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Enzymatic Synthesis of a Diastereomer of Neoabyssomicin Derivative Using the Diels‐Alderase AbyU
Author(s) -
Ding Wenjuan,
Chi Changbiao,
Wei Xiaoyi,
Sun Changli,
Tu Jiajia,
Ma Ming,
Li Qinglian,
Ju Jianhua
Publication year - 2021
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.202100081
Subject(s) - chemistry , diastereomer , derivative (finance) , enzyme , stereochemistry , mutagenesis , substrate (aquarium) , combinatorial chemistry , biosynthesis , biochemistry , mutation , gene , oceanography , financial economics , economics , geology
Main observation and conclusion The enzyme AbyU catalyses a Diels‐Alder (DA) reaction during abyssomicin C biosynthesis. In this study, AbyU is shown to convert the native substrate of another Diels‐Alderase (DAase), AbmU, to a new abyssomicin derivative, abyssomicin 7. Abyssomicin 7 is a diastereomer of the AbmU‐derived, abyssomicin 6. Using structural analyses and site‐directed mutagenesis, we unveil the molecular basis for production of abyssomicin 7, instead of abyssomicin 6, within the AbyU active site.