Accessing natural product biosynthetic processes by mass spectrometry.

Current Opinion in Chemical Biology
Stefanie B Bumpus, Neil L Kelleher

Abstract

Two important classes of natural products are made by nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs). With most biosynthetic intermediates covalently tethered during biogenesis, protein mass spectrometry (MS) has proven invaluable for their interrogation. New mass spectrometric assay formats (such as selective cofactor ejection and proteomics style LC-MS) are showcased here in the context of functional insights into new breeds of NRPS/PKS enzymes, including the first characterization of an 'iterative' PKS, the biosynthesis of the enediyne antitumor antibiotics, the study of a new strategy for PKS initiation via a GNAT-like mechanism, and the analysis of branching strategies in the so-called 'AT-less' NRPS/PKS hybrid systems. The future of MS analysis of NRPS and PKS biosynthetic pathways lies in adoption and development of methods that continue bridging enzymology with proteomics as both fields continue their post-genomic acceleration.

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Citations

Sep 19, 2012·Analytical Chemistry·Rebecca H WillsPeter B O'Connor
Feb 14, 2009·Journal of Natural Products·John A KalaitzisBradley S Moore
Oct 1, 2014·Journal of Chromatography. a·Saikat HaldarHirekodathakallu V Thulasiram
Aug 12, 2009·Journal of Mass Spectrometry : JMS·Ivica Kopriva, Ivanka Jerić
May 13, 2014·Current Opinion in Biotechnology·Sean PoustJay D Keasling
Nov 23, 2010·Current Opinion in Chemical Biology·Jordan L Meier, Michael D Burkart
Jan 26, 2017·Chemical Communications : Chem Comm·Judith HavemannManuela Tosin
Feb 6, 2010·Chembiochem : a European Journal of Chemical Biology·Manuela TosinPeter F Leadlay
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Aug 24, 2021·ACS Chemical Biology·Lauren A WashburnCoran M H Watanabe
Nov 20, 2014·Journal of the American Chemical Society·Gaurav ShakyaMichael D Burkart

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