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Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 D170Q/L172F/Y173L site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 G48A/A51E site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 I74V site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
3.2.1.2 L135V site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 L172F/Y173L site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 L172F/Y173L/A174E site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 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
3.2.1.2 R118Q site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 R311P/I312L site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
3.2.1.2 R311P/I312L/S317A site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 S133N/L135V site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Niallia circulans
3.2.1.2 S137T/K138A site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 S317A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Niallia circulans
3.2.1.2 T116M site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 T116M/R118Q site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 T76V site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
3.2.1.2 T98K/Y99L/A100V/D101E site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans
3.2.1.2 Y72D site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme Niallia circulans
3.2.1.2 Y72D/I74V/T76V site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme Niallia circulans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Niallia circulans P06547
-
-
3.2.1.2 Niallia circulans NCIMB 11033 P06547
-
-

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 40
-
 assay at Niallia circulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 60
-
 half-life of the wild-type enzyme is 6.4 min Niallia circulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 7.5
-
 assay at Niallia circulans