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bioRxiv · 10.1101/2025.05.02.651859

Structure-activity relationship of an all-α-helical prenyltransferase reveals a mechanism for indole prenylation.

Oshiro, T.·Uehara, S.·Tanaka, Y.·Ito, T.·Kodera, Y.·Matsui, T.
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Abstract

Enzymes are involved in the biosynthesis of various secondary metabolites found in nature. The catalytic mechanism is regulated by the three-dimensional structure of the enzyme especially at the catalytic site, resulting in the natural products with complicated conformation derived from a regioselective, chemoselective, and stereoselective fashion of the enzyme reaction. Prenyltransferase (PT), which belongs to the prenylsynthase (PS) family, catalyzes the condensation of isoprene to an aromatic compound, consequently producing a terpenoid scaffold structure. Therefore, it plays an important role in which expands the chemical diversity of terpenoids. Although the three-dimensional structures of PS which categorized in the same family were resolved, the catalytic mechanism of the PT has been vailed. In this study, we determined the X-ray crystal structure of a novel prenyltransferase SxPT1 derived from marine Streptomyces. Here we described that SxPT1 analyzed the enzyme reactions and discussed its catalytic mechanism.

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Oshiro, T., Uehara, S., Tanaka, Y., Ito, T., Kodera, Y., Matsui, T.. 2025-05-03. Structure-activity relationship of an all-α-helical prenyltransferase reveals a mechanism for indole prenylation.. https://doi.org/10.1101/2025.05.02.651859

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