ArticleProtein science : a publication of the Protein Society2014
Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Deciphering gene redundancy in prokaryotic genomes provides evolutionary insights for pathogenicity and its roles in clinical infections.Nature communications · 2025Article
- Use of qPCR to monitor 2,4-dinitroanisole degrading bacteria in water and soil slurry cultures.Journal of industrial microbiology & biotechnology · 2024Article
- Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms.Cells · 2023Review
- Multilayered Networks of SalmoNet2 Enable Strain Comparisons of the Salmonella Genus on a Molecular Level.mSystems · 2022Article
- Whole-cell electric sensor for determination of sodium dodecyl sulfate.World journal of microbiology & biotechnology · 2022Article
- Genomic and Functional Characterization of Environmental Strains of SDS-DegradingFrontiers in microbiology · 2018Article
- The eukaryotic enzyme Bds1 is an alkyl but not an aryl sulfohydrolase.Biochemical and biophysical research communications · 2017Article
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4 authors.
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Abstract
Sodium dodecyl sulfate (SDS) is a widely used anionic surfactant in industry and research settings, and is known to have a detrimental effect to the environment. The pathway of SDS degradation by bacteria is initiated by an alkylsulfatase and the oxidized product, 1-dodecanoic acid, subsequently enters into the β-oxidation pathway and is used as a carbon source. In this work, we solved the crystal structure of Escherichia coli uncharacterized protein YjcS and identified that it belongs to the Type III alkylsulfatase with a signal peptide (residues 1-29) at the N terminus. YjcS hydrolyzed SDS and the double mutant D184N-H185A located in the conserved HXHXDH catalytic motif abolished this activity.
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