Heterologous expression of a cryptic gene cluster from a marine proteobacteriumĪffords new lanthipeptides thalassomonasins A and B. Chanaphat Thetsana, Shinta Ijichi, Issara Kaweewan, Hiroyuki Nakagawa, Shinya Kodani.Journal of the American Chemical Society 2015, 137 Post-translational Introduction of d-Alanine into Ribosomally Synthesized Peptides by the Dehydroalanine Reductase NpnJ. Journal of the American Chemical Society 2016, 138 Leader Peptide Establishes Dehydration Order, Promotes Efficiency, and Ensures Fidelity During Lacticin 481 Biosynthesis. Thibodeaux, Joshua Wagoner, Yi Yu, and Wilfred A.
Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes. Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse. Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products. Journal of the American Chemical Society 2019, 141 Insights into the Dynamic Structural Properties of a Lanthipeptide Synthetase using Hydrogen–Deuterium Exchange Mass Spectrometry. Journal of the American Chemical Society 2020, 142 Promiscuous Enzymes Cooperate at the Substrate Level En Route to Lactazole A. Vinogradov, Morito Shimomura, Naokazu Kano, Yuki Goto, Hiroyasu Onaka, Hiroaki Suga. Mutations in Dynamic Structural Elements Alter the Kinetics and Fidelity of the Multifunctional Class II Lanthipeptide Synthetase, HalM2. Uggowitzer, Yeganeh Habibi, Wanlei Wei, Nicolas Moitessier, Christopher J. 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 Inklaar, Judith Lanooij, Rubén Cebrián, Oscar P.Journal of the American Chemical Society 2021, 143 Substrate Sequence Controls Regioselectivity of Lanthionine Formation by ProcM. Navo, Gonzalo Jiménez-Osés, Raymond Sarksian, Francisco Alberto Fernandez-Lima, Wilfred A. Tung Le, Kevin Jeanne Dit Fouque, Miguel Santos-Fernandez, Claudio D.Lanthipeptides from the Same Core Sequence: Characterization of a Class II Lanthipeptide Synthetase from Microcystis aeruginosa NIES-88. Sha-Sha Zhang, Jiang Xiong, Jiao-Jiao Cui, Kai-Liang Ma, Wen-Liang Wu, Ya Li, Shangwen Luo, Kun Gao, Shi-Hui Dong.Journal of the American Society for Mass Spectrometry 2022, Article ASAP. Trapped Ion Mobility Spectrometry, Ultraviolet Photodissociation, and Time-of-Flight Mass Spectrometry for Gas-Phase Peptide Isobars/Isomers/Conformers Discrimination. This article is cited by 31 publications. Collectively, the data in this study suggest that the high regioselectivity of product formation is governed by the selectivity of the initially formed ring. ProcM was not able to correct the ring topology of incorrectly cyclized intermediates and products, suggesting that thermodynamic control is not operational. Surprisingly, for ProcA3.3 these mutations also altered the regioselectivity of cyclization resulting in a new major product. Mutation of the active site zinc ligands to alanine or the unique zinc ligand Cys971 to histidine resulted in a decrease of the cyclization rate, especially for the second cyclization of the substrates ProcA1.1, ProcA2.8, and ProcA3.3. Despite its structurally diverse set of 30 substrates, the highly substrate-tolerant lanthipeptide synthetase ProcM is shown to display high selectivity for formation of a single product from selected substrates. They contain characteristic lanthionine (Lan) or methyllanthionine (MeLan) structures that contribute to their diverse biological activities. Lanthipeptides are natural products that belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs).