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Literature summary for 2.4.1.B62 extracted from

  • Pruitt, R.; Chumbler, N.; Rutherford, S.; Farrow, M.; Friedman, D.; Spiller, B.; Lacy, D.
    Structural determinants of Clostridium difficile toxin A glucosyltransferase activity (2012), J. Biol. Chem., 287, 8013-8020.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.B62

Cloned(Commentary)

Cloned (Comment) Organism
expression in Bacillus megaterium Clostridioides difficile

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of the toxin A glucosyltransferase domain in the presence and absence of the co-substrate UDP-alpha-D-glucose, to 2.2 and 2.6 A resolution, respectively Clostridioides difficile

Inhibitors

Inhibitors Comment Organism Structure
additional information toxin A undergoes autocatalytic processing. The glucosyltransferase activity of the TcdA(1-1832) protein is activated by autoproteolysis. The presence of the autoprotease domain, residues 543-800, is restricting the activity of the glucosyl transferase domain Clostridioides difficile

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-glucose + Rap2A Clostridioides difficile modification occurs in vitro and in cells UDP + D-glucosyl-Rap2A
-
 ?
UDP-alpha-D-glucose + Rap2A Clostridioides difficile 630 modification occurs in vitro and in cells UDP + D-glucosyl-Rap2A
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridioides difficile Q189K5 toxin A
-
Clostridioides difficile 630 Q189K5 toxin A
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification toxin A undergoes autocatalytic processing. The glucosyltransferase activity of the TcdA(1-1832) protein is activated by autoproteolysis. The presence of the autoprotease domain, residues 543-800, is restricting the activity of the glucosyl transferase domain Clostridioides difficile

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-alpha-D-glucose + Cdc42
-
 Clostridioides difficile UDP + D-glucosyl-Cdc42
-
 ?
UDP-alpha-D-glucose + Cdc42
-
 Clostridioides difficile 630 UDP + D-glucosyl-Cdc42
-
 ?
UDP-alpha-D-glucose + Rac1
-
 Clostridioides difficile UDP + D-glucosyl-Rac1
-
 ?
UDP-alpha-D-glucose + Rac1
-
 Clostridioides difficile 630 UDP + D-glucosyl-Rac1
-
 ?
UDP-alpha-D-glucose + Rap2A modification occurs in vitro and in cells Clostridioides difficile UDP + D-glucosyl-Rap2A
-
 ?
UDP-alpha-D-glucose + Rap2A modification occurs in vitro and in cells Clostridioides difficile 630 UDP + D-glucosyl-Rap2A
-
 ?
UDP-alpha-D-glucose + RhoA
-
 Clostridioides difficile UDP + D-glucosyl-RhoA
-
 ?
UDP-alpha-D-glucose + RhoA
-
 Clostridioides difficile 630 UDP + D-glucosyl-RhoA
-
 ?