{PDOC00324}
{PS00385; ALPHA_L_FUCOSIDASE}
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* Alpha-L-fucosidase putative active site *
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Alpha-L-fucosidase (EC 3.2.1.51) [1] is a  lysosomal  enzyme  responsible  for
hydrolyzing   the   alpha-1,6-linked  fucose  joined   to   the   reducing-end
N-acetylglucosamine  of the carbohydrate moieties of glycoproteins. Deficiency
of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.

A cysteine residue is important for the activity of the enzyme.  There is only
one cysteine conserved  between  the sequence of  mammalian alpha-L-fucosidase
and that of the slime mold Dictyostelium discoideum. We have derived a pattern
from the region around that conserved cysteine.

-Consensus pattern: P-x(2)-L-x(3)-K-W-E-x-C
                    [C may be the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These proteins belong to family 29  in  the  classification of glycosyl
 hydrolases [2,E1].

-Last update: May 2004 / Text revised.

[ 1] Fisher K.J., Aronson N.N. Jr.
     "Isolation and sequence analysis of a cDNA encoding rat liver
     alpha-L-fucosidase."
     Biochem. J. 264:695-701(1989).
     PubMed=2482732
[ 2] Henrissat B.
     "A classification of glycosyl hydrolases based on amino acid sequence
     similarities."
     Biochem. J. 280:309-316(1991).
     PubMed=1747104
[E1] https://www.uniprot.org/docs/glycosid

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