title: Expansion of enzymatic Friedel-Crafts alkylation on indoles: acceptance of unnatural β-unsaturated allyl diphospates by dimethylallyl-tryptophan synthases.
abstract: Prenyltransferases of the dimethylallyl-tryptophan synthase (DMATS) superfamily catalyze Friedel-Crafts alkylation with high flexibility for aromatic substrates, but the high specificity for dimethylallyl diphosphate (DMAPP) prohibits their application as biocatalysts. We demonstrate here that at least one methyl group in DMAPP can be deleted or shifted to the δ-position. For acceptance by some DMATS enzymes, however, a double bond must be situated at the β-position. Furthermore, the alkylation position of an analogue can differ from that of DMAPP.
authors.affiliation: Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17a, 35037 Marburg, Germany.
authors.forename: Mike
authors.initials: M
authors.lastname: Liebhold
authors.forename: Xiulan
authors.initials: X
authors.lastname: Xie
authors.forename: Shu-Ming
authors.initials: SM
authors.lastname: Li
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry / Q000378:metabolism*; D000478:Alkylation; D002384:Catalysis; D004122:Dimethylallyltranstransferase / Q000737:chemistry / Q000378:metabolism*; D007211:Indoles / Q000737:chemistry*; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D014364:Tryptophan / Q000737:chemistry
chemical_list: D007211:Indoles; D014364:Tryptophan; D019883:Alkyl and Aryl Transferases; D004122:Dimethylallyltranstransferase; C032409:tryptophan dimethylallyltransferase