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Literature summary extracted from

  • Haghani, K.; Khajeh, K.; Naderi-Manesh, H.; Ranjbar, B.
    Investigation on the effects of three X->histidine replacements on thermostability of alpha-amylase from Bacillus amyloliquefaciens (2012), J. Microbiol. Biotechnol., 22, 592-599.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 I34H mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity Bacillus amyloliquefaciens
3.2.1.1 P407H mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type Bacillus amyloliquefaciens
3.2.1.1 Q67H mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type Bacillus amyloliquefaciens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 58000
-
 x * 58000, SDS-PAGE Bacillus amyloliquefaciens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus amyloliquefaciens
-
-
-
3.2.1.1 Bacillus amyloliquefaciens ATCC 23350
-
-
-

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 58000, SDS-PAGE Bacillus amyloliquefaciens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 70
-
 wild-type, 75% of initial activity after 80 min, mutant Q67H after 185 min, and mutant P407H 125 min of incubation, respectively Bacillus amyloliquefaciens
3.2.1.1 75
-
 wild-type, half-life 125 min, mutant Q67H, 145 min, and mutant P407H, 185 min Bacillus amyloliquefaciens