Alkylsulfatase that cleaves primary alkyl sulfates such as sodium octyl sulfate and the widely used detergent sodium dodecyl sulfate (SDS). a primary linear alkyl sulfate ester + H2O = a primary alcohol + H(+) + sulfate Binds 2 Zn(2+) ions per subunit. Inhibited by EDTA. Slightly activated in the presence of Ca(2+). kcat is 4.88 sec(-1) with SDS as substrate. Optimum pH is 9.0. Optimum temperature is 70 degrees Celsius. Retains more than 90% activity after incubation at 65 degrees Celsius for 1 hour. Homodimer. Contains three distinct domains: an N-terminal catalytic domain that contains a binuclear Zn(2+) cluster, a central dimerization domain and a C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. The thermal stability and higher specific activities make it an ideal candidate for the application in the biodegradation of SDS-containing waste water under elevated temperature conditions. Belongs to the metallo-beta-lactamase superfamily. Type III sulfatase family.