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Glycoside Hydrolase Family 29
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- Author: ^^^Gerlind Suzlenbacher^^^
- Responsible Curator: ^^^Steve Withers^^^
| Glycoside Hydrolase Family GHnn | |
| Clan | none |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GHnn.html | |
Substrate specificities
The glycoside hydrolases of this family are exo-acting α-fucosidases from archaeal, bacterial and eukaryotic origin. No other activities have been observed. The human enzyme is of medical interest because its deficiency leads to fucosidosis, a autosomal recessive lysosomal storage disease [1].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [3].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [5].
References
- O'Brien JS, Willems PJ, Fukushima H, de Wet JR, Darby JK, Di Cioccio R, Fowler ML, and Shows TB. (1987). Molecular biology of the alpha-L-fucosidase gene and fucosidosis. Enzyme. 1987;38(1-4):45-53. DOI:10.1159/000469189 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 |
[[Category:Glycoside Hydrolase Families|GHnnn]]