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Literature summary for 2.4.1.B62 extracted from

  • Egerer, M.; Giesemann, T.; Jank, T.; Satchell, K.J.; Aktories, K.
    Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity (2007), J. Biol. Chem., 282, 25314-25321.
    View publication on PubMed
Search for more literature for 2.4.1.B62

Protein Variants

Protein Variants Comment Organism
C698A mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity Clostridioides difficile
D587N mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity Clostridioides difficile
H653A mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity Clostridioides difficile
additional information expression of a fragment of toxin B, covering residues 1–955. Wild-type fragment of toxin B is always recovered as a cleaved product with fragments of 63 and 47 kDa, whereas the mutants with changes C698A or H653A are expressed in full length Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile P16154 toxin A
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Clostridioides difficile P18177 toxin B
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification in presence of dithiothreitol or 2-mercaptoethanol, toxin A undergoes autocatalytic cleavage to an N-terminal catalytic domain of 60 kDa and a C-terminal part of 250 kDa. N-ethylmaleimide or iodoacetamide block this cleavage Clostridioides difficile
proteolytic modification in presence of dithiothreitol or 2-mercaptoethanol, toxin B undergoes autocatalytic cleavage with release of the catalytic domain and a fragment of 210 kDa. Myo-inositol hexakisphosphate also facilitates cleavage and has a synergistic effect with dithiothreitol. Co-treatment of toxin B with N-ethylmaleimide blocks the processing induced by myo-inositol hexakisphosphate Clostridioides difficile

General Information

General Information Comment Organism
metabolism cytotoxin A possesses an inherent cysteine protease activity, which is responsible for auto-cleavage of glucosylating toxins Clostridioides difficile
metabolism cytotoxin B possesses an inherent cysteine protease activity, which is responsible for auto-cleavage of glucosylating toxins Clostridioides difficile