Sulfatases (EC 3.1.6.1) are grouped into three types of enzymes. Type I enzymes use 3-oxo-L-alanine or formylglycine, as the catalytic residue. Type II enzymes are non-heme iron-dependent dioxygenases. Type III enzymes adopt a metallo-beta-lactamase fold and bind two zinc ions as cofactors. Sulfazyme™ is a type I arylsulfatase. Arylsulfatases are found in both prokaryotes and eukaryotes with similar substrate preferences. In type I enzymes, 3-oxo-L-alanine initiates the reaction by nucleophilic attack on the sulfur atom of the substrate¹.

The Sulfazyme™ product line are purified recombinant and genetically modified arylsulfatases designed to hydrolyze sulfated compounds at 37 °C at or near pH 8.0. Sulfazyme hydrolyzes beta-linked sulfate ester groups from metabolites generated during phase II detoxification process. Sulfazyme™ is an excellent alternative to acid hydrolysis for the analysis of compounds that contain a sulfate ester moiety. Strong acid hydrolysis can lead to analyte degradation or increased matrix interference, thus artificially altering results².

Choose between Sulfazyme™ PaS for general sulfatase needs, genetically engineered Sulfazyme DS for hydrolyzing dehydroepiandrosterone sulfate (DHEAS), or genetically engineered Sulfazyme βAS for hydrolyzing boldenone sulfate, and testosterone sulfate. Additionally, Sulfazyme™ can be paired with our beta-glucuronidase to analyze both glucuronidated and sulfated metabolites simultaneously. Consult the table below to learn more or sign up to test our next-generation sulfatase variants.

Please contact us to learn more.