CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Glycoside Hydrolase Family 50"
Harry Brumer (talk | contribs) m (Text replacement - "\^\^\^(.*)\^\^\^" to "$1") |
|||
| Line 1: | Line 1: | ||
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> | ||
{{CuratorApproved}} | {{CuratorApproved}} | ||
| − | * [[Author]]: | + | * [[Author]]: [[User:Mirjam Czjzek|Mirjam Czjzek]] |
| − | * [[Responsible Curator]]: | + | * [[Responsible Curator]]: [[User:Mirjam Czjzek|Mirjam Czjzek]] |
---- | ---- | ||
Latest revision as of 13:14, 18 December 2021
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
| 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
That GH50 enzymes potentially utilize a retaining mechanism has only been inferred by analogy with clan GH-A enzymes. No mechanistic or kinetic analysis demonstrating the stereochemical outcome of the reaction have been reported for this family to date.
Catalytic Residues
Similarly, the catalytic residues in this family have not been directly identified, but may be inferred from superposition with other clan GH-A enzymes.
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
- This family was created in the CAZy Ddatabase following 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 8193156:
Error fetching PMID 15307821:
Error fetching PMID 17028783:
Error fetching PMID 19802606:
- Error fetching PMID 8517750:
- Error fetching PMID 8193156:
- Error fetching PMID 15307821:
- Error fetching PMID 17028783:
- Error fetching PMID 19802606: