Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli BL21 (DE3) cells | Pullulanibacillus naganoensis |
Protein Variants | Comment | Organism |
---|---|---|
D787C | higher enzymatic activity than that of wild-type enzyme | Pullulanibacillus naganoensis |
D787C | the enzymatic activity and specific activity of D787C are 1.5fold higher than those of the wild-type. The enzyme shows a 1.8fold increase in kcat and a 1.7-fold increase in kcat/Km. It maintains higher activity compared with that of wild-type enzyme at temperatures over 60°C. Higher acid resistance than wild-type enzyme, maintaining 90% residual activity at pH 4.0 | Pullulanibacillus naganoensis |
D787F | higher enzymatic activity than that of wild-type enzyme | Pullulanibacillus naganoensis |
D787N | higher enzymatic activity than that of wild-type enzyme | Pullulanibacillus naganoensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pullulanibacillus naganoensis | G9JLV4 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pullulanibacillus naganoensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pullulan + H2O | - |
Pullulanibacillus naganoensis | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
pullulan | pH 4.5, 60°C, kcat of wild-type enzyme and mutant enzyme | Pullulanibacillus naganoensis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
pullulan | pH 4.5, 60°C, kcat/Km of wild-type enzyme and mutant enzyme | Pullulanibacillus naganoensis |