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Literature summary for 3.2.1.2 extracted from

  • Yamashiro, K.; Yokobori, S.; Koikeda, S.; Yamagishi, A.
    Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method (2010), Protein Eng. Des. Sel., 23, 519-528.
    View publication on PubMed
Search for more literature for 3.2.1.2

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis, expression of wild-type and mutant enzymes in Escherichia coli Rosetta2 cells, subcloning in strain JM109 Niallia circulans

Protein Variants

Protein Variants Comment Organism
D170Q/L172F/Y173L site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
G48A/A51E site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
I74V site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
L135V site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
L172F/Y173L site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
L172F/Y173L/A174E site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
additional information construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method Niallia circulans
R118Q site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
R311P/I312L site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
R311P/I312L/S317A site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
S133N/L135V site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Niallia circulans
S137T/K138A site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
S317A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Niallia circulans
T116M site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
T116M/R118Q site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
T76V site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
T98K/Y99L/A100V/D101E site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
Y72D site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
Y72D/I74V/T76V site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans P06547
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Niallia circulans NCIMB 11033 P06547
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Subunits

Subunits Comment Organism
More three-dimensional structure modelling, overview Niallia circulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 assay at Niallia circulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 half-life of the wild-type enzyme is 6.4 min Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Niallia circulans