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3.4.23.16: HIV-1 retropepsin

This is an abbreviated version!
For detailed information about HIV-1 retropepsin, go to the full flat file.

Word Map on EC 3.4.23.16

Reaction

specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro =

Synonyms

CRF01_AE protease, Gag protease, HIV aspartyl protease, HIV PR, HIV protease, HIV-1 aspartyl protease, HIV-1 PR, HIV-1 protease, HIV-1 proteinase, HIV-1PR, HIV-2 protease, HIVPR, human immunodeficiency virus 1 protease, human immunodeficiency virus 1 retropepsin, human immunodeficiency virus protease, human immunodeficiency virus type 1 protease, human immunodeficiency virus type I protease, More, PR, PR1, PR2, retropepsin, retroproteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.16 HIV-1 retropepsin

Temperature Stability

Temperature Stability on EC 3.4.23.16 - HIV-1 retropepsin

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
at pH 3.4 and a protease concentration of 0.05 mM (monomer) the midpoint of the heat denaturation transition is 59.5°C
62
-
at pH 3.7 the midpoint of the heat denaturation transition is 62°C
66
-
at pH 4 the midpoint of the heat denaturation transition is 62°C
additional information
-
complexation with acetyl-Thr-Ile-Nle-r-Nle-Gln-Arg-NH2 stabilizes dimers of wild-type enzyme and mutant enzyme D25N. The effect on their Tm is smaller for the mutant enzyme (6.2°C) than for wild-type enzyme (8.7°C). The Tm of mutant enzyme-darunavir complex increases by 3°C relative to free mutant enzyme, as compared with a 22°C increase for wild-type enzyme-darunavir complex