8XYN

Structure of the engineered retro-aldolase RA95.5-8

This is a non-PDB format compatible entry.

Summary for 8XYN

• Entry DOI: 10.2210/pdb8xyn/pdb
• Descriptor: retro-aldolase RA95.5-8, 4-[dodecyl(dimethyl)-$l^{4}-azanyl]butanoic acid (3 entities in total)
• Functional Keywords: retro-aldolase, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 60221.82

Authors

Kunthic, T.,Yu, M.Z.,Xiang, Z. (deposition date: 2024-01-20, release date: 2024-07-24)

Primary citation

Yu, M.Z.,Yuan, Y.,Li, Z.J.,Kunthic, T.,Wang, H.X.,Xu, C.,Xiang, Z.
An Artificial Enzyme for Asymmetric Nitrocyclopropanation of alpha , beta-Unsaturated Aldehydes-Design and Evolution.
Angew.Chem.Int.Ed.Engl., 63:e202401635-e202401635, 2024

PubMed Abstract: The introduction of an abiological catalytic group into the binding pocket of a protein host allows for the expansion of enzyme chemistries. Here, we report the generation of an artificial enzyme by genetic encoding of a non-canonical amino acid that contains a secondary amine side chain. The non-canonical amino acid and the binding pocket function synergistically to catalyze the asymmetric nitrocyclopropanation of α,β-unsaturated aldehydes by the iminium activation mechanism. The designer enzyme was evolved to an optimal variant that catalyzes the reaction at high conversions with high diastereo- and enantioselectivity. This work demonstrates the application of genetic code expansion in enzyme design and expands the scope of enzyme-catalyzed abiological reactions.

PubMed: 38597773
DOI: 10.1002/anie.202401635

Experimental method

X-RAY DIFFRACTION (2.3 Å)