Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00324Alpha-L-fucosidase putative active site
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00324
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.
-------------------------------------------------------------------------------
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 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.