EC Number |
Reference |
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3.4.22.8 | clostripain gene is modified and its signal sequence is replaced with that of penicillin G acylase. The core clostripain protein fused to the penicillin G acylase signal peptide is also prepared. With regard to the expression of the clostripain precursors, the majority of clostripain activity is observed in the culture media, thereby indicating that both the clostripain signal peptide and the penicillin G acylase signal peptide are recognized in the Escherichia coli secretion pathway, and the precursors successfully mature into the active form. The activity is rather low when the core protein is expressed, which indicates that the clostripain pro-peptide is important in the formation of the active enzyme in Escherichia coli |
687876 |
3.4.22.8 | expressed in Clostridium perfringens strains 13 and 13DELTA6 |
718358 |
3.4.22.8 | expression in Bacillus subtilis, the Clostridium histolyticum signal peptide is efficiently recognized by the Bacillus subtilis secretion apparatus |
81594 |
3.4.22.8 | expression in Escherichia coli |
81590, 81594 |
3.4.22.8 | overexpressed in Clostridium perfringens strain 13 |
709851 |
3.4.22.8 | the enzyme is not transported to the Escherichia coli periplasm |
81594 |
3.4.22.8 | wild-type and mutant enzyme H176A expressed in Escherichia coli |
651178 |