Literature summary for 3.4.24.69 extracted from

Chen, R.; Shi, J.; Cai, K.; Tu, W.; Hou, X.; Liu, H.; Xiao, L.; Wang, Q.; Tang, Y.; Wang, H.
Improved soluble expression and characterization of the Hc domain of Clostridium botulinum neurotoxin serotype A in Escherichia coli by using a PCR-synthesized gene and a Trx co-expression strain (2010), Protein Expr. Purif., 71, 79-84.

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Cloned(Commentary)

Cloned (Comment)	Organism
cloning of the gene encoding the BoNT/A heavy chain as 1275 bp AHc fragment synthesized by PCR, and overexpression as His6-tagged protein in Escherichia coli	Clostridium botulinum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Clostridium botulinum	ganglioside GT1b is considered as BoNT/A receptor at nerve cells and can bind to the C-terminal end of the heavy chain	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium botulinum	P10845	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged BoNT/A heavy chain fragment from Escherichia coli by nickel affinity chromatography	Clostridium botulinum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	ganglioside GT1b is considered as BoNT/A receptor at nerve cells and can bind to the C-terminal end of the heavy chain	Clostridium botulinum	?	-	?

Synonyms

Synonyms	Comment	Organism
BoNT/A	-	Clostridium botulinum
Clostridium botulinum neurotoxin serotype A	-	Clostridium botulinum

General Information

General Information	Comment	Organism
physiological function	BoNT/A is an extremely potent bacterial protein toxin. The Hc fragment of BoNT/A is non-toxic, antigenic, and capable of eliciting a protective immunity in animals challenged with homologous BoNT	Clostridium botulinum

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Release 2023.1 (January 2023)