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Literature summary for 3.4.24.68 extracted from

  • Montecucco, C.; Schiavo, G.
    Mechanism of action of tetanus and botulinum neurotoxins (1994), Mol. Microbiol., 13, 1-8.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Proteases activation by rapid cleavage within an exposed loop of the single inactive MW 150000 polypeptide chain and generation of active di-chain neurotoxin Clostridium tetani
Proteases or tissue proteases Clostridium tetani
Proteases bacterial Clostridium tetani

Inhibitors

Inhibitors Comment Organism Structure
captopril
-
Clostridium tetani

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol accumulates until bacterial lysis Clostridium tetani 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cobalt zinc-dependent endoproteinase, can replace zinc Clostridium tetani
Nickel zinc-dependent endoproteinase, can replace zinc Clostridium tetani
Zinc zinc-dependent endoproteinase Clostridium tetani
Zinc 1 atom zinc per molecule toxin, zinc-binding motif: His-Glu-X-X-His, nickel or cobalt can replace zinc Clostridium tetani

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
synaptobrevin + H2O Clostridium tetani tetanus neurotoxin receptors are located on the motor neuron plasmalemma at neuromuscular junction, after binding the toxin is internalized inside vesicles of unknown nature and then translocated across the vesicle membrane ?
-
?
synaptobrevin + H2O Clostridium tetani i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol ?
-
?
synaptobrevin + H2O Clostridium tetani enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known ?
-
?

Organism

Organism UniProt Comment Textmining
Clostridium tetani
-
all toxigenic strains synthesize only one type of neurotoxin
-

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP) structure and mechanism Clostridium tetani

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
in neurotoxin-injected Aplysia neurons 4-10 molecules of L-chains are sufficient to cause blockade of neurotransmitter release with a t1/2 of 20-40 min at 20°C Clostridium tetani

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein Clostridium tetani ?
-
?
additional information no substrates are rat or chicken Clostridium tetani ?
-
?
Synaptobrevin + H2O i.e. VAMP, neuronal vesicle-associated membrane protein, MW 19000, with 2 isoforms in human, chicken, in rat brain: synaptobrevin/VAMP-1 and synaptobrevin/VAMP-2, cleaves at Gln76-Phe77, the same site as botulin neurotoxin B Clostridium tetani Hydrolyzed synaptobrevin
-
?
synaptobrevin + H2O tetanus neurotoxin receptors are located on the motor neuron plasmalemma at neuromuscular junction, after binding the toxin is internalized inside vesicles of unknown nature and then translocated across the vesicle membrane Clostridium tetani ?
-
?
synaptobrevin + H2O i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol Clostridium tetani ?
-
?
synaptobrevin + H2O enzyme disables neuroexocytosis apparatus, acts at spinal inhibitory interneurons, blocking release of various neurotransmitters to produce spastic paralysis, clostridial neurotoxins are described as the most toxic substances known Clostridium tetani ?
-
?