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Literature summary for 3.4.24.69 extracted from

  • Wang, H.H.; Riding, S.; Lindo, P.; Singh, B.R.
    Endopeptidase activities of botulinum neurotoxin type B complex, holotoxin, and light chain (2010), Appl. Environ. Microbiol., 76, 6658-6663.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol
-
Clostridium botulinum

Protein Variants

Protein Variants Comment Organism
additional information the endopeptidase activities of the three forms (complex, purified BoNT/B holotoxin, and separated light chain) are compared under the same conditions. Results show that enzyme activities of the three forms differ significantly and are dependent on nicking and disulfide reduction conditions. Light chain form has the highest level of activity, and the complex has the lowest. The activity is enhanced by nicking of BoNT/B holotoxin and is enhanced even more by dithiothreitol reduction after nicking Clostridium botulinum

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
VAMPTide + H2O
-
Clostridium botulinum ?
-
?

Synonyms

Synonyms Comment Organism
BoNT/B
-
Clostridium botulinum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Clostridium botulinum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Clostridium botulinum