Interpretation of antiSMASH results and proposed biosynthetic origins of basiliskamides A (1) and B (2) and auriporcine (6).

<p>Panel A illustrates the biosynthetic gene cluster hypothesized to be responsible for the production of 6. Adenylation domains are labeled with the amino acids they are predicted to contribute. The two domains potentially involved in loading of the L-leucine residues are contained in the shaded box. The additional domains shaded grey are believed not to be involved in the production of 6 or were incorporated, but later removed from the metabolite. Panel B shows the organization of the putative basiliskamide gene cluster, as well as a proposed biosynthetic scheme for the production of the polyketide portions of 1 and 2. The fused, tandem AT domains are separate from the other modules. The dehydrating bimodule is shown split, as the gene that encodes the two KS domains are separated from the dehydrogenase and ketoreductase. The genes encoding the predicted aminotransferase, condensation, and adenylation domains (hypothesized to transform the amide and add the cinnamic acid moieties to the polyketide chain) are labeled. The putative functions of the genes are indicated as A (adenylation), C (condensation), KR (ketoreductase), E (epimerization), GNAT (GCN5-related acetyltransferase), KS (ketosynthase), ER (enolreductase), MT (methyltransferase), DH (dehydrogenase), and AT (acetyltransferase).