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Literature summary for 3.4.23.16 extracted from
- A molecular dynamics study of the structural stability of HIV-1 protease under physiological conditions: the role of Na+ ions in stabilizing the active site (2005), Proteins, 58, 450-458.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | molecular dynamics technique simulation of pH effecting the enzyme dynamics, effects of Na+ and Cl- ions, overview | Human immunodeficiency virus 1 |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Na+ | role of Na+ ions in stabilizing the active site | Human immunodeficiency virus 1 |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
i.e. HIV-1 | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro | the active site structure and conformational flexibility | Human immunodeficiency virus 1 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HIV-1 protease | - |
Human immunodeficiency virus 1 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 6.5 | the enzyme is most active under weakly acidic conditions, when the cataltyic residues Asp25 and Asp25' share one proton, loss of this proton at neutral pH destabilizes the enzyme structure, molecular dynamics technique simulation of pH effecting the enzyme dynamics, overview | Human immunodeficiency virus 1 |
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