyltransferases have been solved in the past 10 years and provide a solid basis for understanding the mechanism of prenyl transfer reactions. Springer-Verlag Berlin Heidelberg, 2015 Aromatic prenyltransferase nationallicence Dimethylallyltryptophan synthase nationallicence Peptide prenyltransferase nationallicence Phylogenetic relationships nationallicence Prenyl diphosphate synthase nationallicence Protein prenyltransferase nationallicence tRNA prenyltransferase nationallicence Winkelblech Julia Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut Fan Aili 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), 7379-7397 0175-7598 99:18<7379 2015 99 253 https://doi.org/10.1007/s00253-015-6811-y 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/s00253-015-6811-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Winkelblech Julia Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, D-35037, Marburg, Germany aut NATIONALLICENCE 700 1- Fan Aili 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), 7379-7397 0175-7598 99:18<7379 2015 99 253