PROSITE documentation PDOC00117Sulfatases signatures
Sulfatases (EC 3.1.6.-) are enzymes that hydrolyze various sulfate esters. The sequence of different types of sulfatases are available. These enzymes are:
- Arylsulfatase A (EC 3.1.6.8) (ASA), a lysosomal enzyme which hydrolyzes cerebroside sulfate.
- Arylsulfatase B (EC 3.1.6.12) (ASB), a lysosomal enzyme which hydrolyzes the sulfate ester group from N-acetylgalactosamine 4-sulfate residues of dermatan sulfate.
- Arylsulfatase C (ASD).
- Arylsulfatase E (ASE).
- Steryl-sulfatase (EC 3.1.6.2) (STS) (arylsulfatase C), a membrane bound microsomal enzyme which hydrolyzes 3-β-hydroxy steroid sulfates.
- Iduronate 2-sulfatase precursor (EC 3.1.6.13) (IDS), a lysosomal enzyme that hydrolyzes the 2-sulfate groups from non-reducing-terminal iduronic acid residues in dermatan sulfate and heparan sulfate.
- N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4), an enzyme that hydrolyzes the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and the D-galactose 6-sulfate units of keratan sulfate.
- Choline sulfatase (EC 3.1.6.6) (gene betC), a bacterial enzyme that converts choline-O-sulfate to choline.
- Glucosamine-6-sulfatase (EC 3.1.6.14) (G6S), a lysosomal enzyme that hydrolyzes the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
- N-sulphoglucosamine sulphohydrolase (EC 3.10.1.1) (sulphamidase), the lysosomal enzyme that catalyzes the hydrolysis of N-sulfo-d-glucosamine into glucosamine and sulfate.
- Sea urchin embryo arylsulfatase (EC 3.1.6.1).
- Green alga arylsulfatase (EC 3.1.6.1), an enzyme which plays an important role in the mineralization of sulfates.
- Arylsulfatase (EC 3.1.6.1) from Escherichia coli (gene aslA), Klebsiella aerogenes (gene atsA) and Pseudomonas aeruginosa (gene atsA).
- Escherichia coli hypothetical protein yidJ.
It has been shown that all these sulfatases are structurally related [1,2,3].
As signature patterns for that family of enzymes we have selected the two best conserved regions. Both regions are located in the N-terminal section of these enzymes. The first region contains a conserved arginine which could be implicated in the catalytic mechanism; it is located four residues after a position that, in eukaryotic sulfatases, is a conserved cysteine which has been shown [4] to be modified to 2-amino-3-oxopropionic acid. In prokaryotes, this cysteine is replaced by a serine.
Last update:December 2004 / Pattern and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Peters C. Schmidt B. Rommerskirch W. Rupp K. Zuhlsdorf M. Vingron M. Meyer H.E. Pohlmann R. von Figura K. |
| Title | Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. | |
| Source | J. Biol. Chem. 265:3374-3381(1990). | |
| PubMed ID | 2303452 |
| 2 | Authors | Wilson P.J. Morris C.P. Anson D.S. Occhiodoro T. Bielicki J. Clements P.R. Hopwood J.J. |
| Title | Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990). | |
| PubMed ID | 2122463 |
| 3 | Authors | de Hostos E.L. Schilling J. Grossman A.R. |
| Source | Mol. Gen. Genet. 218:229-239(1989). |
| 4 | Authors | Selmer T. Hallmann A. Schmidt B. Sumper M. von Figura K. |
| Title | The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. | |
| Source | Eur. J. Biochem. 238:341-345(1996). | |
| PubMed ID | 8681943 |
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