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Literature summary for 3.4.23.B2 extracted from

  • Konvalinka, J.; Kraeusslich, H.
    Simian immunodeficiency virus retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 158-160.
No PubMed abstract available
Search for more literature for 3.4.23.B2

Application

Application Comment Organism
additional information SIV retropepsin can serve as an inhibitor-resistant retrovirus variant model of HIV-1 retropepsin Simian immunodeficiency virus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, expression as N-terminally capped, biotin-labeled precursor Simian immunodeficiency virus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determination and analysis of free enzyme and enzyme-inhibitor complexes, e.g. with 1,2-epoxy-3-(4-nitrophenoxy)propane at 2.4 A resolution, or with SKF107457 at 2.5 A resolution Simian immunodeficiency virus

Protein Variants

Protein Variants Comment Organism
S4H site-directed mutagenesis, the mutation of the major autodegeneration site stabilizes the enzyme without significantly affecting the kinetic parameters Simian immunodeficiency virus

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(4-nitrophenoxy)propane specific inhibition Simian immunodeficiency virus
additional information several HIV-1 peptomimetic inhibitors also inhibit the SIV retropepsin, inhibitor binding structure Simian immunodeficiency virus
pepstatin A specific inhibition Simian immunodeficiency virus
SKF107457 a hydroxyethylene inhibitor Simian immunodeficiency virus

Organism

Organism UniProt Comment Textmining
Simian immunodeficiency virus
-
 SIV, a lenti-retrovirus, derived from different monkey species, the virus is pathogenic not in all of the species, overview
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the retropepsin is expressed as part of a larger polyprotein precursor, which it cleaves into functional proteins, the major autodegradation site of the enzyme is Phe3-Ser4 Simian immunodeficiency virus

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, and ion exchange or affinity chromatography on a pepstatin A resin, recombinant N-terminally capped, biotin-labeled precursor by streptavidin affinity chromatography, the tag is autocatalytically cleaved after refolding of the enzyme Simian immunodeficiency virus

Reaction

Reaction Comment Organism Reaction ID
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 aspartic acid protease, structure-function relation ship, the active site conformation changes from open to closed upon substrate binding, overview Simian immunodeficiency virus
a

Renatured (Commentary)

Renatured (Comment) Organism
refolding from recombinant cytoplasmic inclusion bodies, refolding of recombinant N-terminally capped, biotin-labeled precursor Simian immunodeficiency virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SIV Gag precursor protein + H2O determination of cleavage sites and substrate specificity Simian immunodeficiency virus ?
-
 ?

Subunits

Subunits Comment Organism
dimer the active enzyme is a homodimer, each subunit contains an Asn-Thr-Gly aspartic acid protease motif Simian immunodeficiency virus

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the A2 peptidase family Simian immunodeficiency virus
simian immunodeficiency virus retropepsin
-
 Simian immunodeficiency virus
SIV retropepsin
-
 Simian immunodeficiency virus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information
-
 Simian immunodeficiency virus