General Stability | Organism |
---|---|
glutathiolation at Cys67 markedly stabilizes the enzyme activity presumably by reducing autoproteolysis | Human immunodeficiency virus 1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5,5'-dithiobis(2-nitrobenzoic acid) | enzyme activity is lost when a mixed disulfide is formed between 5,5'-dithiobis(2-nitrobenzoic acid) and Cys95, the same mixed disulfide at Cys67 reduces activity by 50%. Normal activity can be restored when the enzyme is treated with dithiothreitol | Human immunodeficiency virus 1 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
10870 | - |
electrospray mass spectrometry, unmodified protease | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
produced in Escherichia coli | - |
Human immunodeficiency virus 1 HXB2 | - |
produced in Escherichia coli | - |
Purification (Comment) | Organism |
---|---|
- |
Human immunodeficiency virus 1 |