Glycoside Hydrolase Family 95

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• Author: ^^^Takane Katayama^^^
• Responsible Curator: ^^^Takane Katayama^^^

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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

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This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].

Kinetics and Mechanism

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Catalytic Residues

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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)[5].. 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.[6].

First molecular cloning

1,2-α-L-Fucosidase from Bifidobacterium bifidum, by expression cloning using a genomic library conctructed in Escherichia coli[6].

First catalytic base identification

1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis and chemical rescue of the mutants [5].

First catalytic acid residue identification

1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis of the mutant [5].

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 [5].

References

<biblio>

1. Katayama2004 pmid=15262925
2. Nagae2007 pmid=17459873