Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.,Natural Product Reports

当前位置： X-MOL 学术 › Nat. Prod. Rep. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.
Natural Product Reports ( IF 10.2 ) Pub Date : 2020-03-25 , DOI: 10.1039/c9np00051h
Jeffrey D. Rudolf _{1,

2,

3,

4} , Chin-Yuan Chang _{5,

6,

7,

8}

Affiliation

Covering: up to July 2019 Terpene synthases (TSs) are responsible for generating much of the structural diversity found in the superfamily of terpenoid natural products. These elegant enzymes mediate complex carbocation-based cyclization and rearrangement cascades with a variety of electron-rich linear and cyclic substrates. For decades, two main classes of TSs, divided by how they generate the reaction-triggering initial carbocation, have dominated the field of terpene enzymology. Recently, several novel and unconventional TSs that perform TS-like reactions but do not resemble canonical TSs in sequence or structure have been discovered. In this review, we identify 12 families of non-canonical TSs and examine their sequences, structures, functions, and proposed mechanisms. Nature provides a wide diversity of enzymes, including prenyltransferases, methyltransferases, P450s, and NAD+-dependent dehydrogenases, as well as completely new enzymes, that utilize distinctive reaction mechanisms for TS chemistry. These unique non-canonical TSs provide immense opportunities to understand how nature evolved different tools for terpene biosynthesis by structural and mechanistic characterization while affording new probes for the discovery of novel terpenoid natural products and gene clusters via genome mining. With every new discovery, the dualistic paradigm of TSs is contradicted and the field of terpene chemistry and enzymology continues to expand.

中文翻译：

伪装的萜烯合酶：非经典萜烯合酶的酶学、结构和机会。

覆盖范围：截至 2019 年 7 月萜烯合酶 (TS) 负责产生萜类天然产物超家族中的大部分结构多样性。这些优雅的酶通过各种富电子线性和环状底物介导复杂的基于碳阳离子的环化和重排级联。几十年来，两类主要的 TS（根据它们如何产生引发反应的初始碳正离子划分）一直主导着萜烯酶学领域。最近，已经发现了几种新颖且非常规的 TS，它们执行类似 TS 的反应，但在序列或结构上与规范的 TS 不同。在这篇综述中，我们确定了 12 个非规范 TS 家族，并检查了它们的序列、结构、功能和提出的机制。大自然提供了各种各样的酶，包括异戊烯基转移酶、甲基转移酶、P450 和 NAD+ 依赖性脱氢酶，以及利用独特的 TS 化学反应机制的全新酶。这些独特的非规范TS提供了巨大的机会来了解大自然如何通过结构和机械表征进化出不同的萜烯生物合成工具，同时为通过基因组挖掘发现新型萜类天然产物和基因簇提供新的探针。随着每一个新发现的出现，TS 的二元范式都会受到矛盾，萜烯化学和酶学领域不断扩大。

更新日期：2020-03-26

点击分享查看原文

点击收藏

阅读更多本刊最新论文本刊介绍/投稿指南11