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Difference between revisions of "Glycoside Hydrolase Family 95"
| Line 47: | Line 47: | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: 1,2-α-L-Fucosidase from ''Bifidobacterium bifidum'', determined by 1H-NMR using 2'-fucosyllactose as a substrate. <cite> | + | ;First stereochemistry determination:1,2-α-L-Fucosidase from ''Bifidobacterium bifidum'', determined by 1H-NMR using 2'-fucosyllactose as a substrate.<cite>Katayama2004</cite>. |
| − | ;First catalytic | + | ;First molecular cloning:1,2-α-L-Fucosidase from ''Bifidobacterium bifidum'', by expression cloning using a genomic library conctructed in Escherichia coli.<cite>Katayama2004</cite>. |
| − | ;First | + | ;First catalytic base identification:1,2-α-L-Fucosidase from ''Bifidobacterium bifidum'', kinetic analysis and chemical rescue of the mutants <cite>Nagae2007</cite>. |
| − | ;First 3-D structure: | + | ;First catalytic acid residue identification:1,2-α-L-Fucosidase from ''Bifidobacterium bifidum'', kinetic analysis of the mutant <cite>Nagae2007</cite>. |
| + | ;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 <cite>Nagae2007</cite>. | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Katayama2004 PMID=15262925 |
| − | # | + | #Nagae2007 PMID=17459873 |
#StickWilliams isbn=978-0-240-52118-3 | #StickWilliams isbn=978-0-240-52118-3 | ||
#Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | #Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | ||
Revision as of 01:34, 27 March 2011
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: ^^^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
Content is to be added here.
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
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 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
- Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
-
PMID=15262925
-
PMID=17459873