Literature summary for 3.2.1.1 extracted from

Ghalanbor, Z.; Ghaemi, N.; Marashi, S.A.; Amanlou, M.; Habibi-Rezaei, M.; Khajeh, K.; Ranjbar, B.
Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity (2008), Protein Pept. Lett., 15, 212-214.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Tris	starch-hydrolyzing activity in presence of Tris of different concentrations, pH 7.4, 37°C	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	P06278	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
starch + H2O	soluble starch, 2000000 Dalton, only soluble at temperatures close to 100°C, in phosphate buffer, pH 7.4, assay at 37°C	Bacillus licheniformis	?	-	?

Synonyms

Synonyms	Comment	Organism
Bacillus licheniformis alpha-amylase	-	Bacillus licheniformis
BLA	-	Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Bacillus licheniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C	Bacillus licheniformis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Bacillus licheniformis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
13	-	Tris	determined with Lineweaver-Burk plot, competitive inhibition, pH 7.4, 37°C, docking simulations show that Tris binds deep inside the active site of the enzyme	Bacillus licheniformis

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Release 2023.1 (January 2023)