Deciphering the O -Carbamoylation Modification Mechanism in Venturicidin A Biosynthesis

Organic Letters 2026

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Authors: Q. L. CHEN, Chunya Xie, Jiaozhuang Liu, Zhi Xia Qiao, Zhenghao Peng, L.J. Liu, Xianying He, Chunyao Ling, Zhengrong Zou, Yan-Bin Teng, Yunchang Xie
DOI: 10.1021/acs.orglett.5c04918
Cited by: 1
References: 23

Abstract

Abstract Herein, VtdB was identified as an essential O-carbamoyltransferase that catalyzes the conversion of venturicidin B (3) to venturicidin A (1). Notably, a 2.8 Å resolution crystal structure of the VtdB-substrate complex (VtdB/VTD-B) revealed that 3 occupies a specific hydrophobic pocket within the Kael-like domain, where His35 plays a critical deprotonation role during enzymatic catalysis. These biochemical and structural research provides the first mechanistic insight into d-olivose-glycosylated macrolide recognition by the carbamoyltransferase, enabling its future engineering.

Fields of Study & Subjects

Microbial Natural Products and Biosynthesis Carbohydrate Chemistry and Synthesis Enzyme Structure and Function

Publication details

Journal / source
Organic Letters
Publisher
American Chemical Society (ACS)
Volume
28
Issue
19
Pages
5889–5894
Publication date
13 January 2026
Language
EN