Glycoside hydrolase family 29 explained

Symbol:Alpha_L_fucos
Alpha-L-fucosidase
Pfam:PF01120
Pfam Clan:CL0058
Interpro:IPR000933
Prosite:PDOC00324
Scop:1hl9
Cazy:GH29

In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases.

Glycoside hydrolases 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 >100 different families.[1] [2] [3] This classification is available on the CAZy web site,[4] [5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6] [7]

Glycoside hydrolase family 29 includes alpha-L-fucosidases,[8] 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.[9] 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.[9]

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.[10] 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.[11]

Notes and References

  1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G . Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases . Proceedings of the National Academy of Sciences of the United States of America . 92 . 15 . 7090–4 . July 1995 . 7624375 . 41477 . 10.1073/pnas.92.15.7090 . 1995PNAS...92.7090H . free .
  2. Davies G, Henrissat B . Structures and mechanisms of glycosyl hydrolases . Structure . 3 . 9 . 853–9 . September 1995 . 8535779 . 10.1016/S0969-2126(01)00220-9 . free .
  3. Henrissat B, Bairoch A . Updating the sequence-based classification of glycosyl hydrolases . The Biochemical Journal . 316 . Pt 2 . 695–6 . June 1996 . 8687420 . 1217404 . 10.1042/bj3160695.
  4. Web site: Home. CAZy.org. en. 2018-03-06.
  5. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B . The carbohydrate-active enzymes database (CAZy) in 2013 . Nucleic Acids Research . 42 . Database issue . D490-5 . January 2014 . 24270786 . 10.1093/nar/gkt1178 . 3965031 .
  6. Web site: Glycoside Hydrolase Family 29. CAZypedia.org. en. 2018-03-06.
  7. Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes . Glycobiology . 28 . 1 . 3–8 . December 2018 . 29040563 . 10.1093/glycob/cwx089 . CAZypedia Consortium . free .
  8. Fisher KJ, Aronson NN . Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase . The Biochemical Journal . 264 . 3 . 695–701 . December 1989 . 2482732 . 1133642 . 10.1042/bj2640695.
  9. Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y . Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis . The Journal of Biological Chemistry . 279 . 13 . 13119–28 . March 2004 . 14715651 . 10.1074/jbc.M313783200 . free .
  10. Pasini ME, Intra J, Pavesi G . Expression study of an alpha-l-fucosidase gene in the Drosophilidae family . Gene . 420 . 1 . 23–33 . August 2008 . 18556148 . 10.1016/j.gene.2008.04.021 .
  11. Venditti JJ, Bean BS . Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment . International Journal of Andrology . 32 . 5 . 556–62 . October 2009 . 18522672 . 10.1111/j.1365-2605.2008.00897.x . free .

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