Our knowledge of the extent and diversity of natural products produced via the post-translational modification of peptides is in a growth phase. While the majority of such products retain their peptidic nature, PQQ is constructed solely from the backbones of two amino acids and is devoid of a peptide bond. Yet commonalities exist among many of the RiPP pathways that include the requirement for N-terminal peptide binding motifs (either as stand-alone proteins or via the N-terminal domain of specific enzymatic functions) and the frequent involvement of free radical generating chemical reactions. This presentation will focus on the early steps in PQQ biosynthesis, in particular the interaction between substrate, PqqA, its chaperone, PqqD, and the RS enzyme, PqqE.

Pathway for production of the bacterial cofactor pyrroloquinoline quinone (PQQ): At the confluence of radical SAM (RS) enzymes and ribosomally synthesized and post-translationally modified peptides (RiPPs)

254th National Meeting (2017)

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