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Results 1 - 8 of 8
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69more BoNT/B LC is processed for removal via the proteasome-dependent degradation pathway after ubiquitination in neuronal cells 712548
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification BoNT/A LC undergoes autocatalytic degradation into two major fragments in the presence of exogenous zinc, autolysis of wild-type and mtant BoNT/As, overview 684033
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification BoNTs are produced as a single 150 kDa polypeptide chain that is subsequently cleaved by endogenous proteases to give the dichain holotoxin 683171
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification BoNTs are synthesized as single inactive polypeptide chains that are cleaved by endogenous or exogenous proteases to generate the active dichain form of the toxin. Nicking of the single chain BoNT/E to the dichain form is associated with 100fold increase in toxicity 711228
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification limited trypsin proteolysis of BoNT produces two nicks, the first nick yields a BoNT 50 kDa light chain disulfide linked to a 100 kDa heavy chain, a second nick arose in Hc C-terminal 10 kDa. The second nick occurrs in the putative binding domain of the BoNT molecule and induces alterations in its secondary structure, leading to a significant reduction of mouse toxicity in comparison with that of the fully activated singly nicked BoNT 684032
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification the C2II binding enzyme component is proteolytically activated 683678
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification the inactive precursor protein is cleaved either by clostridial or tissue proteases into a 50-kDa light chain and a 100 kDa heavy chain linked by an essential interchain disulfide bridge and by the belt, a loop from the heavy chain that wraps around the light chain. Intracellular processing of the toxin, importance of unfolding for efficient translocation, detailed overview 710875
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.69proteolytic modification the toxins are synthesized as single polypeptide chains containing both heavy chain and light chain that are activated after undergoing posttranslational proteolysis 713567
Results 1 - 8 of 8