CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Glycoside Hydrolase Family 29"
| Line 30: | Line 30: | ||
== Substrate specificities == | == 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 <cite>1</cite>. | 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 <cite>1</cite>. | ||
| − | + | ||
| − | |||
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 08:03, 28 October 2009
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- 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 |
-
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]]