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Literature summary for 3.4.24.69 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
Search for more literature for 3.4.24.69

Inhibitors

Inhibitors Comment Organism Structure
(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
caftaric acid
-
 Clostridium botulinum
chlorogenic acid
-
 Clostridium botulinum
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
L-chicoric acid
-
 Clostridium botulinum
additional information analysis of Echinacea components in inhibition of BoNT/A protease, overview Clostridium botulinum
N-hydroxyacetamidoadamantan a synthetic hydroxamate Clostridium botulinum

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SNAP-25 + H2O i.e. 25-kDa synaptosome-associated protein Clostridium botulinum ?
-
 ?
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

Synonyms Comment Organism
BoNT/A
-
 Clostridium botulinum
botulinum neurotoxin A protease
-
 Clostridium botulinum

Ki Value [mM]

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