An in vitro assay to explore condensation domain specificity from non-ribosomal peptide synthesis.
Condensation domain
Fuscachelin
NRPS
Non-ribosomal peptide synthesis
SpyTag/SpyCatcher
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
19
8
2024
pubmed:
19
8
2024
entrez:
18
8
2024
Statut:
ppublish
Résumé
Non-ribosomal peptide synthesis produces a wide range of bioactive peptide natural products and is reliant on a modular architecture based on repeating catalytic domains able to generate diverse peptide sequences. In this chapter we detail an in vitro biochemical assay to explore the substrate specificity of condensation domains, which are responsible for peptide elongation, from the biosynthetic machinery that produces from the siderophore fuscachelin. This assay removes the requirement to utilise the specificity of adjacent adenylation domains and allows the acceptance of a wide range of synthetic substrates to be explored.
Identifiants
pubmed: 39155122
pii: S0076-6879(24)00303-3
doi: 10.1016/bs.mie.2024.06.010
pii:
doi:
Substances chimiques
Siderophores
0
Peptide Synthases
EC 6.3.2.-
Peptides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
89-119Informations de copyright
Copyright © 2024. Published by Elsevier Inc.