Any feedback?
Literature summary for 3.4.21.62 extracted from
- Cloning, expression and decoding of the cold adaptation of a new widely represented thermolabile subtilisin-like protease (2013), J. Appl. Microbiol., 114, 352-363.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis | Euphausia superba |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Euphausia superba | - |
collected at Base Frei Montalva, King George Island, Chilean Antarctic | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Euphausia superba | succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| subtilisin-like protease | - |
Euphausia superba |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Euphausia superba |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure homology modeling, structure comparisons, overview | Euphausia superba |
| physiological function | a cold-adapted protease, residue Ala284 is an important cold-adaptation determinant of the enzyme | Euphausia superba |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
