Exploring the Heterogeneous Structural Dynamics of Class II Lanthipeptide Synthetases with Hydrogen–Deuterium Exchange Mass Spectrometry (HDX-MS)
Author:
Affiliation:
1. Department of Chemistry, McGill University, 801 Sherbrooke St., Montreal, Quebec H3A0B8, Canada
Funder
Fonds de Recherche du Qu?bec - Sant?
Fonds de Recherche du Qu?bec - Nature et Technologies
Natural Sciences and Engineering Research Council of Canada
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00360
Reference58 articles.
1. Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes
2. The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold
3. Product Formation by the Promiscuous Lanthipeptide Synthetase ProcM is under Kinetic Control
4. Evolution of lanthipeptide synthetases
5. Substrate Sequence Controls Regioselectivity of Lanthionine Formation by ProcM
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1. The conformationally dynamic structural biology of lanthipeptide biosynthesis;Current Opinion in Structural Biology;2023-08
2. Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL;Angewandte Chemie International Edition;2023-04-27
3. Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL;Angewandte Chemie;2023-04-27
4. Developments in rapid hydrogen–deuterium exchange methods;Essays in Biochemistry;2023-03
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