Publications

• Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9.

  Sun L., Chen P., Su Y., Cai Z., Ruan L., Xu X., Wu Y.

  A novel alkylsulfatase from bacterium <i>Pseudomonas sp. S9</i> (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structu ... >> More

  A novel alkylsulfatase from bacterium <i>Pseudomonas sp. S9</i> (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of 'primary alkyl' chains, confirming that SdsAP is a primary alkylsulfatase. << Less

  Biosci. Rep. 37:0-0(2017) [PubMed] [EuropePMC]

• The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases.

  Hagelueken G., Adams T.M., Wiehlmann L., Widow U., Kolmar H., Tuemmler B., Heinz D.W., Schubert W.D.

  Pseudomonas aeruginosa is both a ubiquitous environmental bacterium and an opportunistic human pathogen. A remarkable metabolic versatility allows it to occupy a multitude of ecological niches, including wastewater treatment plants and such hostile environments as the human respiratory tract. P. a ... >> More

  Pseudomonas aeruginosa is both a ubiquitous environmental bacterium and an opportunistic human pathogen. A remarkable metabolic versatility allows it to occupy a multitude of ecological niches, including wastewater treatment plants and such hostile environments as the human respiratory tract. P. aeruginosa is able to degrade and metabolize biocidic SDS, the detergent of most commercial personal hygiene products. We identify SdsA1 of P. aeruginosa as a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as SDS as a sole carbon or sulfur source. Homologues of SdsA1 are found in many pathogenic and some nonpathogenic bacteria. The crystal structure of SdsA1 reveals three distinct domains. The N-terminal catalytic domain with a binuclear Zn2+ cluster is a distinct member of the metallo-beta-lactamase fold family, the central dimerization domain ensures resistance to high concentrations of SDS, whereas the C-terminal domain provides a hydrophobic groove, presumably to recruit long aliphatic substrates. Crystal structures of apo-SdsA1 and complexes with substrate analog and products indicate an enzymatic mechanism involving a water molecule indirectly activated by the Zn2+ cluster. The enzyme SdsA1 thus represents a previously undescribed class of sulfatases that allows P. aeruginosa to survive and thrive under otherwise bacteriocidal conditions. << Less

  Proc. Natl. Acad. Sci. U.S.A. 103:7631-7636(2006) [PubMed] [EuropePMC]

• Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP).

  Long M., Ruan L., Li F., Yu Z., Xu X.

  A novel alkylsulfatase gene, sdsAP, was cloned from a newly isolated bacterium Pseudomonas sp. S9. It encoded a protein of 675 amino acids with a calculated molecular mass of 74.9 kDa. The protein contained a typical N-terminal signal peptide of 41 amino acid residues, followed by a metallo-β-lact ... >> More

  A novel alkylsulfatase gene, sdsAP, was cloned from a newly isolated bacterium Pseudomonas sp. S9. It encoded a protein of 675 amino acids with a calculated molecular mass of 74.9 kDa. The protein contained a typical N-terminal signal peptide of 41 amino acid residues, followed by a metallo-β-lactamase like domain at the N-terminus and a SCP-2-like domain at the C-terminus. This domain organization mode suggested that it belonged to the type III sulfatase. The mature alkylsulfatase was overexpressed in Escherichia coli. The optimal temperature and pH of the recombinant SdsAP were 70°C and 9.0, respectively. Notably, at optimal conditions, the purified recombinant SdsAP had a high specific activity of 23.25 μmol min(-1) mg(-1), a K(m (app)) of 264.3 μmol, and a V(max (app)) of 33.8 μmol min(-1) mg(-1) for SDS. Additionally, it still retained more than 90% activity after incubation at 65°C for 1 h, which was much different from other alkylsulfatases reported. The recombinant enzyme hydrolyzed the primary alkyl sulfate such as sodium octyl sulfate and sodium dodecyl sulfate (SDS). It was a Zn(2+)-containing and Ca(2+) activated alkylsulfatase. This is the first report to explore the various characteristics of the heterologous recombinant alkylsulfatase in details. These favorable properties could make SdsAP attractive to be useful in the degradation of SDS-containing waste. << Less

  Extremophiles 15:293-301(2011) [PubMed] [EuropePMC]

• Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase.

  Liang Y., Gao Z., Dong Y., Liu Q.

  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 e ... >> More

  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. << Less

  Protein Sci. 23:1442-1450(2014) [PubMed] [EuropePMC]