ArticleApplied and environmental microbiology2007
Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by X-Ray crystallography and microcalorimetry.
Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Quantum mechanical investigation and environmental engineering of LinB for enhanced polyvinyl chloride degradation.Molecular diversity · 2026Article
- ChannelsDB 2.0: a comprehensive database of protein tunnels and pores in AlphaFold era.Nucleic acids research · 2024Article
- Structural and catalytic effects of surface loop-helix transplantation within haloalkane dehalogenase family.Computational and structural biotechnology journal · 2020Article
- The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements.PloS one · 2020Article
- Structures of hyperstable ancestral haloalkane dehalogenases show restricted conformational dynamics.Computational and structural biotechnology journal · 2020Article
- A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization.The Journal of biological chemistry · 2013Article
- Transformation and biodegradation of 1,2,3-trichloropropane (TCP).Environmental science and pollution research international · 2012Review
- Biochemical characterization of haloalkane dehalogenases DrbA and DmbC, Representatives of a Novel Subfamily.Applied and environmental microbiology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1,2,3-Trichloropropane (TCP) is a highly toxic and recalcitrant compound. Haloalkane dehalogenases are bacterial enzymes that catalyze the cleavage of a carbon-halogen bond in a wide range of organic halogenated compounds. Haloalkane dehalogenase LinB from Sphingobium japonicum UT26 has, for a long time, been considered inactive with TCP, since the reaction cannot be easily detected by conventional analytical methods. Here we demonstrate detection of the weak activity (k(cat) = 0.005 s(-1)) of LinB with TCP using X-ray crystallography and microcalorimetry. This observation makes LinB a useful starting material for the development of a new biocatalyst toward TCP by protein engineering. Microcalorimetry is proposed to be a universal method for the detection of weak enzymatic activities. Detection of these activities is becoming increasingly important for engineering novel biocatalysts using the scaffolds of proteins with promiscuous activities.
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Registered trials
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