8WBQ

Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L] mutant E212Q complexed with L-TA.

Summary for 8WBQ

• Entry DOI: 10.2210/pdb8wbq/pdb
• Descriptor: Epoxide hydrolase, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: cis-epoxysuccinate hydrolases, epoxide hydrolase, l(+)-tartaric acid, hydrolase
• Biological source: Rhodococcus opacus
• Total number of polymer chains: 2
• Total formula weight: 59002.02

Authors

Dong, S.,Xuan, J.S.,Feng, Y.G.,Cui, Q. (deposition date: 2023-09-10, release date: 2024-01-31, Last modification date: 2024-02-21)

Primary citation

Dong, S.,Xuan, J.,Feng, Y.,Cui, Q.
Deciphering the stereo-specific catalytic mechanisms of cis-epoxysuccinate hydrolases producing L(+)-tartaric acid.
J.Biol.Chem., 300:105635-105635, 2024

PubMed Abstract: Microbial epoxide hydrolases, cis-epoxysuccinate hydrolases (CESHs), have been utilized for commercial production of enantiomerically pure L(+)- and D(-)-tartaric acids for decades. However, the stereo-catalytic mechanism of CESH producing L(+)-tartaric acid (CESH[L]) remains unclear. Herein, the crystal structures of two CESH[L]s in ligand-free, product-complexed, and catalytic intermediate forms were determined. These structures revealed the unique specific binding mode for the mirror-symmetric substrate, an active catalytic triad consisting of Asp-His-Glu, and an arginine providing a proton to the oxirane oxygen to facilitate the epoxide ring-opening reaction, which has been pursued for decades. These results provide the structural basis for the rational engineering of these industrial biocatalysts.

PubMed: 38199576
DOI: 10.1016/j.jbc.2024.105635

Experimental method

X-RAY DIFFRACTION (2.2 Å)