Any feedback?
Literature summary extracted from
- Disulfide bridges as essential elements for the thermostability of lytic polysaccharide monooxygenase LPMO10C from Streptomyces coelicolor (2017), Protein Eng. Des. Sel., 30, 401-408.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.99.54 | A143C/P183C/S73C/A115C | introduction of two additional disulfide bridges, mutant displays a 12°C increase in melting temperature and is able to retain 60% of its activity after heat treatment | Streptomyces coelicolor |
| 1.14.99.54 | additional information | introduction of additional disulfide bridges. Four out of 16 variants display an improvement in melting temperature, ranging from 2°C to 9°C | Streptomyces coelicolor |
| 1.14.99.54 | S73C/A115C | introduction of an additional disulfide bridge, mutant displays a 9°C increase in melting temperature | Streptomyces coelicolor |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.99.54 | Streptomyces coelicolor | Q9RJY2 | - |
- |
| 1.14.99.54 | Streptomyces coelicolor ATCC BAA-471 | Q9RJY2 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.14.99.54 | additional information | when the three disulfide bridges of the protein are broken, irreversible unfolding occurs and no residual activity can be detected after a heat treatment at 80°C | Streptomyces coelicolor |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.99.54 | LPMO10C | - |
Streptomyces coelicolor |
| 1.14.99.54 | SCO1188 | - |
Streptomyces coelicolor |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.99.54 | 51 | - |
melting temperature, wild-type | Streptomyces coelicolor |
| 1.14.99.54 | 60 | - |
melting temperature, mutant S73C/A115C | Streptomyces coelicolor |
| 1.14.99.54 | 63 | - |
melting temperature, mutant A143C/P183C/S73C/A115C | Streptomyces coelicolor |
| 1.14.99.54 | 80 | - |
2 h, 34% residual activity. When the three disulfide bridges of the protein are broken, irreversible unfolding occurs and no residual activity can be detected after a similar heat treatment | Streptomyces coelicolor |
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
