Projects per year
Abstract
Nonribosomal peptide biosynthesis is a complex enzymatic assembly responsible for producing a great diversity of bioactive peptide natural products. Due to the recurring arrangement of catalytic domains within these machineries, great interest has been shown in reengineering these pathways to produce novel, designer peptide products. However, in order to realize such ambitions, it is first necessary to develop a comprehensive understanding of the selectivity, mechanisms, and structure of these complex enzymes, which in turn requires significant in vitro experiments. Within nonribosomal biosynthesis, some modifications are performed by enzymatic domains that are not linked to the main nonribosomal peptide synthetase but rather act in trans: these systems offer great potential for redesign, but in turn require detailed study. In this chapter, we present an overview of in vitro experiments that can be used to characterize examples of such trans-interacting enzymes from nonribosomal peptide biosynthesis: Cytochrome P450 monooxygenases and flavin-dependent halogenases.
Original language | English |
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Title of host publication | Metabolons and Supramolecular Enzyme Assemblies |
Editors | Claudia Schmidt-Dannert, Maureen B. Quin |
Publisher | Academic Press |
Chapter | 6 |
Pages | 113-154 |
Number of pages | 42 |
ISBN (Print) | 9780128170748 |
DOIs | |
Publication status | Published - 1 Jan 2019 |
Publication series
Name | Methods in Enzymology |
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Volume | 617 |
ISSN (Print) | 0076-6879 |
ISSN (Electronic) | 1557-7988 |
Keywords
- Carrier protein
- Cytochrome P450
- Halogenase
- Nonribosomal peptide synthetase
- trans-interacting enzyme
Projects
- 1 Finished
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ARC Centre of Excellence in Advanced Molecular Imaging
Whisstock, J., Abbey, B., Nugent, K., Quiney, H. M., Godfrey, D. I., Heath, W., Fairlie, D., Chapman, H., Peele, A., Davey, J. & Wittmann, A.
30/06/14 → 31/03/21
Project: Research