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Mechanistic Studies on Trichoacorenol Synthase from Amycolatopsis benzoatilytica.


ABSTRACT: Isotopic labeling experiments performed with a newly identified bacterial trichoacorenol synthase established a 1,5-hydride shift occurring in the cyclization mechanism. During EI-MS analysis, major fragments of the sesquiterpenoid were shown to arise via cryptic hydrogen movements. Therefore, the interpretation of earlier results regarding the cyclization mechanism obtained by feeding experiments in Trichoderma is revised.

SUBMITTER: Rinkel J 

PROVIDER: S-EPMC7155024 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Mechanistic Studies on Trichoacorenol Synthase from Amycolatopsis benzoatilytica.

Rinkel Jan J   Dickschat Jeroen S JS  

Chembiochem : a European journal of chemical biology 20191107 6


Isotopic labeling experiments performed with a newly identified bacterial trichoacorenol synthase established a 1,5-hydride shift occurring in the cyclization mechanism. During EI-MS analysis, major fragments of the sesquiterpenoid were shown to arise via cryptic hydrogen movements. Therefore, the interpretation of earlier results regarding the cyclization mechanism obtained by feeding experiments in Trichoderma is revised. ...[more]

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