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- *************************
- * Sulfatases 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 esters group from N-acetylgalactosamine 4-sulfate residues of
- dermatan sulfate.
- - Steryl-sulfatase (EC 3.1.6.2) (STS) (arylsulfatase C), a membrane bound
- microsomal enzyme which hydrolyzes 3-beta-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.
- - 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.
-
- - Sea urchin embryo arylsulfatase (EC 3.1.6.1).
- - Chlamydomonas reinhardtii arylsulfatase (EC 3.1.6.1), an enzyme which plays
- an important role in the mineralization of sulfates.
- - Escherichia coli arylsulfatase (EC 3.6.1.1) (gene aslA).
- - Klebsiella aerogenes arylsulfatase (EC 3.6.1.1) (gene atsA).
- - Escherichia coli hypothetical protein yidJ.
-
- It has been shown that the mammalian enzymes and the sea urchin sulfatase are
- structurally related [1,2]; this similarity can be extended to bacterial
- enzymes [3], but the algal [4] enzyme does not show any similarity to the
- other sulfatases.
-
- 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.
-
- -Consensus pattern: [SAP]-[LIVMS]-[SC]-x-P-[STA]-R-x(2)-[LIVMF](2)-T-G
- [R is a putative active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: G-Y-x-[ST]-x(2)-[LIVMA]-G-K-x(0,1)-[FYW]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuehlsdorf M.,
- Vingron M., Meyer H.E., Pohlmann R., von Figura K.
- J. Biol. Chem. 265:3374-3381(1990).
- [ 2] Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J.,
- Clements P.R., Hopwood J.J.
- Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990).
- [ 3] de Hostos E.L., Schilling J., Grossman A.R.
- Mol. Gen. Genet. 218:229-239(1989).
- [ 4] Murooka Y., Ishibashi K., Yasumoto M., Sasaki M., Sugino H., Azakami H.,
- Yamashita M.
- J. Bacteriol. 172:2131-2140(1990).
-