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
-
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
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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.68 - tentoxilysin
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glycolipoprotein
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gangliosides are bound to the C-terminal receptor-binding domain via two carbohydrate-binding sites, termed the lactose-binding site or the W pocket, and the sialic acid-binding site or the R pocket, GM1a bound to the W pocket, and GD3 bound to the R pocket
proteolytic modification
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TeNT is produced as a 150-kDa protein that is cleaved to a di-chain protein, comprising an N-terminal light chain and a C-terminal heavy chain domain linked through a single disulfide bond