The coupled reaction catalyzed by EchB and EchC lead to the formation of the common 2',3',5'-trihydroxy-benzene core in echosides biosynthesis.

Abstract

p-Terphenyls represent a unique family of aromatic natural products generated by nonribosomal peptide synthetase-like (NRPS-like) enzyme. After formation of p-terphenyl skeleton, tailoring modifications will give rise to structural diversity and various biological activities. Here we demonstrated a two-enzyme (EchB, a short-chain dehydrogenase/reductase (SDR), and EchC, a nuclear transport factor 2 (NTF2)-like dehydratase) participated transformation from dihydroxybenzoquinone core to 2',3',5'-trihydroxy-benzene in the biosynthesis of echosides. Beginning with polyporic acid as substrate, successive steps of reduction-dehydration-reduction cascade catalyzed by EchB-EchC-EchB were concluded after in vivo gene disruption and in vitro bioassay experiments. These findings demonstrated a conserved synthesis pathway of 2',3',5'-trihydroxy-p-terphenyls in bacteria, such as Actinomycetes and Burkholderia. The parallel pathway in fungi has yet to be explored.

• Authors: Jing Zhu, Mengyujie Liu, Jingjing Deng, Wang Chen, Deyu Zhu, Jing Duan, Yaoyao Li, Haoxin Wang, Yuemao Shen
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 559 Pg. 62-69 (06 25 2021) ISSN: 1090-2104 [Electronic] United States
• PMID: 33932901 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2021 Elsevier Inc. All rights reserved.

Chemical References

• Bacterial Proteins
• Benzene Derivatives
• Biological Products
• Terphenyl Compounds
• Oxidoreductases
• Hydro-Lyases

Topics

• Bacterial Proteins (metabolism)
• Benzene Derivatives (metabolism)
• Biological Products (metabolism)
• Biosynthetic Pathways
• Hydro-Lyases (metabolism)
• Oxidoreductases (metabolism)
• Streptomyces (enzymology, metabolism)
• Terphenyl Compounds (metabolism)