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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

General Stability

General Stability on EC 3.4.23.16 - HIV-1 retropepsin

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1.8 M urea, 50% loss of activity of wild-type enzyme and mutant enzyme C67A/C95A
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glutathiolation at Cys67 markedly stabilizes the enzyme activity presumably by reducing autoproteolysis
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observed enzyme mutations of HIV-1 protease, either naturally occuring or induced by drug therapy, are found in regions that are not structurally designed to withstand unfolding. These mutations are especially likely to occur in the flap region, a part of the protein which is not essential for stability of the protein, but does contribute significantly to the stability of the protease-drug complexes
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the open structure of a multi-drug-resistant HIV-1 protease is stabilized by crystal packing contacts
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wild-type enzyme and proteolysis-resistant mutant enzyme Q7K/L33I/L63I are stabilized at higher ionic strength, 1.0 M NaCl
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