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Substrate-Multiplexed Assessment of Aromatic Prenyltransferase Activity
Peyton M Higgins1, Nicolette G Wehrli1, Andrew R Buller1
1Department of Chemistry, University of Wisconsin-Madison, 1101 University Ave, Madison, Wisconsin, USA.
Chembiochem : a European Journal of Chemical Biology
|September 24, 2024
Summary
Nature
Area of Science:
- Enzymology
- Synthetic Biology
- Natural Product Biosynthesis
Background:
- Enzymes are crucial for natural product biosynthesis.
- Aromatic prenyltransferases (PTs) are key enzymes catalyzing C-C bond formation.
- PTs are valuable tools for synthetic chemistry and biology.
Purpose of the Study:
- To construct and assay a diverse panel of aromatic prenyltransferases (PTs).
- To identify novel PTs with high catalytic efficiency and specificity.
- To benchmark PTs for future synthetic applications.
Main Methods:
- Phylogenetic analysis of PTs.
- Enzyme activity assays.
- Substrate-multiplexed screening for enzyme specificity.
Main Results:
- A phylogenetically diverse panel of PTs was constructed and assayed.
- Substrate-multiplexed screening provided direct information on enzyme specificity.
- Divergent PT homologs with performance rivaling model enzymes were identified.
- The first bacterial O-Tyr PT was discovered.
Conclusions:
- Nature's enzymatic diversity offers a powerful strategy for identifying useful enzymes.
- PTs are versatile biocatalysts with significant potential in synthetic chemistry and biology.
- This study provides valuable benchmarking data for PTs in synthetic applications.
