Reprogramming product selectivity and activity in promiscuous terpene synthases via substrate conformation engineering
Sheng Dong, Hongshuang Liu, Weihong Liao, Xuedong Chen, Tianyu Cui, Ruimin Zhang, Qian Wang, Ying Han, Lei Wang, Xiao Men, Haibo Zhang · 2026
Read Reprogramming product selectivity and activity in promiscuous terpene synthases via substrate conformation engineering by Sheng Dong, Hongshuang Liu, Weihong Liao, Xuedong Chen, Tianyu Cui, Ruimin Zhang, Qian Wang, Ying Han, Lei Wang, Xiao Men, Haibo Zhang (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13627652.txt.
Description
Terpene synthases make nature's vast terpene family, but they are often sloppy and slow, picking several products at modest rates. Sheng Dong and ten co-authors dissect a fungal enzyme that builds germacrene A and find the steering wheel: the size of one residue beside the substrate pocket. Its bulk sets how the starting molecule folds, which redirects the carbocation cascade that decides the product.
Guided reshaping of the pocket produced variants with altered product choices. One variant raised production of the target terpene 24-fold in engineered Escherichia coli, reaching 15.8 grams per liter in a bioreactor, a record for that host. The authors offer substrate-shape engineering as a general strategy for tidier biocatalysts. The study appears in 2026.
Catalog record
| CREATOR | Sheng Dong, Hongshuang Liu, Weihong Liao, Xuedong Chen, Tianyu Cui, Ruimin Zhang, Qian Wang, Ying Han, Lei Wang, Xiao Men, Haibo Zhang |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 48 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |