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Literature summary for 3.4.21.62 extracted from
- Surface charge engineering of a Bacillus gibsonii subtilisin protease (2013), Appl. Microbiol. Biotechnol., 97, 6793-6802.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104, subcloning in Escherichia coli strain DH5alpha | Alkalihalobacillus gibsonii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | mimicking surface deamidation by substituting Gln by Glu and/or Asn by Asp might be a simple and fast protein reengineering approach for modulating enzyme properties such as activity, pH optimum, and thermal resistance, deamidation in five (N97, N253, Q37, Q200, and Q256) out of eight (N97, N154, N250, N253, Q37, Q107, Q200, and Q256) amino acids, comparison of wild-type and mutant enzymes, overview | Alkalihalobacillus gibsonii |
| N115D | site-directed mutagenesis, inactive mutant | Alkalihalobacillus gibsonii |
| N154D | site-directed mutagenesis, the mutant has 107% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N167D | site-directed mutagenesis, the mutant has 77% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N205D | site-directed mutagenesis, the mutant has 113% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N236D | site-directed mutagenesis, the mutant has 115% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N242D | site-directed mutagenesis, the mutant has 118% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N250D | site-directed mutagenesis, the mutant has 113% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N253D | site-directed mutagenesis, the mutant has 135% proteolytc activity compared to the wild-type enzyme and shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10 | Alkalihalobacillus gibsonii |
| N253D/Q256E | site-directed mutagenesis, the mutant shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10, the mutant has a 2fold increased activity compared to the wild-type enzyme with a thermal resistance increased by 2.4°C at pH 8.5 | Alkalihalobacillus gibsonii |
| N60D | site-directed mutagenesis, the mutant has 32% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| N97D | site-directed mutagenesis, the mutant has 146% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q107E | site-directed mutagenesis, the mutant has 53% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q12E | site-directed mutagenesis, the mutant has 114% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q176E | site-directed mutagenesis, the mutant has 97% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q185E | site-directed mutagenesis, inactive mutant | Alkalihalobacillus gibsonii |
| Q200E | site-directed mutagenesis, the mutant has 125% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q230E | site-directed mutagenesis, the mutant has 107% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
| Q256E | site-directed mutagenesis, the mutant has 129% proteolytc activity compared to the wild-type enzyme and shows a dramatic pH activity profiles shifted towards higher activity at lower pH range of pH 8.5-10 | Alkalihalobacillus gibsonii |
| Q37E | site-directed mutagenesis, the mutant has 136% proteolytc activity compared to the wild-type enzyme | Alkalihalobacillus gibsonii |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27000 | - |
x * 27000, recombinant enzyme, SDS-PAGE | Alkalihalobacillus gibsonii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alkalihalobacillus gibsonii | GN111900.1 | - |
- |
| Alkalihalobacillus gibsonii DSM 14391 | GN111900.1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Bacillus subtilis strain DB104 by dialysis and anion and cation exchange chromatography | Alkalihalobacillus gibsonii |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 27000, recombinant enzyme, SDS-PAGE | Alkalihalobacillus gibsonii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bacillus gibsonii alkaline protease | - |
Alkalihalobacillus gibsonii |
| BgAP | - |
Alkalihalobacillus gibsonii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Alkalihalobacillus gibsonii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability profiles of purified wild-type enzyme, and mutants N253D, Q256E, and N253D/Q256E, overview | Alkalihalobacillus gibsonii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.6 | - |
- |
Alkalihalobacillus gibsonii |
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