Natural product biosynthesis by guanidine prenyltransferases in plants and bacteria

IF 47.3 1区综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES

Science Pub Date : 2026-10-22 DOI:10.1126/science.aeg1821

Dominik Kolling, Katharina Konzok, Daghan Taser, Tom Jentsch, Svenja Schwoerer, Henry Struwe, Arne Bültemeier, Jonas Freiberg, Claus-Peter Witte, Jakob Franke, Andriy Luzhetskyy, Andreas Kirschning, Sophia Rudorf, Jesko Koehnke

引用次数: 0

Abstract

Guanidine exists almost exclusively as a resonance-stabilized cation, making its direct enzymatic functionalization challenging. We identified the cyanobacterial enzyme NosH, which catalyzes direct prenyl transfer to free guanidine. Structural and mechanistic analyses revealed guanidine activation by a two-aspartate clamp coupled to prenyl-donor binding through a distinct catalytic architecture. Guided by these features, we identified a large family of guanidine prenyltransferases across bacteria and plants. Plant enzymes produced guanidine alkaloids such as galegine in vitro and heterologous expression of a plant ortholog in Nicotiana benthamiana produced galegine in planta, providing a direct enzymatic link to plant-specialized metabolism.

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植物和细菌中胍基戊烯基转移酶的天然产物生物合成

胍几乎完全作为一种共振稳定阳离子存在，这使得它的直接酶功能化具有挑战性。我们鉴定了蓝藻酶NosH，它催化戊烯基直接转移到游离胍。结构和机理分析表明，胍的活化是通过一种独特的催化结构，通过双天冬氨酸夹耦合到戊烯基供体结合。在这些特征的指导下，我们确定了一个跨细菌和植物的胍戊烯基转移酶大家族。植物酶在离体条件下产生鸟嘌呤类生物碱，而植物同源物在benthamiana中的异源表达产生galegine，为植物特化代谢提供了直接的酶联系。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Science 综合性期刊-综合性期刊

CiteScore

61.10

自引率

0.90%

发文量

审稿时长

2.1 months

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