Literature summary for 3.4.24.69 extracted from

Agarwal, R.; Eswaramoorthy, S.; Kumaran, D.; Dunn, J.J.; Swaminathan, S.
Cloning, high level expression, purification, and crystallization of the full length Clostridium botulinum neurotoxin type E light chain (2004), Protein Expr. Purif., 34, 95-102.

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Cloned(Commentary)

Cloned (Comment)	Organism
full length Clostridium botulinum neurotoxin type E light chain, expression in Escherichia coli	Clostridium botulinum

Crystallization (Commentary)

Crystallization (Comment)	Organism
full length Clostridium botulinum neurotoxin type E light chain, sitting drop vapor diffusion method, crystals diffract to better than 2.1 A, crystals belong to space group P2(1)2(1)2 with cell dimensions a = 88.33 A, b = 144.45 A, c = 83.37 A	Clostridium botulinum

General Stability

General Stability	Organism
stable in many freeze and thawing processes	Clostridium botulinum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
37.5	-	synaptosome-associated protein SNAP-25	37°C, pH 7.4	Clostridium botulinum

Organism

Organism	UniProt	Comment	Textmining
Clostridium botulinum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
full length Clostridium botulinum neurotoxin type E light chain	Clostridium botulinum

Storage Stability

Storage Stability	Organism
-20°C, HEPES buffer, 10-20% glycerol, stable	Clostridium botulinum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
synaptosome-associated protein SNAP-25 + H2O	-	Clostridium botulinum	?	-	?

Synonyms

Synonyms	Comment	Organism
Clostridium botulinum neurotoxin type E	-	Clostridium botulinum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
11.1	-	synaptosome-associated protein SNAP-25	37°C, pH 7.4	Clostridium botulinum

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Release 2023.1 (January 2023)