ArticleApplied and environmental microbiology2018
A Haloalkane Dehalogenase from a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity.
Article in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- HaloTag-Based FACS-Compatible Assay for Intracellular Haloalkane Detection with a Potential Application to Halogenase Screening.Analytical chemistry · 2026Article
- Untapped enzymatic potential: dehalogenase- and peroxidase-driven PVC degradation by gene carriers in Tibetan plateau pikas.Microbiome · 2026Article
- A Haloalkane Dehalogenase DhaA Nanoparticle Based on Pullulan Conjugation and Polyethyleneimine Adsorption.Applied biochemistry and biotechnology · 2025Article
- Azobenzene-Based Photoswitchable Substrates for Advanced Mechanistic Studies of Model Haloalkane Dehalogenase Enzyme Family.ACS catalysis · 2024Article
- Article
- Structural Analysis of the Ancestral Haloalkane Dehalogenase AncLinB-DmbA.International journal of molecular sciences · 2021Article
- A Haloalkane Dehalogenase from Saccharomonospora viridis Strain DSM 43017, a Compost Bacterium with Unusual Catalytic Residues, Unique (Applied and environmental microbiology · 2020Article
- An Ultrasensitive Fluorescence Assay for the Detection of Halides and Enzymatic Dehalogenation.ChemCatChem · 2020Article
- Fluorescent substrates for haloalkane dehalogenases: Novel probes for mechanistic studies and protein labeling.Computational and structural biotechnology journal · 2020Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to those of previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to having this unique substrate specificity, the enzyme was highly tolerant to organic cosolvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high overexpression yield (200 mg of protein per liter of cultivation medium; 50% of total protein), good tolerance to organic cosolvents, and a broad pH range make DmmA an attractive biocatalyst for various biotechnological applications.
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