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© Jean Marc Panaud
Cyanobactérie souche "PCC 9401". Souche de la "Pasteur Culture Collection of Cyanobacteria" conservée à l'état axénique dans l'Unité des Cyanobactéries. La PCC est l'une des Collections spécialisées de l'Institut Pasteur.
Publication : Angewandte Chemie (International ed. in English)

Genome-Mining-Based Discovery of the Cyclic Peptide Tolypamide and TolF, a Ser/Thr Forward O-Prenyltransferase.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Angewandte Chemie (International ed. in English) - 06 Apr 2021

Purushothaman M, Sarkar S, Morita M, Gugger M, Schmidt EW, Morinaka BI,

Link to Pubmed [PMID] – 33586286

Link to DOI – 10.1002/anie.202015975

Angew Chem Int Ed Engl 2021 04; 60(15): 8460-8465

Cyanobactins comprise a widespread group of peptide metabolites produced by cyanobacteria that are often diversified by post-translational prenylation. Several enzymes have been identified in cyanobactin biosynthetic pathways that carry out chemically diverse prenylation reactions, representing a resource for the discovery of post-translational alkylating agents. Here, genome mining was used to identify orphan cyanobactin prenyltransferases, leading to the isolation of tolypamide from the freshwater cyanobacterium Tolypothrix sp. The structure of tolypamide was confirmed by spectroscopic methods, degradation, and enzymatic total synthesis. Tolypamide is forward-prenylated on a threonine residue, representing an unprecedented post-translational modification. Biochemical characterization of the cognate enzyme TolF revealed a prenyltransferase with strict selectivity for forward O-prenylation of serine or threonine but with relaxed substrate selectivity for flanking peptide sequences. Since cyanobactin pathways often exhibit exceptionally broad substrate tolerance, these enzymes represent robust tools for synthetic biology.

https://pubmed.ncbi.nlm.nih.gov/33586286