Fig. 3: Generality of the chemoenzymatic strategy.
From: Non-ribosomal peptide cyclase-directed chemoenzymatic synthesis of lariat lipopeptides
a, The structure of the l-Trp1′-l-Lys dipeptide unit used to install the pseudo-N terminus. b, Wollamide B1-based branched EG-functionalized substrates 12–16 were synthesized to assess the effect of distance between the pseudo-N terminus and C terminus. c, Conversions of 12–16 using WolJ in the absence and presence of 50% DMSO. The conversions to macrocyclization (orange) and EG hydrolysis (blue) products are shown. d, Structures of cyc-12–16. The Cα atoms of d-aa and l-aa at the substrate termini are highlighted by magenta and purple circles, respectively. The ring sizes are indicated in circles in the structures. e, TycC-TE-mediated cyclization of the branched substrate 17. The conversion in buffer containing 50% DMSO is indicated. f, Effect of distance between termini on the TycC-TE-mediated cyclization of the branched substrates 18–20. The structure of tyrocidine A is shown for comparison. Conversions are indicated. aYield in buffer excluding DMSO. bYield in buffer containing 50% DMSO. g, WolJ-mediated cyclization of branched substrate 28. The conversion in buffer containing 60% DMSO is indicated. C-terminal Gly is highlighted with a grey circle. h, Structure of wollamide B.
