Glycoside hydrolase family 29
| Alpha-L-fucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of thermotoga maritima alpha-fucosidase | |||||||||
| Identifiers | |||||||||
| Symbol | Alpha_L_fucos | ||||||||
| Pfam | PF01120 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR000933 | ||||||||
| PROSITE | PDOC00324 | ||||||||
| SCOP | 1hl9 | ||||||||
| SUPERFAMILY | 1hl9 | ||||||||
| CAZy | GH29 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of over 100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
Glycoside hydrolase family 29 includes alpha-L-fucosidases,[6] They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.[7] The enzyme is a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain.[7]
Drosophila melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilisation by interacting with alpha-l-fucose residues on the micropyle of the eggshell.[8] In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. These help preserve protein integrity.[9]
References
- ↑ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477
. PMID 7624375. - ↑ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ↑ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ↑ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ↑ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ↑ Fisher KJ, Aronson NN (December 1989). "Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase". Biochem. J. 264 (3): 695–701. PMC 1133642. PMID 2482732.
- 1 2 Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y (March 2004). "Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis". J. Biol. Chem. 279 (13): 13119–28. doi:10.1074/jbc.M313783200. PMID 14715651.
- ↑ Pasini ME, Intra J, Pavesi G (August 2008). "Expression study of an alpha-l-fucosidase gene in the Drosophilidae family". Gene. 420 (1): 23–33. doi:10.1016/j.gene.2008.04.021. PMID 18556148.
- ↑ Venditti JJ, Bean BS (October 2009). "Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment". Int. J. Androl. 32 (5): 556–62. doi:10.1111/j.1365-2605.2008.00897.x. PMID 18522672.
This article incorporates text from the public domain Pfam and InterPro IPR000933