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Literature summary extracted from

  • Silhar, P.; Capkova, K.; Salzameda, N.T.; Barbieri, J.T.; Hixon, M.S.; Janda, K.D.
    Botulinum neurotoxin A protease: discovery of natural product exosite inhibitors (2010), J. Am. Chem. Soc., 132, 2868-2869.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.69 (2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide a synthetic hydroxamate, D-chicoric acid is synergistic with a competitive inhibitor I2 when used in combination Clostridium botulinum
3.4.24.69 caftaric acid
-
 Clostridium botulinum
3.4.24.69 chlorogenic acid
-
 Clostridium botulinum
3.4.24.69 D-chicoric acid mechanism of inhibition, overview. The inhibitor binds to an exosite, displays noncompetitive partial inhibition, and is synergistic with a competitive inhibitor I2 when used in combination Clostridium botulinum
3.4.24.69 L-chicoric acid
-
 Clostridium botulinum
3.4.24.69 additional information analysis of Echinacea components in inhibition of BoNT/A protease, overview Clostridium botulinum
3.4.24.69 N-hydroxyacetamidoadamantan a synthetic hydroxamate Clostridium botulinum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.69 Zn2+ BoNT/A is a zinc metalloprotease Clostridium botulinum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.69 SNAP-25 + H2O Clostridium botulinum i.e. 25-kDa synaptosome-associated protein ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.69 Clostridium botulinum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.69 SNAP-25 + H2O i.e. 25-kDa synaptosome-associated protein Clostridium botulinum ?
-
 ?
3.4.24.69 SNAP-25 + H2O i.e. 25-kDa synaptosome-associated protein, the Michaelis complex involves an extensive network of binding interactions ranging from the active site to the opposite surface of the BoNT/A. In the complex, the N-terminal residues of SNAP-25 147-167 form an alpha-helix, imbedded in the rear surface of BoNT/A while the C-terminal residues 201-204 form a distorted beta-strand, and the spanning residues are mostly extended Clostridium botulinum ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.69 BoNT/A
-
 Clostridium botulinum
3.4.24.69 botulinum neurotoxin A protease
-
 Clostridium botulinum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.24.69 additional information
-
 additional information inhibition kinetics and mechanism of Echinacea components on BoNT/A, overview Clostridium botulinum