Application | Comment | Organism |
---|---|---|
synthesis | recombinant expression of enzyme as insoluble inclusion bodies, solubilization in 6 M guanidine-HCl in presence of reducing agent and renaturation by fast frequent dilution method. Highest yield of refolded protein at pH 8.4, 4°C. Renaturation is accompanied by gradual splitting of K12-E13 and T47-E48 bonds resulting in a 26 kDa protein that is converted to 25 kDa mature protein by limited proteolysis trypsin or subtilisin. Complete cleavage of N-terminal pro-peptide is necessary for final packing and activation of enzyme | Bacillus licheniformis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | recombinant expression as insoluble inclusion bodies | Bacillus licheniformis | 5737 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
recombinant enzyme | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | proteolytic modification of native precursor results in a 25 kDa protein. Recombinant expression of enzyme in Escherichia coli with subsequent renaturation of inclusion bodies results in a 26 kDa protein that is converted to 25 kDa mature protein by limited proteolysis trypsin or subtilisin. Clomplete cleavage of N-terminal pro-peptide is necessary for final packing and activation of enzyme | Bacillus licheniformis |
Renatured (Comment) | Organism |
---|---|
recombinant expression of enzyme as insoluble inclusion bodies, solubilization in 6 M guanidine-HCl in presence of reducing agent and renaturation by fast frequent dilution method. Highest yield of refolded protein at pH 8.4, 4°C. Renaturation is accompanied by gradual splitting of K12-E13 and T47-E48 bonds resulting in a 26 kDa protein | Bacillus licheniformis |