Literature summary for 3.2.1.1 extracted from

Priyadharshini, R.; Manoharan, S.; Hemalatha, D.; Gunasekaran, P.
Repeated random mutagenesis of alpha-amylase from Bacillus licheniformis for improved pH performance (2010), J. Microbiol. Biotechnol., 20, 1696-1701.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Bacillus licheniformis

Protein Variants

Protein Variants	Comment	Organism
I157S/W193R	random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme	Bacillus licheniformis
additional information	repeated cycles of random mutagenesis of a region comprising residues from the position 34-281, mutant library construction. Mutant TP8H5 shows an altered pH profile as compared to the wild-type. The sequencing of variant TP8H5 indicated 2 amino acid changes, Ile157Ser and Trp193Arg, which are located in the solvent accessible flexible loop region in domain B	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-
Bacillus licheniformis MTCC 6598	-	-	-

Synonyms

Synonyms	Comment	Organism
AmyL	-	Bacillus licheniformis

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	wild-type and mutant I157S/W193R enzymes	Bacillus licheniformis

pH Range

pH Minimum	pH Maximum	Comment	Organism
3	10	activity range, mutant I157S/W193R enzyme	Bacillus licheniformis
4	10	activity range, wild-type enzyme	Bacillus licheniformis

General Information

General Information	Comment	Organism
physiological function	alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose	Bacillus licheniformis

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Release 2023.1 (January 2023)