Any feedback?
Literature summary for 3.4.16.4 extracted from
- Interaction energies between beta-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation (2001), Protein Sci., 10, 1254-1259.
General Stability
| General Stability | Organism |
|---|---|
| the binding of beta-lactam antibiotics cefoxitin, cloxacillin, moxalactam, and imipenem all stabilize the enzyme significantly with an increase in melting temperature of up to 4.6°C | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| penicillin-binding protein 5 | - |
Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 49 | - |
melting temperature (Tm), reversible denaturation in a two-state manner. The binding of beta-lactam antibiotics cefoxitin, cloxacillin, moxalactam, and imipenem all stabilize the enzyme significantly with DELTATm values as high as 4.6°C | Escherichia coli |
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
