A clickable coenzyme A derived probe for investigating phosphopantetheinyl transferase activity in natural product biosynthesis.
| Autor: | Yin Z; Kekulé-Institute for Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany. dickschat@uni-bonn.de., Xu H; Kekulé-Institute for Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany. dickschat@uni-bonn.de., Dickschat JS; Kekulé-Institute for Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany. dickschat@uni-bonn.de. |
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| Jazyk: | angličtina |
| Zdroj: | Organic & biomolecular chemistry [Org Biomol Chem] 2024 Nov 13; Vol. 22 (44), pp. 8714-8719. Date of Electronic Publication: 2024 Nov 13. |
| DOI: | 10.1039/d4ob01485e |
| Abstrakt: | Phosphopantetheinyl transferases activate carrier proteins through attachment of a coenzyme A derived phosphopantetheinyl linker. This study describes a method to monitor this process through a modified HSCoA with an alkyne group, allowing for the Cu-catalysed alkyne-azide cycloaddition of a fluorescent tag. Application of the method in an enzyme screening resulted in the identification of new promiscuous PPTases. |
| Databáze: | MEDLINE |
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