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Difference between revisions of "Glycoside Hydrolase Family 50"

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== Substrate specificities ==
 
== Substrate specificities ==
To date, all characterized [[glycoside hydrolases]] of family 50 are &beta-agarases (EC [{{EClink}}3.2.1.81 3.2.1.81]) that cleave &beta;-1,4 glycosidic bonds of agarose, releasing neoagaro-biose, -tetraose or -hexaose. Three enzymes, Aga50A and Aga50D from Saccharophagus degradans and Aga50B from Vibrio sp. have been reported to be pure exo-&beta-agarases <cite>REF1</cite>
+
To date, all characterized [[glycoside hydrolases]] of family 50 are &beta;-agarases (EC [{{EClink}}3.2.1.81 3.2.1.81]) that cleave &beta;-1,4 glycosidic bonds of agarose, releasing neoagaro-biose, -tetraose or -hexaose. Three enzymes, Aga50A and Aga50D from Saccharophagus degradans and Aga50B from Vibrio sp. have been reported to be pure exo-&beta;-agarases <cite>REF1</cite>
  
  
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== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.
+
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
+
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation.
;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.
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.
+
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
 
#REF1 pmid=8193156
 
#REF1 pmid=8193156
#He1999 pmid=9312086
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#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]
 
 
</biblio>
 
</biblio>
  
  
 
[[Category:Glycoside Hydrolase Families|GH050]]
 
[[Category:Glycoside Hydrolase Families|GH050]]

Revision as of 12:59, 29 May 2010

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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 GH50
Clan GH-A
Mechanism probably retaining
Active site residues inferred from clan GH-A as two Glu
CAZy DB link
http://www.cazy.org/GH50.html


Substrate specificities

To date, all characterized glycoside hydrolases of family 50 are β-agarases (EC 3.2.1.81) that cleave β-1,4 glycosidic bonds of agarose, releasing neoagaro-biose, -tetraose or -hexaose. Three enzymes, Aga50A and Aga50D from Saccharophagus degradans and Aga50B from Vibrio sp. have been reported to be pure exo-β-agarases [1]


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
Cite some reference here, with a short (1-2 sentence) explanation .
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation.
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation.
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation.

References

  1. Sugano Y, Matsumoto T, and Noma M. (1994). Sequence analysis of the agaB gene encoding a new beta-agarase from Vibrio sp. strain JT0107. Biochim Biophys Acta. 1994;1218(1):105-8. DOI:10.1016/0167-4781(94)90109-0 | PubMed ID:8193156 [REF1]