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Difference between revisions of "Glycosyltransferase Family 1"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
  
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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 01:41, 11 July 2024

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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.


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
http://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

  1. 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.

    [DaviesSinnott2008]
  2. 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 | PubMed ID:18838391 [Cantarel2009]
  3. 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 | PubMed ID:11785761 [Bourne2001]
  4. 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 | PubMed ID:11470430 [Mulichak2001]

All Medline abstracts: PubMed