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Glycoside Hydrolase Family 50
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- Author:
- Responsible Curator: ^^^Mirjam Czjzek^^^
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 familly 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/a)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
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