Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cyclophilin | human cyclophilin enhances activity, it is proposed that cyclophilin functions as an auxiliary enzyme for the protease during cleavage in the virion | Human immunodeficiency virus 1 |
Protein Variants | Comment | Organism |
---|---|---|
C67A | kcat/Km ratio for KARV-Nle-Phe(NO2)-EA-Nle-NH2 as substrate is similar to that of the wild-type enzyme | Human immunodeficiency virus 1 |
C67A/C95A | urea denaturation is unchanged from that of the wild-type enzyme. Kcat/Km ratio for KARV-Nle-Phe(NO2)-EA-Nle-NH2 as substrate is similar to that of the wild-type enzyme | Human immunodeficiency virus 1 |
General Stability | Organism |
---|---|
1.8 M urea, 50% loss of activity of wild-type enzyme and mutant enzyme C67A/C95A | Human immunodeficiency virus 1 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.133 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, wild-type enzyme | Human immunodeficiency virus 1 | |
0.231 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, mutant enzyme C95A | Human immunodeficiency virus 1 | |
0.244 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, mutant enzyme C67A/C95A | Human immunodeficiency virus 1 | |
0.263 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, mutant enzyme C67A | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Human immunodeficiency virus 1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Arg-Glu-[5-[(2'-aminoethyl)-amino]naphthalenesulfonyl]-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-[4-[[4'-(dimethylamino)phenyl]azo]-benzoyl]-Arg + H2O | - |
Human immunodeficiency virus 1 | ? | - |
? | |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O | - |
Human immunodeficiency virus 1 | KARV-Nle + Phe(NO2)-EA-Nle-NH2 | - |
? | |
additional information | autocatalytic maturation, two temporally regulated N-terminal cleavages, first at the native TFP/p6pol followed by cleavage at the p6pol/PR, are crucial for protease maturation and enzymatic activity | Human immunodeficiency virus 1 | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.9 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, wild-type enzyme | Human immunodeficiency virus 1 | |
3.5 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, mutant enzyme C67A/C95A and mutant enzyme C95A | Human immunodeficiency virus 1 | |
3.7 | - |
KARV-Nle-Phe(NO2)-EA-Nle-NH2 | pH 5.0, 25°C, mutant enzyme C67A | Human immunodeficiency virus 1 |