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Difference between revisions of "Glycoside Hydrolase Family 50"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Actually, a potential retaining mechanism of this glycoside hydrolase familly can only be inferred from analogy to clan GH-A enzymes {{CAZyDBlink}}GH50.html. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.
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Actually, a potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan GH-A enzymes {{CAZyDBlink}}GH50.html. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.
  
  
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== Three-dimensional structures ==
 
== Three-dimensional structures ==
Unknown; from analogy to clan GH-A enzymes it can be inferred that the 3D structure will be based on a (&beta;/a)<sub>8</sub> barrel fold.
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Unknown; from analogy to clan GH-A enzymes it can be inferred that the 3D structure will be based on a (&beta;/&alpha;)<sub>8</sub> barrel fold.
  
  

Revision as of 06:18, 30 June 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
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 and -hexaose [1, 2, 3, 4]. Three enzymes, Aga50A and Aga50D from Saccharophagus degradans and Aga50B from Vibrio sp. have been reported to be pure exo-β-agarases [5].


Kinetics and Mechanism

Actually, a potential retaining mechanism of this glycoside hydrolase family can only be inferred from analogy to clan GH-A enzymes https://www.cazy.org/GH50.html. No mechanistic or kintetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.


Catalytic Residues

Unkown


Three-dimensional structures

Unknown; from analogy to clan GH-A enzymes it can be inferred that the 3D structure will be based on a (β/α)8 barrel fold.


Family Firsts

Identification of first family member
The family was created in Cazy based on the work of Sugano et al. [1].
First stereochemistry determination
not determined yet.
First catalytic nucleophile identification
not determined yet.
First general acid/base residue identification
not determined yet.
First 3-D structure
not determined yet.

References

Error fetching PMID 8517750:
Error fetching PMID 8193156:
Error fetching PMID 15307821:
Error fetching PMID 17028783:
Error fetching PMID 19802606:
  1. Error fetching PMID 8517750: [REF1]
  2. Error fetching PMID 8193156: [REF2]
  3. Error fetching PMID 15307821: [REF3]
  4. Error fetching PMID 17028783: [REF4]
  5. Error fetching PMID 19802606: [REF5]

All Medline abstracts: PubMed