期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 61, 期 29, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202203909
关键词
alpha-Farnesene; Multienzyme Catalysis; Multienzyme Compartmentalization; Phase Separation; Terpene Biosynthesis
资金
- National Key R&D Program of China [2018YFA0903204]
- University Grants Committee of Hong Kong [14304921]
This study demonstrates the construction of synthetic multienzyme condensates through LLPS, which significantly enhances the biosynthesis of α-farnesene.
Liquid-liquid phase separation (LLPS) forms biomolecular condensates or coacervates in cells. Metabolic enzymes can form phase-separated subcellular compartments that enrich enzymes, cofactors, and substrates. Herein, we report the construction of synthetic multienzyme condensates that catalyze the biosynthesis of a terpene, alpha-farnesene, in the prokaryote E. coli. RGGRGG derived from LAF-1 was used as the scaffold protein to form the condensates by LLPS. Multienzyme condensates were then formed by assembling two enzymes Idi and IspA through an RIAD/RIDD interaction. Multienzyme condensates constructed inside E. coli cells compartmentalized the cytosolic space into regions of high and low enzyme density and led to a significant enhancement of alpha-farnesene production. This work demonstrates LLPS-driven compartmentalization of the cytosolic space of prokaryotic cells, condensation of a biosynthetic pathway, and enhancement of the biosynthesis of alpha-farnesene.
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