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Literature summary for 3.2.1.1 extracted from

  • Lin, L.L.; Chen, P.J.; Liu, J.S.; Wang, W.C.; Lo, H.F.
    Identification of glutamate residues important for catalytic activity or thermostability of a truncated Bacillus sp. strain TS-23 alpha-amylase by site-directed mutagenesis (2006), Protein J., 25, 232-239.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
N- and C-terminally truncated alpha-amylase and Ala- and Asp-substituted variants are overexpressed in the recombinant Escherichia coli cells Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants Comment Organism
E151A mutant of N- and C-terminally truncated alpha-amylase, specific activity for E151A is decreased by more than 30% Bacillus sp. (in: Bacteria)
E219 mutant of N- and C-terminally truncated alpha-amylase, decreased half-life at 70°C Bacillus sp. (in: Bacteria)
E295A mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity Bacillus sp. (in: Bacteria)
E295D mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) TS-23
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ala- and Asp-substituted variants overexpressed in recombinant Escherichia coli cells Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
soluble starch + H2O
-
 Bacillus sp. (in: Bacteria) ?
-
 ?
soluble starch + H2O
-
 Bacillus sp. (in: Bacteria) TS-23 ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 t1/2 of N- and C-terminally truncated alpha-amylase is 14 min, t1/2 of the E219A mutant and the E219D mutant of N- and C-terminally truncated alpha-amylase is 5 min Bacillus sp. (in: Bacteria)