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PROSITE documentation PDOC00324

Alpha-L-fucosidase putative active site





Description

α-L-fucosidase (EC 3.2.1.51) [1] is a lysosomal enzyme responsible for hydrolyzing the α-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of α-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 α-L-fucosidase and that of the slime mold Dictyostelium discoideum. We have derived a pattern from the region around that conserved cysteine.

Note:

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

Last update:

May 2004 / Text revised.

Technical section

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

ALPHA_L_FUCOSIDASE, PS00385; Alpha-L-fucosidase putative active site  (PATTERN)


References

1AuthorsFisher K.J., Aronson N.N. Jr.
TitleIsolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase.
SourceBiochem. J. 264:695-701(1989).
PubMed ID2482732

2AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104

E1Sourcehttp://www.uniprot.org/docs/glycosid



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