AI Article Synopsis
- Non-ribosomal peptide synthesis generates various bioactive peptides through a modular system of catalytic domains that create diverse sequences.
- The chapter describes an in vitro biochemical assay designed to investigate the substrate specificity of condensation domains, which are crucial for elongating peptides.
- This assay simplifies the process by eliminating the need for adjacent adenylation domains and permits the testing of many synthetic substrates.
Article Abstract
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.
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| http://dx.doi.org/10.1016/bs.mie.2024.06.010 | DOI Listing |
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