InterPro domain: IPR012083

Arylsulphatase from the multicellular green flagellate Volvox carteri is a 649 amino acid polypeptide [ 1 ]. Like arylsulphatases in other organisms, it occurs in the periplasm. In Pseudomonas aeruginosa PAO1, however, this enzyme does not appear to be periplasmic or membrane-associated [ 2 ]. The synthesis of arylsufatase is repressed when sulphate, cysteine or thiocyanate is the only source for growth. A post-translational protein modification where a cysteine is replaced by a serinesemialdehydepresence has been described in two human sulphatases and in V. carteri. This modification is required for the catalytic activity of sulphatases and may be present in all sulphatases of eukaryotic origin [ 3 ].

1. An inducible arylsulfatase of Volvox carteri with properties suitable for a reporter-gene system. Purification, characterization and molecular cloning. Eur. J. Biochem. 221, 143-50
2. Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA). Eur. J. Biochem. 229, 385-94
3. The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur. J. Biochem. 238, 341-5