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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
+
#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 11:59, 29 May 2010

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Glycoside Hydrolase Family GH50
Clan GH-A
Mechanism probably retaining
Active site residues inferred from clan GH-A as two Glu
CAZy DB link
https://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]