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Literature summary for 3.4.23.47 extracted from

  • Dunn, B.M.
    Human immunodeficiency virus 2 retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rowlings, N. D. ; Woessner, J. F. , eds. ), 1, 154-157.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
genetic organization, processing steps, expression of the viral enzyme in bacterial and yeast recombinant systems Human immunodeficiency virus 2

Crystallization (Commentary)

Crystallization (Comment) Organism
substrate binding pocket structure analysis Human immunodeficiency virus 2

Protein Variants

Protein Variants Comment Organism
additional information construction of a hybrid gene with the viral reverse transcriptase, constuction of a hybrid comprising HIV-1 and HIV-2 retropepsin, overview Human immunodeficiency virus 2

Inhibitors

Inhibitors Comment Organism Structure
(hydroxyethyl)amide isostere
-
Human immunodeficiency virus 2
acetyl-pepstatin
-
Human immunodeficiency virus 2
pepstatin A
-
Human immunodeficiency virus 2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Human immunodeficiency virus 2
0.16
-
YVSQNFPIVQNR pH 4.7 Human immunodeficiency virus 2

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2
-
i.e. HIV-2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification self-processing of the immature progeny virus at the host cell membrane prior to virus budding, dimerization occurs before proteolytic cleavage Human immunodeficiency virus 2

Reaction

Reaction Comment Organism Reaction ID
Endopeptidase for which the P1 residue is preferably hydrophobic substrate binding pocket structure and reaction mechanism, the enzyme prefers the cleavage site sequence VSQNY*PIVQ with Glu being preferred at the P2' site Human immunodeficiency virus 2

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
HIV-1 Gag-Pol poylprotein + H2O site-specific proteolytic cleavage, protein precursors and peptides derived thereof Human immunodeficiency virus 2 ?
-
?
HIV-2 Gag-Pol poylprotein + H2O site-specific proteolytic cleavage, protein precursors and peptides derived thereof Human immunodeficiency virus 2 ?
-
?
Lys-Ala-Arg-Val-Nle-Nph-Glu-Ala-Nle-NH2 + H2O the enzyme is highly active with peptide substrates containing variations of this cleavage sequence Human immunodeficiency virus 2 Lys-Ala-Arg-Val-Nle + Nph-Glu-Ala-Nle-NH2
-
?
additional information the enzyme prefers the cleavage site sequence VSQNY*PIVQ with Glu being preferred at the P2' site Human immunodeficiency virus 2 ?
-
?
myristylated p53-Gag precursor + H2O
-
Human immunodeficiency virus 2 ?
-
?
p24-Gag protein + H2O
-
Human immunodeficiency virus 2 ?
-
?
YVSQNFPIVQNR + H2O synthetic peptide substrate based on the Ma/Ca cleavage site of HIV-1 Gag Human immunodeficiency virus 2 YVSQNF + PIVQNR
-
?

Subunits

Subunits Comment Organism
dimer the HIV-2 retropepsin must form a homodimer in order to create a functional active site, dimerization occurs before proteolytic cleavage Human immunodeficiency virus 2

Synonyms

Synonyms Comment Organism
HIV-2 proteinase
-
Human immunodeficiency virus 2
human immunodeficiency virus 2 retropepsin
-
Human immunodeficiency virus 2
More the enzyme belongs to the peptidase family A2 Human immunodeficiency virus 2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.7
-
assay at Human immunodeficiency virus 2

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000012
-
(hydroxyethyl)amide isostere
-
Human immunodeficiency virus 2
0.000005
-
acetyl-pepstatin pH 4.7, competitive versus YVSQNFPIVQNR Human immunodeficiency virus 2
0.000015
-
pepstatin A pH 4.7 Human immunodeficiency virus 2