Substrate‐Multiplexed Assessment of Aromatic Prenyltransferase Activity
Abstract: An increasingly effective strategy to identify synthetically useful enzymes is to sample the diversity already present in Nature. Here, we construct and assay a panel of phylogenetically diverse aromatic prenyltransferases (PTs). These enzymes catalyze a variety of C−C bond forming reactions in natural product biosynthesis and are emerging as tools for synthetic chemistry and biology. Homolog screening was further empowered through substrate‐multiplexed screening, which provides direct information on enzyme specificity. We perform a head‐to‐head assessment of the model members of the PT family and further identify homologs with divergent sequences that rival these superb enzymes. This effort revealed the first bacterial O−Tyr PT and, together, provide valuable benchmarking for future synthetic applications of PTs.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Substrate‐Multiplexed Assessment of Aromatic Prenyltransferase Activity ; day:11 ; month:11 ; year:2024 ; extent:7
ChemBioChem ; (11.11.2024) (gesamt 7)
- Creator
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Higgins, Peyton M.
Wehrli, Nicolette G.
Buller, Andrew R.
- DOI
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10.1002/cbic.202400680
- URN
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urn:nbn:de:101:1-2411121329380.160375180175
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:20 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Higgins, Peyton M.
- Wehrli, Nicolette G.
- Buller, Andrew R.
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