3.4.23.B2: Simian immunodeficiency virus proteinase

This is an abbreviated version!
For detailed information about Simian immunodeficiency virus proteinase, go to the full flat file.

Reaction

The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala =

Synonyms

More, Pol polyprotein, retropepsin, Simian immunodeficiency virus protease, simian immunodeficiency virus retropepsin, SIV PR, SIV protease, SIV proteinase, SIV retropepsin, SIV-PR

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B2 Simian immunodeficiency virus proteinase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	AA Sequence
1	Application
4	Cloned(Commentary)
8	Crystallization (Commentary)
3	General Stability
7	IC50 Value
35	Inhibitors
10	Ki Value [mM]
4	KM Value [mM]
1	Metals/Ions
4	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
26	Organism
3	pH Optimum
2	pH Stability
5	pI Value
1	Posttranslational Modification
6	Protein Variants
5	Purification (Commentary)
2	Reaction
1	Reaction Type
24	Reference
2	Renatured (Commentary)
1	Specific Activity [micromol/min/mg]
2	Storage Stability
21	Substrates and Products (Substrate)
5	Subunits
13	Synonyms
1	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
4	Turnover Number [1/s]

Engineering

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Engineering on EC 3.4.23.B2 - Simian immunodeficiency virus proteinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Protein Variants Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D25N

Simian immunodeficiency virus

-

totally inactive mutant enzyme, incapable of autoprocessing

647805

K69H

Simian immunodeficiency virus

-

the isoelectric point of the mutant enzyme is pH 7.0 compared to that of the wild-type enzyme of 7.4. The purified mutant enzyme is less soluble at low pH when concentrating sample in preparation for crystallization

647805

S4H

2 entries

additional information

2 entries

S4H

Simian immunodeficiency virus

-

mutation does not significantly affect the kinetic parameters of the enzyme but stabilizes it approximately 4fold to autolysis. Crystals of the variant SIV PR S4H appear to have the same morphology as those obtained from wild-type enzyme

647818

S4H

Simian immunodeficiency virus

-

site-directed mutagenesis, the mutation of the major autodegeneration site stabilizes the enzyme without significantly affecting the kinetic parameters

668793

additional information

Simian immunodeficiency virus

-

generation of an protease-inactive mutant of SIVmac239, the phosphorylation pattern of the mutant Pr55Gag protein is unaltered compared to the wild-type, overview

670087

additional information

Simian immunodeficiency virus

-

it is demonstrated that the SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag by viral protease

682974