ArticleApplied and environmental microbiology2005
Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 78 citations in OpenAlex.
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- Atypical homodimerization revealed by the structure of the (S)-enantioselective haloalkane dehalogenase DmmarA from Mycobacterium marinum.Acta crystallographica. Section D, Structural biology · 2023Article
- Deconstructed Plastic Substrate Preferences of Microbial Populations from the Natural Environment.Microbiology spectrum · 2023Article
- Expanding Characterized Diversity and the Pool of Complete Genome Sequences ofFrontiers in microbiology · 2021Article
- Fluorescent substrates for haloalkane dehalogenases: Novel probes for mechanistic studies and protein labeling.Computational and structural biotechnology journal · 2020Article
- A Haloalkane Dehalogenase from a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity.Applied and environmental microbiology · 2018Article
- Ylehd, an epoxide hydrolase with promiscuous haloalkane dehalogenase activity from tropical marine yeast Yarrowia lipolytica is induced upon xenobiotic stress.Scientific reports · 2017Article
- Gene Expression Analysis ofFrontiers in microbiology · 2017Article
- Discovery of Novel Haloalkane Dehalogenase Inhibitors.Applied and environmental microbiology · 2016Article
- Rhizobia and their bio-partners as novel drivers for functional remediation in contaminated soils.Frontiers in plant science · 2015Review
- Dynamics and hydration explain failed functional transformation in dehalogenase design.Nature chemical biology · 2014Article
- Biochemical characterization of a haloalkane dehalogenase DadB from Alcanivorax dieselolei B-5.PloS one · 2014Article
- Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium.Applied and environmental microbiology · 2012Article
- Crystallization and preliminary X-ray analysis of the haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Biochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58.Applied and environmental microbiology · 2011Article
- Sequence- and activity-based screening of microbial genomes for novel dehalogenases.Microbial biotechnology · 2010Article
- Biochemical characterization of haloalkane dehalogenases DrbA and DmbC, Representatives of a Novel Subfamily.Applied and environmental microbiology · 2009Article
- Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Biodegradation of bis(2-chloroethyl) ether by Xanthobacter sp. strain ENV481.Applied and environmental microbiology · 2007Article
- Crystallization and preliminary crystallographic analysis of a haloalkane dehalogenase, DbjA, from Bradyrhizobium japonicum USDA110.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
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9 authors at 2 institutions in 2 countries.
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Abstract
Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, have open reading frames (ORFs), mlr5434 and blr1087, respectively, that encode putative haloalkane dehalogenase homologues. The crude extracts of Escherichia coli strains expressing mlr5434 and blr1087 showed the ability to dehalogenate 18 halogenated compounds, indicating that these ORFs indeed encode haloalkane dehalogenases. Therefore, these ORFs were referred to as dmlA (dehalogenase from Mesorhizobium loti) and dbjA (dehalogenase from Bradyrhizobium japonicum), respectively. The principal component analysis of the substrate specificities of various haloalkane dehalogenases clearly showed that DbjA and DmlA constitute a novel substrate specificity class with extraordinarily high activity towards beta-methylated compounds. Comparison of the circular dichroism spectra of DbjA and other dehalogenases strongly suggested that DbjA contains more alpha-helices than the other dehalogenases. The dehalogenase activity of resting cells and Northern blot analyses both revealed that the dmlA and dbjA genes were expressed under normal culture conditions in MAFF303099 and USDA110 strain cells, respectively.
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