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 See a page that's out-of-date and just needs a touch-up?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 "Glycosyltransferase Family 1"
David Teze (talk | contribs) |
David Teze (talk | contribs) |
||
| Line 40: | Line 40: | ||
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | The large majority of GT1 presents a His-Asp catalytic dyad, acting as a general base. The histidine abstract a proton, increasing the nucleophilicity of the glycosyl acceptor. The aspartate activates the histidine, the abstracted proton being shared almost equally between these two residues. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | GT1 present a GT-B fold, | |
== Family Firsts == | == Family Firsts == | ||
Revision as of 01:13, 9 July 2024
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.
| Glycosyltransferase Family GT1 | |
| Fold | GT-B, 2 Rosmann domains |
| Mechanism | Inverting via a SN2 (O-, N-, S-) or SEAr (C-) |
| Active site residues | Generally a His/Asp dyad as catalytic base |
| CAZy DB link | |
| https://www.cazy.org/GT1.html | |
Substrate specificities
Content is to be added here
Authors may get an idea of what to put in each field from Curator Approved Glycosyltransferase Families. (TIP: Right click with your mouse and open this link in a new browser window...)
In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
The large majority of GT1 presents a His-Asp catalytic dyad, acting as a general base. The histidine abstract a proton, increasing the nucleophilicity of the glycosyl acceptor. The aspartate activates the histidine, the abstracted proton being shared almost equally between these two residues.
Three-dimensional structures
GT1 present a GT-B fold,
Family Firsts
Content is to be added here.
References
-
Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. DOI:10.1042/BIO03004026.
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |