Biosynthesis of the Fungal Nonribosomal Peptide Penilumamide A and Biochemical Characterization of a Pterin-Specific Adenylation Domain

Abstract

We report the characterization of the penilumamide A biosynthetic gene cluster from the marine-derived fungus Aspergillus flavipes CNL-338. In vitro reconstitution studies demonstrated that three Plm nonribosomal peptide synthetases encoding four modules are required for constructing the lumazine-containing tripeptide. Further investigations using dissected adenylation domains determined substrate specificity for methionine and anthranilic acid and led to the first biochemical characterization of an adenylation domain with selectivity for a pterin-derived building block. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=106 SRC="FIGDIR/small/505926v1_ufig1.gif" ALT="Figure 1"> View larger version (17K): org.highwire.dtl.DTLVardef@dfc4aeorg.highwire.dtl.DTLVardef@e9a4fdorg.highwire.dtl.DTLVardef@14ee7beorg.highwire.dtl.DTLVardef@1508021_HPS_FORMAT_FIGEXP M_FIG C_FIG