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Difference between revisions of "Glycosyltransferase Family 1"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | The overall mechanism of GT1 enzymes features a catalytic base which activates the glycosyl acceptor, while the nucleotide glycosyl donor dissociate into an ion-pair between an oxocarbenium-like glycosyl and the phosphate of the nucleotide. | |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 00:41, 11 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
The overall mechanism of GT1 enzymes features a catalytic base which activates the glycosyl acceptor, while the nucleotide glycosyl donor dissociate into an ion-pair between an oxocarbenium-like glycosyl and the phosphate of the nucleotide.
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
From 2021 to July 2024, experimental structures of 75 different GT1 enzymes have been deposited, including with donors and acceptors. GT1 present a GT-B fold [3], characterized by two Rossman domains. The N-terminal domain binds the glycosyl acceptor site (+1), and the C-terminal one (-1) binds the glycosyl donor, usually a UDP alpha glycosyl.
Family Firsts
First 3D structure, GtfB (Amycolatopsis orientalis) PDB ID 1IIR in 2001 [4].
References
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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 |
- Bourne Y and Henrissat B. (2001). Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr Opin Struct Biol. 2001;11(5):593-600. DOI:10.1016/s0959-440x(00)00253-0 |
- Mulichak AM, Losey HC, Walsh CT, and Garavito RM. (2001). Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure. 2001;9(7):547-57. DOI:10.1016/s0969-2126(01)00616-5 |