3.4.24.68: tentoxilysin
This is an abbreviated version!
For detailed information about tentoxilysin, go to the full flat file.
Word Map on EC 3.4.24.68
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3.4.24.68
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synaptic
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botulinum
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toxoid
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nerve
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epitope
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neurotransmitter
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exocytosis
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spinal
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ganglioside
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tetany
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cord
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clostridial
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retrograde
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presynaptic
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synaptobrevin
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snare
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antitoxin
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epilepsy
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neuromuscular
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transmitter
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synapses
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diphtheria
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excitatory
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bonts
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vesicle-associated
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snap-25
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syntaxin
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postsynaptic
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paralysis
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vamp
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motoneuron
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synaptosomes
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gt1b
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booster
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n-ethylmaleimide-sensitive
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toxin-induced
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v-snares
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intrahippocampal
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transsynaptic
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phrenic
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neuroparalytic
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holotoxin
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k+-evoked
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neurospecific
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electrograph
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monosynaptic
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circumsporozoite
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synaptosome-associated
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medicine
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interictal
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3hnoradrenaline
- 3.4.24.68
- synaptic
- botulinum
- toxoid
- nerve
- epitope
-
neurotransmitter
-
exocytosis
- spinal
- ganglioside
- tetany
- cord
-
clostridial
-
retrograde
-
presynaptic
- synaptobrevin
- snare
- antitoxin
- epilepsy
- neuromuscular
-
transmitter
- synapses
- diphtheria
-
excitatory
-
bonts
-
vesicle-associated
- snap-25
- syntaxin
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postsynaptic
- paralysis
- vamp
- motoneuron
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synaptosomes
- gt1b
-
booster
-
n-ethylmaleimide-sensitive
-
toxin-induced
-
v-snares
-
intrahippocampal
-
transsynaptic
-
phrenic
-
neuroparalytic
-
holotoxin
-
k+-evoked
-
neurospecific
-
electrograph
-
monosynaptic
-
circumsporozoite
-
synaptosome-associated
- medicine
-
interictal
-
3hnoradrenaline
Reaction
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP) =
Synonyms
TeNT, TeNT-Hc, TeNT-LC protein, Tentoxylysin, tetanospasmin, Tetanus neurotoxin, tetanus toxin, TetX
ECTree
3.4.24.68 tentoxilysinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.68 - tentoxilysin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
rat synaptobrevin 2 + H2O
?
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catalytic activity of all mutants
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?
vesicle-associated membrane protein-2 + H2O
?
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neuronal SNARE protein, i.e. VAMP2
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-
?
synaptobrevin + H2O
?
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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
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-
?
synaptobrevin + H2O
?
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i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol
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-
?
synaptobrevin + H2O
?
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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
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-
?
synaptobrevin + H2O
?
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neurotoxin blocks neurotransmitter release in Aplysia neurons
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-
?
synaptobrevin + H2O
?
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TeNT is a zinc metalloprotease, that is produced by anaerobically grown Clostridium tetani in infected tissue, where it binds to ganglioside receptors of peripheral nerves. TeNT is then endocytosed. The A subunit exits from the endosome and undergoes retrograde transport via the nerve axon to the spinal cord of the host, where it specifically cleaves one of the nerve cell SNARE proteins, synaptobrevin
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-
?
synaptobrevin + H2O
?
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a host nerve cell SNARE protein, purified recombinant His-tagged synaptobrevin expressed in Escherichia coli
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-
?
synaptobrevin + H2O
?
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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
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-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
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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
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-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
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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
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-
?
synaptobrevin-2 + H2O
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i.e. vesicle associated membrane protein-2, VAMP-2
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?
synaptobrevin-2 + H2O
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i.e. vesicle associated membrane protein-2, VAMP-2, or Syb2, specific proteolytic cleavage, development of a sensitive in vitro assay method using immobilized recombinant substrate and a highly specific polyclonal antibody against the newly generated C-terminus of the product, overview
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?
vesicle associated membrane protein + H2O
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?
vesicle-associated membrane protein VAMP + H2O
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L-chain highly specific for the substrate
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?
vesicle-associated membrane protein VAMP + H2O
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L-chain highly specific for the substrate
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?
additional information
?
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synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
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?
additional information
?
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synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
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-
?
additional information
?
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catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin
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?
additional information
?
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most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity
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?
additional information
?
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most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords
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?
additional information
?
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tetanus neurotoxin is a potent inhibitor of neuroexocytosis. Organization and regulation of the neurotoxin gene. The gene located immediately upstream of the tetanus toxin gene, encodes a positive regulatory protein, TetR
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?
additional information
?
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TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview
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?
additional information
?
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the conformational changes of the C fragment of tetanus neurotoxin (TeNTHc) resulting from disulfide bond formation reduce the ganglioside-binding activity but do not destroy its immunogenicity as a potent vaccine candidate
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?
additional information
?
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synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
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?
additional information
?
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most powerful known natural toxin
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?
