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Literature summary extracted from

  • Schiavo, G.; Montecucco, C.
    Tetanus and botulism neurotoxins: isolation and assay (1995), Methods Enzymol., 248, 643-652.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.68 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
3.4.24.68 Proteases bacterial Clostridium tetani
3.4.24.69 Proteases activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin Clostridium sp.
3.4.24.69 Proteases activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin Clostridium botulinum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.68 NaOCl inactivation Clostridium tetani

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.68 cytosol accumulates until bacterial lysis Clostridium tetani 5829
-
3.4.24.69 cytosol accumulates until bacterial lysis Clostridium sp. 5829
-
3.4.24.69 cytosol accumulates until bacterial lysis Clostridium botulinum 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.68 Zinc zinc-dependent endoproteinase Clostridium tetani
3.4.24.68 Zinc L-chain: form of zinc-endopeptidase, 0.8-1 gatom zinc/mol toxin, bound to light or L-chain Clostridium tetani
3.4.24.69 Zinc the L-chain of BoNT/B is a form of zinc-endopeptidase Clostridium sp.
3.4.24.69 Zinc the L-chain of BoNT/B is a form of zinc-endopeptidase Clostridium botulinum
3.4.24.69 Zinc 0.8-1 gatom zinc/mol neurotoxin Clostridium sp.
3.4.24.69 Zinc 0.8-1 gatom zinc/mol neurotoxin Clostridium botulinum
3.4.24.69 Zinc zinc-dependent endopeptidase (serotype BoNT/B) Clostridium sp.
3.4.24.69 Zinc zinc-dependent endopeptidase (serotype BoNT/B) Clostridium botulinum
3.4.24.69 Zinc atom absorption spectroscopy Clostridium sp.
3.4.24.69 Zinc atom absorption spectroscopy Clostridium botulinum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.68 150700
-
 Clostridium tetani, calculated from amino acid sequence Clostridium tetani

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.68 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 ?
-
 ?
3.4.24.68 synaptobrevin + H2O Clostridium tetani Harvard 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 ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium sp. neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium botulinum neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium sp. causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium botulinum causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding ?
-
 ?
3.4.24.69 synaptobrevin + H2O Clostridium sp. i.e. VAMP ?
-
 ?
3.4.24.69 synaptobrevin + H2O Clostridium botulinum i.e. VAMP ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.68 Clostridium tetani
-
 all toxigenic strains synthesize only one type of neurotoxin
-
3.4.24.68 Clostridium tetani
-
 Harvard
-
3.4.24.68 Clostridium tetani Harvard
-
 Harvard
-
3.4.24.69 Clostridium botulinum
-
 7 serologically different neurotoxin types: BoNT/A-G
-
3.4.24.69 Clostridium sp.
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.4.24.68 extremely sensitive to oxidants Clostridium tetani
3.4.24.69 extremely sensitive to oxidants Clostridium botulinum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.68 single-chain, two-chain and L-chain form Clostridium tetani
3.4.24.68 very toxic! Booster injection of tetanus toxoid before starting research with tetanus toxin advisable, human anti-tetanus neurotoxin antibodies available Clostridium tetani
3.4.24.69 serotypes BoNT/A, B, E, C, D, F Clostridium botulinum

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.68 culture supernatant
-
 Clostridium tetani
-

Storage Stability

EC Number Storage Stability Organism
3.4.24.68 -80°C, in 10 mM HEPES buffer, pH 7.2, 50 mM NaCl, after freezing in liquid N2, stable Clostridium tetani
3.4.24.69 -80°C, in 10 mM HEPES buffer, pH 7.2, 50 mM NaCl, after freezing in liquid N2, stable Clostridium botulinum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.68 additional information synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein Clostridium tetani ?
-
 ?
3.4.24.68 additional information synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein Clostridium tetani Harvard ?
-
 ?
3.4.24.68 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
-
 ?
3.4.24.68 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 Harvard Hydrolyzed synaptobrevin
-
 ?
3.4.24.68 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 ?
-
 ?
3.4.24.68 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 Harvard ?
-
 ?
3.4.24.69 additional information no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins Clostridium sp. ?
-
 ?
3.4.24.69 additional information no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins Clostridium botulinum ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature Clostridium sp. ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature Clostridium botulinum ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding Clostridium sp. ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding Clostridium botulinum ?
-
 ?
3.4.24.69 Proteins of neuroexocytosis apparatus + H2O
-
 Clostridium sp. ?
-
 ?
3.4.24.69 Proteins of neuroexocytosis apparatus + H2O
-
 Clostridium botulinum ?
-
 ?
3.4.24.69 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 sp. Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 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 botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes BoNT/B Clostridium sp. Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes BoNT/B Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes D, F or G Clostridium sp. Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes D, F or G Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying synaptobrevin/VAMP-2 Clostridium sp. Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying synaptobrevin/VAMP-2 Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O highly specific neurotoxins Clostridium sp. Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O highly specific neurotoxins Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 synaptobrevin + H2O i.e. VAMP Clostridium sp. ?
-
 ?
3.4.24.69 synaptobrevin + H2O i.e. VAMP Clostridium botulinum ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A and E Clostridium sp. Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A and E Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Syntaxin + H2O serotype BoNT/C Clostridium sp. ?
-
 ?
3.4.24.69 Syntaxin + H2O serotype BoNT/C Clostridium botulinum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.69 More synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds Clostridium sp.
3.4.24.69 More synthesized as single-chain polypeptide of about MW 150000 Da, proteolytic activation yields 2-chain neurotoxin with N-terminal light (MW 50000 Da) and C-terminal heavy chains (MW 100000 Da) connected by single disulfide bonds Clostridium botulinum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.68 37
-
 assay at Clostridium tetani
3.4.24.69 37
-
 assay at Clostridium sp.
3.4.24.69 37
-
 assay at Clostridium botulinum