Functional Expression and Characterization of the Highly Promiscuous Lanthipeptide Synthetase SyncM, Enabling the Production of Lanthipeptides with a Broad Range of Ring Topologies
Patricia Arias-Orozco, Maartje R. Inklaar, Judith Lanooij, Rubén Cebrián, Oscar P. Kuipers
Abstract
MITS9509. We have characterized the functionality of SyncM by the successful expression of 15 out of 18 different SyncA substrates, subsequently determining the dehydration and cyclization processes in six representatives of them. This characterization highlights the very relaxed substrate specificity of SyncM toward its precursors and the ability to catalyze the formation of exceptionally large rings in a variety of topologies. Our results suggest that SyncM could be an attractive enzyme to design and produce a wide variety of new-to-nature lanthipeptides with a broad range of ring topologies.
Topics & Concepts
Heterologous expressionSynthetic biologyLactococcus lactisHeterologousBiochemistryBiologyLantibioticsEnzymeBiosynthesisSubstrate (aquarium)LanthionineComputational biologyCombinatorial chemistryChemistryAmino acidBacteriaGeneRecombinant DNAGeneticsNisinLactic acidEcologyMicrobial Natural Products and BiosynthesisBiochemical and Structural CharacterizationChemical Synthesis and Analysis