ArticleApplied and environmental microbiology2015
Novel LinA type 3 δ-hexachlorocyclohexane dehydrochlorinase.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Microbially-mediated halogenation and dehalogenation cycling of organohalides in the ocean.Nature communications · 2025Article
- Revelation of bioremediation approaches for hexachlorocyclohexane degradation in soil.World journal of microbiology & biotechnology · 2023Review
- Theoretical insight on the treatment of β-hexachlorocyclohexane waste through alkaline dehydrochlorination.Scientific reports · 2021Article
- Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Article
- Genome Organization of Sphingobium indicum B90A: An Archetypal Hexachlorocyclohexane (HCH) Degrading Genotype.Genome biology and evolution · 2017Article
- Revealing large metagenomic regions through long DNA fragment hybridization capture.Microbiome · 2017Article
- Comparison of the complete genome sequences of four γ-hexachlorocyclohexane-degrading bacterial strains: insights into the evolution of bacteria able to degrade a recalcitrant man-made pesticide.DNA research : an international journal for rapid publication of reports on genes and genomes · 2016Article
- Degradation study of lindane by novel strainsBioresources and bioprocessing · 2016Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LinA is the first enzyme of the microbial degradation pathway of a chlorinated insecticide, hexachlorocyclohexane (HCH), and mediates the dehydrochlorination of α-, γ-, and δ-HCH. Its two variants, LinA type 1 and LinA type 2, which differ at 10 out of 156 amino acid residues, have been described. Their activities for the metabolism of different HCH isomers differ considerably but overall are high for γ-HCH, moderate for α-HCH, low for δ-HCH, and lacking for β-HCH. Here, we describe the characterization of a new variant of this enzyme, LinA type 3, whose gene was identified from the metagenome of an HCH-contaminated soil sample. Its deduced primary structure in the region spanning amino acid residues 1 to 147 of the protein exhibits 17 and 12 differences from LinA type 1 and LinA type 2, respectively. In addition, the residues GIHFAPS, present at the region spanning residues 148 to 154 in both LinA type 1 and LinA type 2, are deleted in LinA type 3.The activity of LinA type 3 for the metabolism of δ-HCH is several orders of magnitude higher than that of LinA type 1 or LinA type 2 and can be useful for improvement of the metabolism of δ-HCH.
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