Literature summary for 3.4.24.68 extracted from

Sutton, J.M.; Chow-Worn, O.; Spaven, L.; Silman, N.J.; Hallis, B.; Shone, C.C.
Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurones (2001), FEBS Lett., 493, 45-49.

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Protein Variants

Protein Variants	Comment	Organism
D1309A	site-directed mutagenesis	Clostridium tetani
D1309N	site-directed mutagenesis	Clostridium tetani
E1310A	site-directed mutagenesis	Clostridium tetani
E1310Q	site-directed mutagenesis	Clostridium tetani
F1305A	site-directed mutagenesis	Clostridium tetani
K1295A	site-directed mutagenesis	Clostridium tetani
K1297A	site-directed mutagenesis	Clostridium tetani
R1168A	site-directed mutagenesis	Clostridium tetani
R1168K	site-directed mutagenesis	Clostridium tetani
W1303A	site-directed mutagenesis	Clostridium tetani
Y1170A	site-directed mutagenesis	Clostridium tetani
Y1290F	site-directed mutagenesis	Clostridium tetani
Y1290K	site-directed mutagenesis	Clostridium tetani
Y1290S	site-directed mutagenesis	Clostridium tetani
Y1292K	site-directed mutagenesis	Clostridium tetani

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Clostridium tetani	most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium tetani	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
TeNT Hc fragment mutants	Clostridium tetani

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	most powerful known natural toxin, acts by blocking the release of glycine from inhibitory neurons within the spinal cords	Clostridium tetani	?	-	?

Synonyms

Synonyms	Comment	Organism
TeNT	-	Clostridium tetani
Tetanus neurotoxin	-	Clostridium tetani

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Release 2023.1 (January 2023)