Any feedback?
Literature summary for 3.4.23.16 extracted from
- Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration (1996), J. Biol. Chem., 271, 5458-5463.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Q7K/L331I/L631I | mutant enzyme is highly resistant to autolysis, while retaining the physical properties, specificity, and susceptibility to inhibition of the wild-type enzyme | Human immunodeficiency virus 1 |
General Stability
| General Stability | Organism |
|---|---|
| wild-type enzyme and proteolysis-resistant mutant enzyme Q7K/L33I/L63I are stabilized at higher ionic strength, 1.0 M NaCl | Human immunodeficiency virus 1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
- |
- |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
greatest conformational stability at pH 5, wild-type enzyme and proteolysis-resistant mutant enzyme Q7K/L33I/L63I are are more stable at pH 5.0 than at pH 7.0, the mutant enzyme is slightly more stable than the wild-type enzyme | Human immunodeficiency virus 1 |
| 7 | - |
wild-type enzyme and proteolysis-resistant mutant enzyme Q7K/L33I/L63I are more stable at pH 5.0 than at pH 7.0, the mutant enzyme is slightly more stable than the wild-type enzyme | Human immunodeficiency virus 1 |
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
