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S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
A40S
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mutant enzyme shows 23% of the activity compared to wild-type enzyme with PPAVSLAMTMRR
A40T
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mutant enzyme is inactive with PPAVSLAMTMRR
D37S
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mutant enzyme is inactive with PPAVSLAMTMRR
H65G
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mutant enzyme is inactive with PPAVSLAMTMRR
H65G/R105P/G106V
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mutant enzyme shows about 25% of the activity of the wild-type enzyme in RSV substrates, about 5fold higher activity with the HIV-1 peptide substrate PRKILFLDGRR
L180A/L184A/V187A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residues, the mutant protein shows normal nucleocytoplasmic trafficking and localization at the cell plasmamembrane and in the cytosol
L219A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
L229A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
M239F
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein does not affect the enzyme activity and virus replication
M239G
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
N61P/P62L/Q63M
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mutant enzyme shows 434% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
P240F
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
R105P/G106V/H65G
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mutant enzyme exhibits behavior very similar to the wild-type enzyme for substitutions in the P4, P3, P2, P2', and P3' of the PPAVSLAMTMRR substrate positions. In contrast the mutants behave more like the HIV-1 protease in preference for amino acids substituted in the P1 and P1' positions
S38T
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200% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
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the murtant enzyme has 9 structurally equivalent residues from HIV-1 protease. Unlike the wild-type enzyme, the mutant enzyme hydrolyzes peptides representing the HIV-1 protease polyprotein cleavage sites
S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
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site-directed mutagenesis leading to the mutant RSV S9 protease, which is active with HIV-1 retropepsin substrates and inhibitable by HIV-1 retropepsin-specific inhibitors in contrast to the wild-type enzyme
V104T/R105P/G106V/S107N
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mutant enzyme shows 496% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
V225A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
V241G
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site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein abolishes the enzyme activity and blocks Rous sarcoma virus replication, detrimental effect, overview
W222A
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site-directed mutagenesis of the Gag polyprotein p10 sequence residue leads to accumulation of the mutant protein in the nucleus and reduced virus assembly, overview
S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
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site-directed mutagenesis leading to the mutant RSV S9 protease, which is active with HIV-1 retropepsin substrates and inhibitable by HIV-1 retropepsin-specific inhibitors in contrast to the wild-type enzyme
S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
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site-directed mutagenesis leading to the mutant RSV S9 protease, which is active with HIV-1 retropepsin substrates and inhibitable by HIV-1 retropepsin-specific inhibitors in contrast to the wild-type enzyme
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A100L
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less than 1% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
A100L
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mutant enzyme shows 1% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
DELTAN61-Q63
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245% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
DELTAN61-Q63
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mutant enzyme shows 245% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
I42D
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mutant enzyme shows 62% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme. Mutant enzyme exhibits HIV-1 protease specificity for P2- or P2'-modified peptide substrates but unchanged specificity with P4-, P3-, P1, P1' and P3'-modified substrates
I42D
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62% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
I44V
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mutant enzyme shows 211% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme. Mutant enzyme exhibits HIV-1 protease specificityfor P2- or P2'-modified peptide substrates but unchanged specificity with P4-, P3-, P1, P1' and P3'-modified substrates
I44V
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211% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V
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31% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V
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mutant enzyme shows 31% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
M73V/A100L
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96% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V/A100L
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mutant enzyme shows 88% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
Q63M
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448% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
Q63M
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mutant enzyme shows 447% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V
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mutant enzyme exhibits behavior very similar to the wild-type enzyme for substitutions in the P4, P3, P2, P2', and P3' of the PPAVSLAMTMRR substrate positions. In contrast the mutants behave more like the HIV-1 protease in preference for amino acids substituted in the P1 and P1' positions
R105P/G106V
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mutant enzyme shows 98% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V
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mutant enzyme shows the same activity as the wild-type enzyme with all RSV substrates, 10fold higher activity with the HIV-1 peptide substrate PRKILFLDGRR
R105P/G106V/S107N
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mutant enzyme shows 738% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V/S107N
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cleaves TSCYHCGT 50fold faster than the wild-type enzyme, cleaves PASSLAMT 140fold faster than the wild-type enzyme, cleaves PAVSLAMT 13.7fold faster than the wild-type enzyme, cleaves GAVSLAMT 48fold faster than the wild-type enzyme, cleaves PFVSLAMT 2.6fold faster than the wild-type enzyme
S107N
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377% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
S107N
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mutant enzyme shows 370% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
V104T
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229% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
V104T
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mutant enzyme shows 229% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
additional information
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mutations at the N-terminus: deletions of one or three residues, addition of one residue or substitution of Alan for the N-terminal Leu reduces enzymatic activity on peptide and protein substrates 100fold to 1000fold. The purified mutant enzymes remain monomeric up to a concentration of about 2 mg/ml. The three-dimensional structure of the monomeric mutant protein lacking the three N-terminal residues, DELTALAM, is significantly different from that of the wild-type enzyme
additional information
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if one of the surface loops is shortened, then the mutant exhibits only 2-3% of the activity associated with the wild-type enzyme
additional information
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delocalization mutations of the NES motif of p10 sequence shows that the motif can be located anywhere within the Gag polyprotein without loosing its function in translocation, overview