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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 and -tetraose <cite>REF1</cite>,<cite>REF2</cite>. Three enzymes, Aga50A and Aga50D from ''Saccharophagus degradans'' and Aga50B from ''Vibrio sp.'' have been reported to be pure exo-&beta;-agarases <cite>REF3</cite>.
  
  
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== References ==
 
== References ==
 
<biblio>
 
<biblio>
#REF1 pmid=8193156
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#REF1 pmid=8517750
 +
#REF2 pmid=8193156
 +
#REF3 pmid=19802606
 
   
 
   
 
</biblio>
 
</biblio>

Revision as of 13:38, 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
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 and -tetraose [1],[2]. Three enzymes, Aga50A and Aga50D from Saccharophagus degradans and Aga50B from Vibrio sp. have been reported to be pure exo-β-agarases [3].


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, Terada I, Arita M, Noma M, and Matsumoto T. (1993). Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107. Appl Environ Microbiol. 1993;59(5):1549-54. DOI:10.1128/aem.59.5.1549-1554.1993 | PubMed ID:8517750 [REF1]
  2. 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 [REF2]
  3. Kim HT, Lee S, Lee D, Kim HS, Bang WG, Kim KH, and Choi IG. (2010). Overexpression and molecular characterization of Aga50D from Saccharophagus degradans 2-40: an exo-type beta-agarase producing neoagarobiose. Appl Microbiol Biotechnol. 2010;86(1):227-34. DOI:10.1007/s00253-009-2256-5 | PubMed ID:19802606 [REF3]

All Medline abstracts: PubMed