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 188.8.131.52) (ASA), a lysosomal enzyme which hydrolyzes
Arylsulfatase B (EC 184.108.40.206) (ASB), a lysosomal enzyme which hydrolyzes
the sulfate ester group from N-acetylgalactosamine 4-sulfate residues of
Arylsulfatase C (ASD).
Arylsulfatase E (ASE).
Steryl-sulfatase (EC 220.127.116.11) (STS) (arylsulfatase C), a membrane bound
microsomal enzyme which hydrolyzes 3-β-hydroxy steroid sulfates.
Iduronate 2-sulfatase precursor (EC 18.104.22.168) (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 22.214.171.124), 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 126.96.36.199) (gene betC), a bacterial enzyme that
converts choline-O-sulfate to choline.
Glucosamine-6-sulfatase (EC 188.8.131.52) (G6S), a lysosomal enzyme that
hydrolyzes the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate
and keratan sulfate.
N-sulphoglucosamine sulphohydrolase (EC 184.108.40.206) (sulphamidase), the
lysosomal enzyme that catalyzes the hydrolysis of N-sulfo-d-glucosamine into
glucosamine and sulfate.
Green alga arylsulfatase (EC 220.127.116.11), an enzyme which plays an important
role in the mineralization of sulfates.
Arylsulfatase (EC 18.104.22.168) 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  to be modified to 2-amino-3-oxopropionic acid. In prokaryotes,
this cysteine is replaced by a serine.
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