Pathways & interactions
Sulfatase, conserved site (IPR024607)
Short name: Sulfatase_CS
Sulphatases EC:3.1.6. are enzymes that hydrolyze various sulphate esters. The sequence of different types of sulphatases are available and have shown to be structurally related [PMID: 2303452, PMID: 2122463, PMID: 2476654]; these include:
- arylsulphatase A EC:220.127.116.11 (ASA), a lysosomal enzyme which hydrolyses cerebroside sulphate;
- arylsulphatase B EC:18.104.22.168 (ASB), which hydrolyses the sulphate ester group from N-acetylgalactosamine 4-sulphate residues of dermatan sulphate;
- arylsulphatase C (ASD) and E (ASE);
- steryl-sulphatase EC:22.214.171.124 (STS), a membrane bound microsomal enzyme which hydrolyses 3-beta-hydroxy steroid sulphates;
- iduronate 2-sulphatase precursor EC:126.96.36.199 (IDS), a lysosomal enzyme that hydrolyses the 2-sulphate groups from non-reducing-terminal iduronic acid residues in dermatan sulphate and heparan sulphate;
- N-acetylgalactosamine-6-sulphatase EC:188.8.131.52, which hydrolyses the 6-sulphate groups of the N-acetyl-d-galactosamine 6-sulphate units of chondroitin sulphate and the D-galactose 6-sulphate units of keratan sulphate;
- glucosamine-6-sulphatase EC:184.108.40.206 (G6S), which hydrolyses the N-acetyl-D-glucosamine 6-sulphate units of heparan sulphate and keratan sulphate;
- N-sulphoglucosamine sulphohydrolase EC:220.127.116.11 (sulphamidase), the lysosomal enzyme that catalyses the hydrolysis of N-sulpho-d-glucosamine into glucosamine and sulphate;
- sea urchin embryo arylsulphatase EC:18.104.22.168;
- green algae arylsulphatase EC:22.214.171.124, which plays an important role in the mineralisation of sulphates;
- and arylsulphatase EC:126.96.36.199 from Escherichia coli (aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA).
This entry represents two conserved sites for the sulphatase family located in the N-terminal region. The SULPHATASE_1 site contains the conserved arginine which could be implicated in the catalytic mechanism; it is located four residues after a position that, in eukaryotic sulphatases, is a conserved cysteine which has been shown [PMID: 8681943] to be modified to 2-amino-3-oxopropionic acid. In prokaryotes, this cysteine is replaced by a serine.