PROSITE documentation PDOC00324Alpha-L-fucosidase putative active site
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.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Fisher K.J. Aronson N.N. Jr. |
Title | Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase. | |
Source | Biochem. J. 264:695-701(1989). | |
PubMed ID | 2482732 |
2 | Authors | Henrissat B. |
Title | A classification of glycosyl hydrolases based on amino acid sequence similarities. | |
Source | Biochem. J. 280:309-316(1991). | |
PubMed ID | 1747104 |
E1 | Title | https://www.uniprot.org/docs/glycosid |
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