Enzymatic Access to Norstatines by PLP-Dependent Decarboxylative C–C Bond Formation Involved in Leuhistin Biosynthesis

Journal of the American Chemical Society 2026

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Authors: Taku Mizutani, Takayoshi Awakawa, Naruhiko Adachi, Yusuke Yamada, Takahiro Mori, Ikuro Abe
DOI: 10.1021/jacs.6c05214
Cited by: 1
References: 33

Abstract

deprotonation. This suggests the catalytic mechanism is distinct among the canonical PLP-dependent decarboxylative C-C bond forming enzymes. Genome mining of LhnE homologues also implicated the existence of previously unknown norstatine natural products. Furthermore, LhnE was successfully applied to the biocatalytic synthesis of non-natural norstatines. Together, this study provides novel insights into PLP-dependent C-C bond formation and establishes a biocatalytic route for streamlined access to norstatine pharmacophores.

Fields of Study & Subjects

Microbial Natural Products and Biosynthesis Microbial Metabolism and Applications Sirtuins and Resveratrol in Medicine

Publication details

Journal / source
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Volume
148
Issue
18
Pages
18633–18637
Publication date
1 May 2026
Language
EN