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Mechanistic Studies on Trichoacorenol Synthase from Amycolatopsis benzoatilytica
Author(s) -
Rinkel Jan,
Dickschat Jeroen S.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900584
Subject(s) - atp synthase , mechanism (biology) , hydride , chemistry , stereochemistry , biochemistry , biology , enzyme , hydrogen , organic chemistry , physics , quantum mechanics
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.