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Literature summary 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

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 or tissue proteases 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 butyricum
3.4.24.69 Proteases activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin Clostridium botulinum
3.4.24.69 Proteases activation by rapid cleavage of MW 150000 polypeptide chain and generation of active di-chain neurotoxin Clostridium baratii
3.4.24.69 Proteases bacterial or tissue proteases Clostridium butyricum
3.4.24.69 Proteases bacterial or tissue proteases Clostridium botulinum
3.4.24.69 Proteases bacterial or tissue proteases Clostridium baratii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.68 captopril
-
 Clostridium tetani
3.4.24.69 captopril
-
 Clostridium baratii
3.4.24.69 captopril
-
 Clostridium botulinum
3.4.24.69 captopril
-
 Clostridium butyricum

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 butyricum 5829
-
3.4.24.69 cytosol accumulates until bacterial lysis Clostridium botulinum 5829
-
3.4.24.69 cytosol accumulates until bacterial lysis Clostridium baratii 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.68 Cobalt zinc-dependent endoproteinase, can replace zinc Clostridium tetani
3.4.24.68 Nickel zinc-dependent endoproteinase, can replace zinc Clostridium tetani
3.4.24.68 Zinc zinc-dependent endoproteinase Clostridium tetani
3.4.24.68 Zinc 1 atom zinc per molecule toxin, zinc-binding motif: His-Glu-X-X-His, nickel or cobalt can replace zinc Clostridium tetani
3.4.24.69 Zinc contains zinc binding motif of metalloendopeptidases His-Glu-X-X-His Clostridium butyricum
3.4.24.69 Zinc contains zinc binding motif of metalloendopeptidases His-Glu-X-X-His Clostridium botulinum
3.4.24.69 Zinc contains zinc binding motif of metalloendopeptidases His-Glu-X-X-His Clostridium baratii
3.4.24.69 Zinc atom absorption spectroscopy Clostridium butyricum
3.4.24.69 Zinc atom absorption spectroscopy Clostridium botulinum
3.4.24.69 Zinc atom absorption spectroscopy Clostridium baratii
3.4.24.69 Zinc 1 atom of zinc per molecule botulinum neurotoxin, bound to light chain (i.e. L-chain) Clostridium butyricum
3.4.24.69 Zinc 1 atom of zinc per molecule botulinum neurotoxin, bound to light chain (i.e. L-chain) Clostridium botulinum
3.4.24.69 Zinc 1 atom of zinc per molecule botulinum neurotoxin, bound to light chain (i.e. L-chain) Clostridium baratii

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 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 ?
-
 ?
3.4.24.68 synaptobrevin + H2O Clostridium tetani i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol ?
-
 ?
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 ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium butyricum 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 baratii 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 butyricum involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium botulinum involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium baratii involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O Clostridium butyricum 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 Neuroexocytosis multi-subunit complex + H2O Clostridium baratii 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 butyricum i.e. VAMP ?
-
 ?
3.4.24.69 synaptobrevin + H2O Clostridium botulinum i.e. VAMP ?
-
 ?
3.4.24.69 synaptobrevin + H2O Clostridium baratii i.e. VAMP ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O Clostridium butyricum i.e. SNAP 25, protein of presynaptic membrane ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O Clostridium botulinum i.e. SNAP 25, protein of presynaptic membrane ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O Clostridium baratii i.e. SNAP 25, protein of presynaptic membrane ?
-
 ?

Organism

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

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
3.4.24.69 Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates structure/function relationship Clostridium butyricum
a
3.4.24.69 Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates structure/function relationship Clostridium botulinum
a
3.4.24.69 Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates structure/function relationship Clostridium baratii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.68 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)

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 no substrates are rat or chicken Clostridium tetani ?
-
 ?
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 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 ?
-
 ?
3.4.24.68 synaptobrevin + H2O i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol 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 ?
-
 ?
3.4.24.69 additional information no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins Clostridium butyricum ?
-
 ?
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 additional information no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins Clostridium baratii ?
-
 ?
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 butyricum ?
-
 ?
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 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 baratii ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction Clostridium butyricum ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction Clostridium botulinum ?
-
 ?
3.4.24.69 Neuroexocytosis multi-subunit complex + H2O involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction Clostridium baratii ?
-
 ?
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 butyricum ?
-
 ?
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 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 baratii ?
-
 ?
3.4.24.69 Proteins of neuroexocytosis apparatus + H2O
-
 Clostridium butyricum ?
-
 ?
3.4.24.69 Proteins of neuroexocytosis apparatus + H2O
-
 Clostridium botulinum ?
-
 ?
3.4.24.69 Proteins of neuroexocytosis apparatus + H2O
-
 Clostridium baratii ?
-
 ?
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 butyricum 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 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 baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes BoNT/B Clostridium butyricum 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 BoNT/B Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Ala-+-Ala-Lys Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Ala-+-Ala-Lys Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Ala-+-Ala-Lys Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Gln-Lys-+-Leu-Ser Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Gln-Lys-+-Leu-Ser Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Gln-Lys-+-Leu-Ser Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O hydrolyzed by serotypes D, F or G Clostridium butyricum 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 hydrolyzed by serotypes D, F or G Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying synaptobrevin/VAMP-2 Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying synaptobrevin/VAMP-2 Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying synaptobrevin/VAMP-2 Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying Val76 instead of Gln76 is not hydrolyzed by serotype BoNT/B Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying Val76 instead of Gln76 is not hydrolyzed by serotype BoNT/B Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O carrying Val76 instead of Gln76 is not hydrolyzed by serotype BoNT/B Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O highly specific neurotoxins Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O highly specific neurotoxins Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O highly specific neurotoxins Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Gln-+-Phe-Glu (at the same site as the tetanus neurotoxin) Clostridium butyricum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Gln-+-Phe-Glu (at the same site as the tetanus neurotoxin) Clostridium botulinum Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 Synaptobrevin + H2O serotype BoNT/B: cleavage at Ser-Gln-+-Phe-Glu (at the same site as the tetanus neurotoxin) Clostridium baratii Hydrolyzed synaptobrevin
-
 ?
3.4.24.69 synaptobrevin + H2O i.e. VAMP Clostridium butyricum ?
-
 ?
3.4.24.69 synaptobrevin + H2O i.e. VAMP Clostridium botulinum ?
-
 ?
3.4.24.69 synaptobrevin + H2O i.e. VAMP Clostridium baratii ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A and E Clostridium butyricum 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 Synaptosome-associated protein + H2O serotype BoNT/A and E Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro, in isolated synaptosomes Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro, in isolated synaptosomes Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro, in isolated synaptosomes Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asn-Gln-+-Arg-Ala Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asn-Gln-+-Arg-Ala Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asn-Gln-+-Arg-Ala Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro and in injected Aplysia neurons Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro and in injected Aplysia neurons Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O in vitro and in injected Aplysia neurons Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asp-Arg-+-Ile-Met Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asp-Arg-+-Ile-Met Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O serotype BoNT/A: cleavage at Asp-Arg-+-Ile-Met Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O MW 25000 Clostridium butyricum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O MW 25000 Clostridium botulinum Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O MW 25000 Clostridium baratii Hydrolyzed synaptosome-associated protein
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium butyricum ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium botulinum ?
-
 ?
3.4.24.69 Synaptosome-associated protein + H2O i.e. SNAP 25, protein of presynaptic membrane Clostridium baratii ?
-
 ?
3.4.24.69 Syntaxin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium butyricum ?
-
 ?
3.4.24.69 Syntaxin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium botulinum ?
-
 ?
3.4.24.69 Syntaxin + H2O in vitro, in synaptosomes and in injected Aplysia neurons Clostridium baratii ?
-
 ?
3.4.24.69 Syntaxin + H2O serotype BoNT/C Clostridium butyricum ?
-
 ?
3.4.24.69 Syntaxin + H2O serotype BoNT/C Clostridium botulinum ?
-
 ?
3.4.24.69 Syntaxin + H2O serotype BoNT/C Clostridium baratii ?
-
 ?