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Information on EC 3.4.24.68 - tentoxilysin
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EC Tree
3.4.24.68 tentoxilysinSpecify your search results
Word Map
- 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
-
postsynaptic
- paralysis
- vamp
- motoneuron
-
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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
Synonyms
tetanus toxin, tetanus neurotoxin, tetanospasmin, tent-hc, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TeNT
Tentoxylysin
-
-
-
-
Tetanus neurotoxin
tetanus toxin
TeNT
-
-
Tetanus neurotoxin
-
-
-
-
Tetanus neurotoxin
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
structure and mechanism
-
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
structure and mechanism
-
-
Hydrolysis of -Gln76-/-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP)
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
107231-12-9
-
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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
?
-
catalytic activity of all mutants
-
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
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
-
-
?
synaptobrevin + H2O
?
-
i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol
-
-
?
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
-
-
?
synaptobrevin + H2O
?
-
neurotoxin blocks neurotransmitter release in Aplysia neurons
-
-
?
synaptobrevin + H2O
?
-
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
-
-
?
synaptobrevin + H2O
?
-
a host nerve cell SNARE protein, purified recombinant His-tagged synaptobrevin expressed in Escherichia coli
-
-
?
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
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
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
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
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
-
-
?
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2
-
-
?
synaptobrevin-2 + H2O
?
-
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
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
L-chain highly specific for the substrate
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
L-chain highly specific for the substrate
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin
-
-
?
additional information
?
-
-
most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity
-
?
additional information
?
-
-
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
synaptobrevin-1 (with Val76 instead of Gln76) or short peptides containing the cleavage site of the target protein
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
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NATURAL SUBSTRATE
NATURAL 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
synaptobrevin-2 + H2O
?
-
i.e. vesicle associated membrane protein-2, VAMP-2
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
neuronal SNARE protein, i.e. VAMP2
-
-
?
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
-
-
?
synaptobrevin + H2O
?
-
i.e. VAMP, neuronal vesicle-associated membrane protein, predominantly exposed to cytosol
-
-
?
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
-
-
?
synaptobrevin + H2O
?
-
neurotoxin blocks neurotransmitter release in Aplysia neurons
-
-
?
synaptobrevin + H2O
?
-
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
-
-
?
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
-
-
?
vesicle associated membrane protein + H2O
?
-
-
-
-
?
additional information
?
-
-
most powerful known natural toxin, 2 carbohdrate binding sites in the Hcc-domain of tetanus neurotoxin are required for toxicity
-
?
additional information
?
-
-
most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
most powerful known natural toxin
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
Zn2+
Zinc
-
1 atom zinc per molecule toxin, zinc-binding motif: His-Glu-X-X-His, nickel or cobalt can replace zinc
Zinc
-
L-chain: form of zinc-endopeptidase, 0.8-1 gatom zinc/mol toxin, bound to light or L-chain
Zn2+
crystal structure provides insight into the role of the zinc ion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ala-Ser-Gln-Phe-Glu-Thr-Ser
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica
Gln-Phe-Glu-Thr
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica
additional information
-
enzyme inhibition by a cleavage site-specific antibody, overview
-
additional information
-
design, random selection, and recombinant production from phagemid in Escherichia coli of human single chain antibody fragments that inhibit tetanus toxin binding to retinoic acid pulsed human neuroblastoma cells and TeNT protease activity completely, overview
-
additional information
-
geldanamycin efficiently blocks the neurotoxic activity of the enzyme. The interchain disulfide of the enzyme can be specifically reduced by incubating the enzyme with NADPH, thioredoxin and thioredoxin reductase. Reduced enzyme is not toxic
-
additional information
-
not inhibited by botulinum antitoxin types A, C, D, E and F
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Proteases
-
activation by rapid cleavage within an exposed loop of the single inactive MW 150000 polypeptide chain and generation of active di-chain neurotoxin
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
additional information
-
quantitative immunoaffinity assay method development and evaluation, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
all toxigenic strains synthesize only one type of neurotoxin
-
-
brenda
tetanus toxin is encoded on a 74082 kb plasmid containing 61 genes
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
effect of medium composition on the production of tetanus toxin. The highest final average yield of tetanus toxin is obtained at 9.7 mg/ml starting level of glucose and 43.5 g/l N-T Case TT as carbon and nitrogen source
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
TeNT cleaves vesicle-associated membrane protein-2, thereby inhibiting neurotransmitter release in the central nervous system to elicit spastic paralysis
metabolism
-
the enzyme cleaves a neuronal soluble N-ethylmaleimide-sensitive attachment receptor protein, leading to the blockade of inhibitory neurotransmitter release and subsequent generalized muscular spasm
physiological function
physiological function
-
cleavage of synaptobrevin results in inhibition of release of neurotransmitters glycine and gamma-amino butyric acid from inhibitory interneurons causing spastic paralysis
physiological function
-
the enzyme is the most important virulence factor that plays a key role in the pathogenicity of tetanus
physiological function
-
the enzyme undergoes binding to specific components of the basal membrane at the neuromuscular junction, is endocytosed into motor neurons and sorted to axonal signaling endosomes. Following this, the enzyme is transported to the soma of motor neurons located in the spinal cord or brainstem, and then transcytosed to inhibitory interneurons, where it blocks synaptic transmission. Enzyme-induced impairment of inhibitory input leads to hyperactivity of motor neurons, causing spastic paralysis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TETX_CLOTE
Clostridium tetani (strain Massachusetts / E88)
1315
0
150682
Swiss-Prot
-
B0ELZ9_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
1454
0
168911
TrEMBL
other Location (Reliability: 1)
A0A381FRC7_9FLAO
1000
0
106982
TrEMBL
-
G0QYH3_ICHMG
Ichthyophthirius multifiliis (strain G5)
2104
0
247373
TrEMBL
other Location (Reliability: 1)
B0ELU4_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
745
0
85687
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM