Guanidine prenyltransferases drive natural product biosynthesis in plants and bacteria
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A study published in Science on October 22, 2026 (Volume 394, Issue 6822, pages 413-418; DOI 10.1126/science.aeg1821) examines how guanidine prenyltransferases mediate natural product biosynthesis in plants and bacteria. Prenyltransferases attach prenyl groups to acceptor molecules, a modification that expands structural diversity in natural products, and the guanidine-dependent variants characterized here add a mechanistic branch to this enzyme family. The work spans both plant and bacterial systems, pointing to a biosynthetic strategy distributed across kingdoms. The published paper establishes the enzymatic activity and its natural product context; follow-up questions, such as the full range of substrates, the enzymes' distribution in other organisms, and potential applications in biocatalysis or drug discovery, remain open for the field.
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- science.orgNatural product biosynthesis by guanidine prenyltransferases in plants and bacteria
The study examines natural product biosynthesis mediated by guanidine prenyltransferases in plants and bacteria. The article was published in Science, volume 394, issue 6822, pages 413-418, October 2026, DOI 10.1126/science.aeg1821.
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