ArticleACS catalysis2025
Engineering of Conserved Sequence Motif 1 Residues in Halohydrin Dehalogenase HheC Simultaneously Enhances Activity, Stability, and Enantioselectivity.
Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Engineered halohydrin dehalogenase mediates remote enantiocontrolled dehalogenative hydroxylation via an unconventional mechanism.Nature communications · 2026Article
- A Dynamic Loop in Halohydrin Dehalogenase HheG Regulates Activity and Enantioselectivity in Epoxide Ring Opening.ACS catalysis · 2024Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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Abstract
Halohydrin dehalogenases (HHDHs) are powerful enzymes for the asymmetric diversification of oxyfunctionalized synthons. They feature two characteristic sequence motifs that distinguish them from homologous short-chain dehydrogenases and reductases. Sequence motif 1, carrying a conserved threonine, glycine, and a central aromatic residue, lines the nucleophile binding pocket of HHDHs. It could therefore impact nucleophile binding and presumably also the activity of the enzymes. However, experimental evidence supporting this theory is largely missing. Herein, we systematically studied the mutability of the three conserved motif 1 residues as well as their resulting impact on enzyme activity, stability, and selectivity in two model HHDHs: HheC from
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