Sulfatases, which cleave sulfate esters in biological systems, play a key role in regulating
the sulfation states that determine the function of many physiological molecules. Sulfatase …

Sulfatases contain an active site formylglycine residue that is generated by post-translational
modification. Crystal structures of two lysosomal sulfatases revealed significant similarity to …

Sulfatases cleave sulfate groups from various molecules and constitute a biologically and
industrially important group of enzymes. However, the number of sulfatases whose substrate …

Background: Sulfatases constitute a family of enzymes with a highly conserved active site
region including a Cα− formylglycine that is posttranslationally generated by the oxidation of …

The sulfatase family of enzymes catalyzes hydrolysis of sulfate ester bonds of a wide variety
of substrates. Seventeen genes have been identified in this class of sulfatases, many of …

The sulfonation (also known as sulfurylation) of biomolecules has long been known to take
place in a variety of organisms, from prokaryotes to multicellular species, and new biological …

Arylsulfatase A belongs to the sulfatase family whose members carry a Cα-formylglycine that
is post-translationally generated by oxidation of a conserved cysteine or serine residue. The …

Sulfatases are a highly conserved family of enzymes found in all three domains of life. To be
active, sulfatases undergo a unique post-translational modification leading to the conversion …

Formylglycine (fGly) is a catalytically essential residue found almost exclusively in the active
sites of type I sulfatases. Formed by post-translational oxidation of cysteine or serine side …

Arylsulfatase A (ASA) belongs to the sulfatase family whose members carry a Cα-
formylglycine that is post-translationally generated by oxidation of a conserved cysteine or …