Protein Variants | Comment | Organism |
---|---|---|
additional information | enzyme PR mutant with mutations Q7K/L33I/L63I/C67A/C95A and the additional mutation D25N/C2-S-S-C97, in which the terminal beta-strand is linked through a disulfide bridge, is less prone to aggregation, even at a relatively high protein concentration of about 1 mM | Human immunodeficiency virus 1 |
Q7K/D29N/L33I/L63I/C67A/C95A | 920fold less active than with Q7K/L33I/L63I/C67A/C95A, poor catalytic activity arises both from the destabilization of the dimer as well as changes in the active site environment | Human immunodeficiency virus 1 |
Q7K/L33I/L63I/C67A/R87K/C95A | 4600fold less active than with Q7K/L33I/L63I/C67A/C95A | Human immunodeficiency virus 1 |
Q7K/T26A/L33I/L63I/C67A/C95A | mutant enzyme with restricted autoproteolysis, mutation T26A destabilizes the dimer, exhibits a monomer fold and is prone to aggregation | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | P04585 | - |
- |
Purification (Comment) | Organism |
---|---|
mutant enzymes Q7K/T26A/L33I/L63IC67A/C95A and Q7K/D29N/L33I/L63IC67A/C95A | Human immunodeficiency virus 1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O | - |
Human immunodeficiency virus 1 | KARV-Nle + Phe(NO2)-EA-Nle-NH2 | - |
? |