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Literature summary for 3.4.21.62 extracted from
- Improved catalytic efficiency of a monomeric gamma-glutamyl transpeptidase from Bacillus licheniformis in presence of subtilisin (2010), Biotechnol. Lett., 32, 1137-1141.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | subtilisin-30 kDa gamma-glutamyl transpeptidase complex exhibits better catalytic properties and can be exploited in various biotechnological applications | synthetic construct |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| synthetic construct | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 67 kDa gamma-glutamyl transpeptidase + H2O | proteolytic digestion of 67 kDa gamma-glutamyl transpeptidase from Bacillus licheniformis ER-15 by subtilisin to the 30 kDa form, which in turn remains associated with subtilisin as a heterodimeric protein | synthetic construct | 30 kDa gamma-glutamyl transpeptidase + ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| subtilisin | - |
synthetic construct |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | subtilisin enhances transpeptidase activity of 67 kDa gamma-glutamyl transpeptidase and 30 kDa gamma-glutamyl transpeptidase, by nearly 1.5- and 2fold, respectively. In presence of subtilisin, 30 kDa gamma-glutamyl transpeptidase has improved catalytic efficiency, altered pH and temperature optima and has salt-tolerant glutaminase activity | synthetic construct |
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