8wbk

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Current revision (11:01, 21 February 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q1KLR5_RHOOP Q1KLR5_RHOOP]
[https://www.uniprot.org/uniprot/Q1KLR5_RHOOP Q1KLR5_RHOOP]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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Deciphering the stereo-specific catalytic mechanisms of cis-epoxysuccinate hydrolases producing L(+)-tartaric acid.,Dong S, Xuan J, Feng Y, Cui Q J Biol Chem. 2024 Jan 8:105635. doi: 10.1016/j.jbc.2024.105635. PMID:38199576<ref>PMID:38199576</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 8wbk" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
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</StructureSection>
</StructureSection>

Current revision

Crystal structure of cis-Epoxysuccinate Hydrolases RhCESH[L]

PDB ID 8wbk

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