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Difference between revisions of "Glycosyltransferase Family 138"

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== Substrate specificities ==
 
== Substrate specificities ==
GT138 family of glycosyltransferase is exemplified by AvrB that contains a Fido domain <cite>Peng2024, Kinch2009</cite>. AvrB is a bacterial effector from the plant pathogen ''Pseudomonas syringae''. AvrB utilizes UDP-rhamnose or dTDP-rhamnose as a co-substrate to modify the host protein RIN4 and causes the programmed cell death (namely hypersensitive response).
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GT138 family of glycosyltransferase is exemplified by AvrB that contains a Fido domain <cite>Peng2024, Kinch2009</cite>. Proteins with Fido domain are diverse enzymes with activities of AMPylation, phosphorylation, UMPylation, and phosphocholination. AvrB is a bacterial effector from the plant pathogen ''Pseudomonas syringae''. AvrB utilizes UDP-rhamnose or dTDP-rhamnose as a co-substrate to modify the host protein RIN4 and causes the programmed cell death (namely hypersensitive response).
 
 
 
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==

Revision as of 23:08, 31 January 2025

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Glycosyltransferase Family GT138
Clan Fido
Mechanism Inverting
Active site residues Known
CAZy DB link
https://www.cazy.org/GT138.html


Substrate specificities

GT138 family of glycosyltransferase is exemplified by AvrB that contains a Fido domain [1, 2]. Proteins with Fido domain are diverse enzymes with activities of AMPylation, phosphorylation, UMPylation, and phosphocholination. AvrB is a bacterial effector from the plant pathogen Pseudomonas syringae. AvrB utilizes UDP-rhamnose or dTDP-rhamnose as a co-substrate to modify the host protein RIN4 and causes the programmed cell death (namely hypersensitive response).

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination
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First catalytic nucleophile identification
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First general acid/base residue identification
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First 3-D structure
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References

  1. 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]
  2. 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]