Deciphering the stereo-specific catalytic mechanisms of cis-epoxysuccinate hydrolases producing L(+)-tartaric acid.
J Biol Chem
; 300(2): 105635, 2024 Feb.
Article
em En
| MEDLINE
| ID: mdl-38199576
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Epóxido Hidrolases
/
Biocatálise
/
Hidrolases
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article