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Glycoside Hydrolase Family 95

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Revision as of 02:36, 27 March 2011 by Takane Katayama (talk | contribs)
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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.


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

<biblio>

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