(822.6) PEARL mediated biosynthesis: a novel pathway to aromatic amines

Poster Board Number: A446

Page Daniels (University of Illinois at Urbana Champaign), Hyunji Lee (University of Illinois at Urbana Champaign), Chi Ting (University of Illinois at Urbana Champaign), Lingyang Zhu (University of Illinois at Urbana Champaign), Wilfred van der Donk (University of Illinois at Urbana Champaign)

Aromatic amines are common functional groups found in several metabolites. The biosynthesis of aromatic amines canonically involves amino group installation prior to aromatization. We report a fundamentally distinct pathway to aromatic amines by conversion of phenolic groups to amines. Recent studies identified the use of short, catalytic scaffold peptides for the biosynthesis of amino acid derived natural products. During this process, a peptide-amino acyl tRNA ligase (PEARL) appends amino acids to the C-terminus of a ribosomally synthesized peptide in an ATP- and tRNA-dependent manner. We report two pathways in which the short, ribosomally synthesized peptides serve as the scaffold for downstream enzymes to modify a PEARL-appended tryptophan into a pyrroloiminoquinone. These pathways feature previously unknown biochemical processes using a ribosomally synthesized peptide as a scaffold for non-ribosomal peptide extension and chemical modification to generate an amino acid derived natural product. These pathways showcase a new use for PEARLs resulting in the amination of indoles.

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Howard Hughes Medical Institute, Chemistry and Biology Interface Program



Novel pathway to aromatic amines reveals key insights into pyrroloiminoquinone biosynthesis