PROSITE documentation PDOC00117

Sulfatases signatures




Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

SULFATASE_1, PS00523; Sulfatases signature 1  (PATTERN)

SULFATASE_2, PS00149; Sulfatases signature 2  (PATTERN)


References

1AuthorsPeters C., Schmidt B., Rommerskirch W., Rupp K., Zuhlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K.
TitlePhylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.
SourceJ. Biol. Chem. 265:3374-3381(1990).
PubMed ID2303452

2AuthorsWilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J., Clements P.R., Hopwood J.J.
TitleHunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA.
SourceProc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990).
PubMed ID2122463

3Authorsde Hostos E.L., Schilling J., Grossman A.R.
SourceMol. Gen. Genet. 218:229-239(1989).

4AuthorsSelmer T., Hallmann A., Schmidt B., Sumper M., von Figura K.
TitleThe evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri.
SourceEur. J. Biochem. 238:341-345(1996).
PubMed ID8681943



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