Projects per year
Abstract
Polyketides are a structurally and functionally diverse family of bioactive natural products that have proven to be a rich source of pharmaceutical and agrochemical lead compounds. Many polyketides are biosynthesized by large multifunctional megaenzymes termed type 1 modular polyketide synthases (PKSs). These systems possess a distinctive assembly line-like architecture, comprising a series of linearly arranged, multi-domain extension modules, housed in sequence within giant polypeptide chains. Due to their inherently modular structures, PKSs represent attractive targets for re-engineering, enabling access to functionally optimized ‘non-natural’ natural products. In this chapter we describe methods for the molecular cloning, recombinant over-expression, and purification of intact PKS modules and multi-modular PKS polypeptides. The usefulness of these methods is demonstrated by applying them to the study of the abyssomicin C PKS, a >1 MDa multi-modular synthase responsible for the biosynthesis of a polyketide antimicrobial lead compound.
Original language | English |
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Title of host publication | Methods in Enzymology |
Subtitle of host publication | Metabolons and Supramolecular Enzyme Assemblies |
Publisher | Elsevier Inc. |
Chapter | 4 |
Pages | 63-82 |
Number of pages | 20 |
Volume | 617 |
ISBN (Electronic) | 978-0-12-817074-8 |
DOIs | |
Publication status | E-pub ahead of print - 4 Feb 2019 |
Publication series
Name | Methods in Enzymology |
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Publisher | Academic Press |
ISSN (Print) | 0076-6879 |
Research Groups and Themes
- BrisSynBio
- Bristol BioDesign Institute
- BCS and TECS CDTs
Keywords
- Polyketide synthase
- protein expression
- enzymology
- protein structure
- natural products
- Synthetic biology
Fingerprint
Dive into the research topics of 'Cloning, Expression and Purification of Intact Polyketide Synthase Modules'. Together they form a unique fingerprint.Projects
- 1 Finished
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BrisSynBio: Bristol Centre for Synthetic Biology
Woolfson, D. N. (Principal Investigator)
31/07/14 → 31/03/22
Project: Research
Student theses
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Structural and Functional Interrogation of the Abyssomicin C Biosynthetic Pathway
Maschio, L. (Author), Race, P. (Supervisor) & Willis, C. (Supervisor), 29 Sept 2020Student thesis: Doctoral Thesis › Doctor of Philosophy (PhD)
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