ArticleApplied and environmental microbiology2014
Expanding the Halohydrin Dehalogenase Enzyme Family: Identification of Novel Enzymes by Database Mining.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 66 citations in OpenAlex.
- Biocatalytic kinetic resolution for efficient and enantioselective synthesis of δ-haloalcohols and tetrahydrofurans.Communications chemistry · 2025Article
- Engineering of Conserved Sequence Motif 1 Residues in Halohydrin Dehalogenase HheC Simultaneously Enhances Activity, Stability, and Enantioselectivity.ACS catalysis · 2025Article
- Synthesis and Investigation of Antibacterial Properties of Thymol, Carvacrol, Eugenol, and Perillyl Alcohol Based β-Halo Alcohol and β-Halo Thiol Compounds.Journal of biochemical and molecular toxicology · 2025Article
- Biocatalytic enantioselective formation and ring-opening of oxetanes.Nature communications · 2025Article
- A Dynamic Loop in Halohydrin Dehalogenase HheG Regulates Activity and Enantioselectivity in Epoxide Ring Opening.ACS catalysis · 2024Article
- A Novel Lipase fromInternational journal of molecular sciences · 2023Article
- Community-integrated multi-omics facilitates screening and isolation of the organohalide dehalogenation microorganism.Innovation (Cambridge (Mass.)) · 2023Article
- G-type Halohydrin Dehalogenases Catalyze Ring Opening Reactions of Cyclic Epoxides with Diverse Anionic Nucleophiles.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Database Mining for Novel Bacterial β-Etherases, Glutathione-Dependent Lignin-Degrading Enzymes.Applied and environmental microbiology · 2020Article
- The biotechnological potential of marine bacteria in the novel lineage of Pseudomonas pertucinogena.Microbial biotechnology · 2020Review
- Position 123 of halohydrin dehalogenase HheG plays an important role in stability, activity, and enantioselectivity.Scientific reports · 2019Article
- Exploiting distant homologues for phasing through the generation of compact fragments, local fold refinement and partial solution combination.Acta crystallographica. Section D, Structural biology · 2018Article
- Enhancing the biocatalytic manufacture of the key intermediate of atorvastatin by focused directed evolution of halohydrin dehalogenase.Scientific reports · 2017Article
- Recent advances on halohydrin dehalogenases-from enzyme identification to novel biocatalytic applications.Applied microbiology and biotechnology · 2016Review
- Estimating the success of enzyme bioprospecting through metagenomics: current status and future trends.Microbial biotechnology · 2016Review
- DomSign: a top-down annotation pipeline to enlarge enzyme space in the protein universe.BMC bioinformatics · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halohydrin dehalogenases are very rare enzymes that are naturally involved in the mineralization of halogenated xenobiotics. Due to their catalytic potential and promiscuity, many biocatalytic reactions have been described that have led to several interesting and industrially important applications. Nevertheless, only a few of these enzymes have been made available through recombinant techniques; hence, it is of general interest to expand the repertoire of these enzymes so as to enable novel biocatalytic applications. After the identification of specific sequence motifs, 37 novel enzyme sequences were readily identified in public sequence databases. All enzymes that could be heterologously expressed also catalyzed typical halohydrin dehalogenase reactions. Phylogenetic inference for enzymes of the halohydrin dehalogenase enzyme family confirmed that all enzymes form a distinct monophyletic clade within the short-chain dehydrogenase/reductase superfamily. In addition, the majority of novel enzymes are substantially different from previously known phylogenetic subtypes. Consequently, four additional phylogenetic subtypes were defined, greatly expanding the halohydrin dehalogenase enzyme family. We show that the enormous wealth of environmental and genome sequences present in public databases can be tapped for in silico identification of very rare but biotechnologically important biocatalysts. Our findings help to readily identify halohydrin dehalogenases in ever-growing sequence databases and, as a consequence, make even more members of this interesting enzyme family available to the scientific and industrial community.
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