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

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Family Firsts

First stereochemistry determination

1,2-α-L-Fucosidase from Bifidobacterium bifidum, determined by 1H-NMR using 2'-fucosyllactose as a substrate.[5].

First molecular cloning

1,2-α-L-Fucosidase from Bifidobacterium bifidum, by expression cloning using a genomic library conctructed in Escherichia coli.[5].

First catalytic base identification

1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis and chemical rescue of the mutants [6].

First catalytic acid residue identification

1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis of the mutant [6].

First 3-D structure

the catalytic domain of 1,2-α-L-Fucosidase from Bifidobacterium bifidum,wild-type enzyme in apo-form, E566A in complex with 2'-fucosyllactose, D766A in complex with fucose and lactose [6].

References

4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

5. PMID=15262925

6. PMID=17459873