Fig. 1
From: Reprogramming of the antimycin NRPS-PKS assembly lines inspired by gene evolution
Organization of modular enzymes involved in the biosynthesis of antimycin-type depsipeptides. C condensation, A adenylation, T thiolation, KR ketoreductase, KS ketosynthase, AT acyltransferase, ACP acyl carrier protein, MT methyltransferase, TE thioesterase, CCR crotonyl-CoA reductase/carboxylase, R1 and R2 various alkyl groups, Rstarter the acyl moiety of 3-FSA. The module and domain organizations of the starter, the module 1, and the module 2 are identical among the all three systems. The starter and the module 1 uptake 3-FSA and L-threonine, respectively, common to all pathways, but the module 2 uptake pyruvate (AntC), isoleucic acid (SmlB), and valic acid (NatB), respectively. JBIR-06 and neoantimycin systems include an additional NRPS modules (module 3) after the module 2 in the same ORF. The module 3 in SmlB uptakes phenylpyruvic acid, and the module 3 in NatB uptakes leucic acid. The PKS modules of JBIR-06 and neoantimycin systems (module 4) contain MT domain between AT and ACP, and accept malonyl-CoA as an extender unit, to yield dimethyl group at the α-position of polyketide moiety, differently from antimycin system. Furthermore, neoantimycin system includes an extra NRPS module (module 5 as NatD) which uptakes isoleucic acid or valic acid
