An Orthogonal D 2 O-Based Induction System that Provides Insights into d -Amino Acid Pattern Formation by Radical S-Adenosylmethionine Peptide Epimerases

Brandon I. Morinaka 1 Marjan Verest 1 Michael F. Freeman 1 Muriel Gugger 2 Jörn Piel 1, *
* Auteur correspondant
1 ETH Zürich - Eidgenössische Technische Hochschule [Zürich]
2 Collection des Cyanobactéries
Abstract : Radical S-adenosyl methionine peptide epimerases (RSPEs) are an enzyme family that accomplishes regiospecific and irreversible introduction of multiple d-configured residues into ribosomally encoded peptides. Collectively, RSPEs can generate diverse epimerization patterns in a wide range of substrates. Previously, the lack of rapid methods to localize epimerized residues has impeded efforts to investigate the function and applicative potential of RSPEs. An efficient mass spectrometry-based assay is introduced that permits characterization of products generated in E. coli. Applying this to a range of non-natural peptide-epimerase combinations, it is shown that the d-amino acid pattern is largely but not exclusively dictated by the core peptide sequence, while the epimerization order is dependent on the enzyme-leader pair. RSPEs were found to be highly promiscuous, which allowed for modular introduction of peptide segments with defined patterns.
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Angewandte Chemie International Edition, Wiley-VCH Verlag, 2016, 55, 〈10.1002/anie.201609469〉
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01416272
Contributeur : Bénédicte Benedic <>
Soumis le : lundi 26 décembre 2016 - 15:56:10
Dernière modification le : mardi 27 décembre 2016 - 01:02:56

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Brandon I. Morinaka, Marjan Verest, Michael F. Freeman, Muriel Gugger, Jörn Piel. An Orthogonal D 2 O-Based Induction System that Provides Insights into d -Amino Acid Pattern Formation by Radical S-Adenosylmethionine Peptide Epimerases. Angewandte Chemie International Edition, Wiley-VCH Verlag, 2016, 55, 〈10.1002/anie.201609469〉. 〈pasteur-01416272〉

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