Accepted name: arylsulfatase (type I)
Reaction: an aryl sulfate + H2O = a phenol + sulfate
Other name(s): sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; type I sulfatase; arylsulfatase
Systematic name: aryl-sulfate sulfohydrolase
Comments: 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. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC, formylglycine-generating enzyme, EC, serine-type anaerobic sulfatase-maturating enzyme, or EC, cysteine-type anaerobic sulfatase-maturating enzyme.
1.  Dodgson, K.S., Spencer, B. and Williams, K. Studies on sulphatases. 13. The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metacaligenes. Biochem. J. 64 (1956) 216–221. [PMID: 13363831]
2.  Webb, E.C. and Morrow, P.F.W. The activation of an arysulphatase from ox liver by chloride and other anions. Biochem. J. 73 (1959) 7–15. [PMID: 13843260]
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5.  Schmidt, B., Selmer, T., Ingendoh, A. and von Figura, K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82 (1995) 271–278. [PMID: 7628016]
6.  Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273 (1998) 25560–25564. [PMID: 9748219]
[EC created 1961, modified 2011, modified 2021]