Biochemical Characterization of a Multifunctional Mononuclear Nonheme Iron Enzyme (PtID) in Neopentalenoketolactone Biosynthesis
Biochemical Characterization of a Multifunctional Mononuclear Nonheme Iron Enzyme (PtID) in Neopentalenoketolactone Biosynthesis
复制标题
新戊烯酮内酯生物合成中多功能单核非血红素铁酶 (PtID) 的生化表征
DOI：
10.1021/acs.orglett.9b02872
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发表时间：
2019-09-20
期刊：
影响因子：
5.2
通讯作者：
Zhao, Changming
中科院分区：
文献类型：
--
作者：
Deng, Qian;Liu, Yang;Zhao, Changming
戊烯内酯是一种具有抗菌活性的微生物倍半萜类化合物。它的生物合成途径阐明了所有相关基因的遗传和生化特征的组合。针对阿维链霉菌新戊烯酮内酯生物合成相关基因簇，提出了一种α-酮戊二酸依赖性单核非血红素铁酶PtID催化去饱和和烯烃环氧化反应。然而，这些活动仍有待验证的体外生化证据。在这份报告中，我们证明了PtID具有多种活性，包括羟基化，去饱和和环氧化，并证实了在新戊烯酮内酯途径中存在难以捉摸的环氧化物中间体。
Pentalenolactone is a microbial sesquiterpenoid with antibiotic activity. Its biosynthetic pathway was elucidated by a combination of genetic and biochemical characterizations of all genes involved. For the related neopentalenoketolactone biosynthetic gene cluster from Streptomyces avermitilis, an alpha-ketoglutarate-dependent mononuclear nonheme iron enzyme, PtID, was proposed to catalyze both desaturation and olefin epoxidation reactions. Yet, these activities remained to be validated by in vitro biochemical evidence. In this report, we demonstrated that PtID has multiple activities, including hydroxylation, desaturation, and epoxidation, and confirmed the presence of the elusive epoxide intermediate in a neopentalenoketolactone pathway.