Chapter title |
The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.
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Book title |
Non-Ribosomal Peptide Biosynthesis and Engineering
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Published in |
Methods in molecular biology, January 2023
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DOI | 10.1007/978-1-0716-3214-7_1 |
Pubmed ID | |
Book ISBNs |
978-1-07-163213-0, 978-1-07-163214-7
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Authors |
Maruyama, Chitose, Hamano, Yoshimitsu |
Abstract |
Peptide natural products constitute a major class of secondary metabolites produced by microorganisms (mostly bacteria and fungi). In the past several decades, researchers have gained extensive knowledge about nonribosomal peptides (NRPs) generated by ribosome-independent systems, namely, NRP synthetases (NRPSs). NRPSs are multifunctional enzymes consisting of semiautonomous domains that form a peptide backbone. Using a thiotemplate mechanism that employs assembly-line logic with multiple modules, NRPSs activate, tether, and modify amino acid building blocks, sequentially elongating the peptide chain before releasing the complete peptide. Adenylation, thiolation, condensation, and thioesterase domains play central roles in these reactions. This chapter focuses on the current understanding of these central domains in NRPS assembly-line enzymology. |
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