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Literature summary for 3.4.22.68 extracted from
- Bioprocess optimization for the overproduction of catalytic domain of ubiquitin-like protease 1 (Ulp1) from S. cerevisiae in E. coli fed-batch culture (2019), Enzyme Microb. Technol., 120, 98-109 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | optimization of expression of the catalytic domain. Optimization of cultivation conditions at shake flask results in Ulp1 expression of 195 mg/l in TB medium. Ni-NTA affinity purification of Ulp1 using 0.1% Triton X-100, 0.01mM DTT, 0.02mM EDTA and 1% glycerol leads to a purity of about 95% with a recovery yield of 80% and specific activity of 398600 U/mg. The protease cleaves the SUMO tag even at 1:10,000 enzyme to substrate ratio The in vivo cleavage of SUMO tag via coexpression strategy also results in more than 80% cleavage of SUMO fusion protein | Saccharomyces cerevisiae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
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Release 2023.1 (January 2023)
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