||Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. It is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 22.214.171.124, branched primary-alkylsulfatase, and EC 126.96.36.199, (R)-specific secondary-alkylsulfatase (type III).
||Hagelueken, G., Adams, T.M., Wiehlmann, L., Widow, U., Kolmar, H., Tummler, B., Heinz, D.W. and Schubert, W.D. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proc. Natl. Acad. Sci. USA 103 (2006) 7631–7636. [DOI] [PMID: 16684886]
||Long, M., Ruan, L., Li, F., Yu, Z. and Xu, X. Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP). Extremophiles 15 (2011) 293–301. [DOI] [PMID: 21318560]
||Liang, Y., Gao, Z., Dong, Y. and Liu, Q. Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase. Protein Sci. 23 (2014) 1442–1450. [DOI] [PMID: 25066955]
||Sun, L., Chen, P., Su, Y., Cai, Z., Ruan, L., Xu, X. and Wu, Y. Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9. Biosci Rep 37 (2017) . [DOI] [PMID: 28442601]