Structural highlights
Function
A0A977K7H6_9PEZI
Publication Abstract from PubMed
The creation of enzymes with abiological abilities offers exciting opportunities to access new-to-nature biocatalysis beyond that found in nature. Here, we repurpose a novel protein scaffold, CTB10, as an artificial photoenzyme through genetic code expansion. It enables catalytic deracemization of cyclopropane, a process that remains inaccessible to traditional biocatalysis due to its thermodynamically unfavorable nature. Following structural optimization through directed evolution, a broad substrate scope with high enantioselectivities is achieved. Furthermore, the crystal structure of the CTB10-based photoenzyme-substrate complex well demonstrates how the catalytic chiral cavity is sculpted to promote efficient and selective light-enabled deracemization. Therefore, this study unlocks the potential for achieving challenging deracemization through biocatalysis.
Light-Driven Deracemization by a Designed Photoenzyme.,Li M, Zhang Y, Fu K, Deng Z, Yuan Z, Luo Z, Rao Y J Am Chem Soc. 2025 Apr 23;147(16):13190-13199. doi: 10.1021/jacs.4c16521. Epub , 2025 Apr 12. PMID:40219972[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li M, Zhang Y, Fu K, Deng Z, Yuan Z, Luo Z, Rao Y. Light-Driven Deracemization by a Designed Photoenzyme. J Am Chem Soc. 2025 Apr 23;147(16):13190-13199. PMID:40219972 doi:10.1021/jacs.4c16521