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Difference between revisions of "Glycoside Hydrolase Family 117"

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== Substrate specificities ==
 
== Substrate specificities ==
 
The only activity so far identified in this recently discovered family of glycoside hydrolases is that α-1,3-L-(3,6-anhydro)-galactosidase <cite>1 2 3</cite>. Nevertheless phylogenetic analysis of this family and activity test on a member from an other clade show that the family GH117 is polyspecific <cite>3</cite>.
 
The only activity so far identified in this recently discovered family of glycoside hydrolases is that α-1,3-L-(3,6-anhydro)-galactosidase <cite>1 2 3</cite>. Nevertheless phylogenetic analysis of this family and activity test on a member from an other clade show that the family GH117 is polyspecific <cite>3</cite>.
 
Content is to be added here.
 
 
This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below).  Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>.  You can even cite books using just the ISBN <cite>StickWilliams</cite>.  References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. 
 
  
  
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== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
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From structural analysis and sequences alignment the catalytic residues have been predicted to be two out of the three acidic residues Asp-97, Asp-252 and Glu-310 (Zg4663 numbering) <cite>3</cite>.
  
  
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;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
 
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
 
;First 3-D structure: Zg4663, α-1,3-L-(3,6-anhydro)-galactosidase (AhgA), PDB: [http://www.pdb.org/pdb/explore/explore.do?structureId=3p2n 3P2N] <cite>3</cite>.
 
;First 3-D structure: Zg4663, α-1,3-L-(3,6-anhydro)-galactosidase (AhgA), PDB: [http://www.pdb.org/pdb/explore/explore.do?structureId=3p2n 3P2N] <cite>3</cite>.
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== References ==
 
== References ==
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#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]
 
</biblio>
 
</biblio>
 +
 +
 +
This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below).  Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>.  You can even cite books using just the ISBN <cite>StickWilliams</cite>.  References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. 
 +
  
 
[[Category:Glycoside Hydrolase Families|GH117]]
 
[[Category:Glycoside Hydrolase Families|GH117]]

Revision as of 06:13, 4 May 2011

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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 GH117
Clan None
Mechanism Not known
Active site residues Not known
CAZy DB link
https://www.cazy.org/GH117.html


Substrate specificities

The only activity so far identified in this recently discovered family of glycoside hydrolases is that α-1,3-L-(3,6-anhydro)-galactosidase [1, 2, 3]. Nevertheless phylogenetic analysis of this family and activity test on a member from an other clade show that the family GH117 is polyspecific [3].


Kinetics and Mechanism

Mechanism of glycoside hydrolase family 117 is still unknown.


Catalytic Residues

From structural analysis and sequences alignment the catalytic residues have been predicted to be two out of the three acidic residues Asp-97, Asp-252 and Glu-310 (Zg4663 numbering) [3].


Three-dimensional structures

Zg4663, α-1,3-L-(3,6-anhydro)-galactosidase (AhgA), PDB: 3P2N [3].


Family Firsts

First stereochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [4].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [6].
First 3-D structure
Zg4663, α-1,3-L-(3,6-anhydro)-galactosidase (AhgA), PDB: 3P2N [3].


References

  1. Sugano Y, Kodama H, Terada I, Yamazaki Y, and Noma M. (1994). Purification and characterization of a novel enzyme, alpha-neoagarooligosaccharide hydrolase (alpha-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107. J Bacteriol. 1994;176(22):6812-8. DOI:10.1128/jb.176.22.6812-6818.1994 | PubMed ID:7961439 [1]
  2. Suzuki H, Sawai Y, Suzuki T, and Kawai K. (2002). Purification and characterization of an extracellular alpha-neoagarooligosaccharide hydrolase from Bacillus sp. MK03. J Biosci Bioeng. 2002;93(5):456-63. DOI:10.1016/s1389-1723(02)80092-5 | PubMed ID:16233232 [2]
  3. Rebuffet E, Groisillier A, Thompson A, Jeudy A, Barbeyron T, Czjzek M, and Michel G. (2011). Discovery and structural characterization of a novel glycosidase family of marine origin. Environ Microbiol. 2011;13(5):1253-70. DOI:10.1111/j.1462-2920.2011.02426.x | PubMed ID:21332624 [3]
  4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [Sinnott1990]
  5. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 | PubMed ID:9312086 [He1999]
  6. [StickWilliams]

All Medline abstracts: PubMed


This is an example of how to make references to a journal article [4]. (See the References section below). Multiple references can go in the same place like this [4, 6]. You can even cite books using just the ISBN [7]. References that are not in PubMed can be typed in by hand [5].