2.4.1.B62: small GTPase glucosyltransferase
This is an abbreviated version!
For detailed information about small GTPase glucosyltransferase, go to the full flat file.
Reaction
Synonyms
Clostridium sordellii lethal toxin, cytotoxin B, cytotoxin L, glucosyltransferase TcdA, glucosyltransferase TcdB, haemorrhagic toxin, hemorrhagic toxin, letal toxin, lethal toxin, lethal-toxin, TcdA, TcdB, TcsH, TcsL, toxA, ToxB, toxin, toxin A, toxin B
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 2.4.1.B62 - small GTPase glucosyltransferase
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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
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
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
proteolytic modification
the toxin requires InsP6-dependent autocleavage for activation
proteolytic modification
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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
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proteolytic modification
maturation of the host cell endosome causes a conformational change in the pore-forming domain of TcsL, causing it to form a pore in the endosomal membrane. The autoprocessing domain is activated by host inositol hexakisphosphate and cleaves the glucosyltransferase domain (GTD), presumably to permit access to substrates residing at the plasma membrane
proteolytic modification
Paeniclostridium sordellii JGS6382
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maturation of the host cell endosome causes a conformational change in the pore-forming domain of TcsL, causing it to form a pore in the endosomal membrane. The autoprocessing domain is activated by host inositol hexakisphosphate and cleaves the glucosyltransferase domain (GTD), presumably to permit access to substrates residing at the plasma membrane
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