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Glycoside Hydrolase Family 95
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- Author: ^^^Takane Katayama^^^
- Responsible Curator: ^^^Takane Katayama^^^
| Glycoside Hydrolase Family GHnn | |
| Clan | none, (α/α)6 |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GHnn.html | |
Substrate specificities
Glycoside hydrolases of this family essentially act on Fucα(1-2)Gal linkages attached at the non-reducing ends of glycoconjugates [1].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
The first solved 3-D structure was the catalytic domain (aa. 577-1474 of 1959) of 1,2-α-L-fucosidase from Bifidobacterium bifidum (PDB ID 2eab WT in apo form, PDB ID 2eac WT in compex with deoxyfuconojirimycin, PDB ID 2ead E566A in complex with 2'-fucosyllactose, PDB ID 2eae D766A in complex with fucose and lactose)[2]. The catalytic domain adopts (α/α)6-barrel fold that is quite similar to those of clan GH-L (GH15, GH65, and GH125) and GH94. The members of Clan GH-L and GH95 act on α-linkages, whereas GH94 acts on β-linkage.
Family Firsts
- First stereochemistry determination
- 1,2-α-L-Fucosidase from Bifidobacterium bifidum, determined by 1H-NMR using 2'-fucosyllactose as a substrate.[1].
- First molecular cloning
- 1,2-α-L-Fucosidase from Bifidobacterium bifidum, by expression cloning using a genomic library conctructed in Escherichia coli[1].
- First catalytic base identification
- 1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis and chemical rescue of the mutants [2].
- First catalytic acid residue identification
- 1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis of the mutant [2].
- First 3-D structure
- The catalytic domain of 1,2-α-L-fucosidase from Bifidobacterium bifidum,wild-type enzyme in apo-form, wild-type enzyme in complex with deoxyfuconojirimycin, E566A in complex with 2'-fucosyllactose, D766A in complex with fucose and lactose [2].
References
<biblio>
- Katayama2004 pmid=15262925
- Nagae2007 pmid=17459873