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Glycoside Hydrolase Family 50

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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 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

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

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