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Literature summary for 3.4.22.68 extracted from
- Comparative study of the insoluble and soluble Ulp1 protease constructs as carrier free and dependent protein immobilizates (2019), J. Biosci. Bioeng., 127, 23-29 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | comparison of Ulp1 protease in active upon expression as inclusion bodies and soluble protein. Fusion of the N-terminal selfassembling peptide GFIL8 to Ulp1 increases production of active inclusion bodies in Escherichia coli. Attachment of the N-terminal cellulose-binding module facilitates the immobilization on regenerated amorphous cellulose with a binding capacity up to about 235 mg protein per gram of cellulose. The immobilized soluble Ulp1 maintains about 42% initial cleavage activity with repetitive use, whereas the aggregated Ulp1 loses its cleavage capacity after cleaving the protein substrate once. Crosslinking of inclusion bodies using glutaraldehyde inactivates Ulp1 | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
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Release 2023.1 (January 2023)
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