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. Author manuscript; available in PMC: 2021 Oct 1.
Published in final edited form as: Curr Opin Chem Biol. 2020 Aug 4;58:45–53. doi: 10.1016/j.cbpa.2020.06.003

Figure 3.

Figure 3.

Hybrid synthases of the venemycin PKS (top) were constructed with traditional domain boundaries between the KS and ACP (middle). Module swaps were then constructed using boundaries between the KS and AT (gray box). The new boundary definition resulted in a chimera that was several-fold faster than its traditional boundary counterpart. A (adenylation domain), KR (Ketoreductase), ACP (acyl carrier protein), KS (ketosynthase), AT (acyltransferase), TE (thioesterase), KSQ (ketosynthase-like decarboxylase), KR0 (inactive ketoreductase).