Enzymatic Synthesis of a Diastereomer of Neoabyssomicin Derivative Using the Diels‐Alderase AbyU. Issue 7 (27th May 2021)

• Record Type: Journal Article
• Authors: Ding, Wenjuan; Chi, Changbiao; Wei, Xiaoyi; Sun, Changli; Tu, Jiajia; Ma, Ming; Li, Qinglian; Ju, Jianhua
• Is Part Of: Chinese journal of chemistry. Volume 39:Issue 7(2021)
• Page Start: 1871
• Page End: 1877
• Publication Date: 2021-05-27
• Subjects: Biosynthesis -- Bioorganic chemistry -- Enzyme catalysis -- Neoabyssomicin -- Diels‐Alderase; Chemistry -- Periodicals; 540.5
• DOI: 10.1002/cjoc.202100081
• Languages: English
• ISSNs: 1001-604X

Abstract

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. Abstract : AbyU is shown to convert the native substrate 4 of another Diels‐Alderase (DAase), AbmU, to a new abyssomicin derivative, abyssomicin 7. Abyssomicin 7 is a diastereomer of the AbmU‐derived, abyssomicin 6.