ArticleBiotechnology letters2024
Essential amino acid residues and catalytic mechanism of trans-epoxysuccinate hydrolase for production of meso-tartaric acid.
Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Improving the thermal stability ofJournal of Zhejiang University. Science. B · 2025Article
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5 authors.
Funding
Abstract
objectivesThis study aimed to discuss the essential amino acid residues and catalytic mechanism of trans-epoxysuccinate hydrolase from Pseudomonas koreensis for the production of meso-tartaric acid.
resultsThe optimum conditions of the enzyme were 45 °C and pH 9.0, respectively. It was strongly inhibited by Zn
conclusionsThe structure and catalytic mechanism of trans-epoxysuccinate hydrolase were first reported. Ten residues were critical for its catalysis and a two-step mechanism by an Asp-His-Asp catalytic triad was proposed.
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