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Literature summary for 3.2.1.1 extracted from

  • Wang, C.; Huang, R.; He, B.; Du, Q.
    Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (2012), BMC Bioinformatics, 13, 263.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
H100I increase in half-inactivation temperature, kcat value similar to wild-type Bacillus subtilis
H100M/D144R increase in half-inactivation temperature, 70% decrease in kcat value Bacillus subtilis
additional information improvement of the thermal stability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis (CCSM), in which the functionally correlated variation sites of proteins are chosen as the hotspot sites to construct focused mutant libraries. Method leads to identification of beneficial mutation sites, and enhances the thermal stability of wild-type alpha-amylase Amy7C by 8°C Bacillus subtilis
N197C decrease in half-inactivation temperature, kcat value similar to wild-type Bacillus subtilis
T147P increase in half-inactivation temperature, 25% decrease in kcat value Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis H9B4I9
-
-
Bacillus subtilis CN7 H9B4I9
-
-

Synonyms

Synonyms Comment Organism
Amy7C
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
58.3
-
mutant N197C, half inactivation Bacillus subtilis
62.3
-
wild-type, half inactivation Bacillus subtilis
66.8
-
mutant H100I, half inactivation Bacillus subtilis
69.3
-
mutant T147P, half inactivation Bacillus subtilis
70.3
-
mutant H100M/D144R, half inactivation Bacillus subtilis