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The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
-
-
-
-
The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
substrate binding structure and mechanism
-
The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
substrate binding structure and mechanism
-
The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3
substrate binding structure and mechanism
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Gag polyprotein precursor + H2O
?
gag precursor polyprotein + H2O
?
Gag-Pol precursor polyprotein + H2O
?
GAVSLAMT + H2O
GAVS + LAMT
-
-
-
?
KARVLAEAMS + H2O
KARVL + AEAMS
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PARVLAEAMRR + H2O
PARVL + AEAMRR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PARVLFLDGRR + H2O
PARVL + FLDGRR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PASSLAMT + H2O
PASS + LAMT
-
-
-
?
PATIMMORERR + H2O
PATIM + MORERR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PATVLTVALRR + H2O
PATVL + TVALRR
PAVSLAMT + H2O
PAVS + LAMT
PAVYLAMT + H2O
PAVY + LAMT
-
-
-
?
PFQAYPLREA + H2O
PFQAY + PLREA
-
-
-
-
?
PFVSLAMT + H2O
PFVS + LAMT
-
-
-
?
PGNFLQSRR + H2O
PGNF + LQSRR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
-
?
PHAVSLAMTMRR + H2O
PHAVS + LAMTMRR
-
-
-
-
?
PPAVALAMTMRR + H2O
PPAVA + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVELAMTMRR + H2O
PPAVE + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVFLAMTMRR + H2O
PPAVF + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVHLAMTMRR + H2O
PPAVH + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVLLAMTMRR + H2O
PPAVL + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVRLAMTMRR + H2O
PPAVR + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
PPAVSLAYMRR + H2O
PPAVS + LAYTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVWLAMTMRR + H2O
PPAVW + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVYLAMTMRR + H2O
PPAVY + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPDVSLAMTMRR + H2O
PPDVS + LAMTMRR
-
slight increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPFVSLAMTMRR + H2O
PPFVS + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPHVSLAMTMRR + H2O
PPHVS + LAMTMRR
PPNVSLAMTMRR + H2O
PPNVS + LAMTMRR
PPRVSLAMTMRR + H2O
PPRVS + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PRKILFLDGRR + H2O
PRKIL + FLDGRR
-
-
-
-
?
Rous sarcoma virus glycoprotein precursor + H2O
?
-
the enzyme has a stringent requirement for the presence of a pair of basic residues (Arg-Arg or Lys-Arg), when the cleavage sequence is deleted or modified to contain unpaired basic residues, intracellular cleavage of the glycoprotein precursor is completely blocked
-
-
?
TFQAYPLREA + H2O
TFQAY + PLREA
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
TLNFPISPKK + H2O
TLNF + PISPKK
-
slow cleavage with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
TSCYHCGT + H2O
TSCY + HCGT
-
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
-
medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
-
medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
-
medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VSFNFPQITKK + H2O
VSFNF + PQITKK
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
-
Phe and Leu are preferred at position P3
-
-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
-
Phe and Leu are preferred at position P3
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
-
preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
-
preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
-
preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
additional information
?
-
Gag polyprotein precursor + H2O
?
-
cleavage into several different mature proteins, processing by the p10 sequence portion of the Gag-polyprotein C-terminus
-
-
?
Gag polyprotein precursor + H2O
?
-
maturation, processing by the p10-capsid protease sequence of the Gag-polyprotein C-terminus
-
-
?
Gag polyprotein precursor + H2O
?
-
processing by the p10-capsid protease sequence of the Gag-polyprotein C-terminus, specific cleavage site
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the avian myoblastosis retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the avian myoblastosis retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
gag precursor polyprotein + H2O
?
-
the p2 region of RSV Gag, particularly the Pro-Pro-Pro-Tyr motif is important in the processing of the gag precursor polyprotein, most probably by controlling the activation of the virally encoded protease
-
-
?
gag precursor polyprotein + H2O
?
-
viral protein maturation occurs after protease subunits are released from the Gag polyprotein
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the p15 protein or rous sarcoma virus retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
PATVLTVALRR + H2O
PATVL + TVALRR
-
synthetic peptide substrate, required features, overview
-
-
?
PATVLTVALRR + H2O
PATVL + TVALRR
-
synthetic peptide substrate, required features, overview
-
-
?
PAVSLAMT + H2O
PAVS + LAMT
-
-
-
?
PAVSLAMT + H2O
PAVS + LAMT
-
-
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
synthetic peptide substrate, required features, overview
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
synthetic peptide substrate, required features, overview
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
-
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
nucleocapsi-protease peptide substrate
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
synthetic peptide substrate, required features, overview
-
-
?
PPHVSLAMTMRR + H2O
PPHVS + LAMTMRR
-
-
-
-
?
PPHVSLAMTMRR + H2O
PPHVS + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPNVSLAMTMRR + H2O
PPNVS + LAMTMRR
-
-
-
-
?
PPNVSLAMTMRR + H2O
PPNVS + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
additional information
?
-
-
the Rous sarcoma virus retropepsin differs by only two amino acid residues from the avian myeloblastosis virus retropepsin, both are biochemically indistinguishable, overview
-
-
?
additional information
?
-
-
the Rous sarcoma virus retropepsin differs by only two amino acid residues from the avian myeloblastosis virus retropepsin, both are biochemically indistinguishable, overview
-
-
?
additional information
?
-
-
the enzyme is a homodimer which acts symmetrically in substrate selection with each enzyme subunit being capable of recognizing both halves of a peptide substrate equally
-
-
?
additional information
?
-
-
Rous sarcoma virus protease and avian myeloblastosis virus protease differ in sequence by two amino acids, are biochemically indistinguishable and used interchangeable in these studies
-
-
?
additional information
?
-
-
molecular mechanics calculations
-
-
?
additional information
?
-
-
no cleavage of PPAVSLWMTMRR
-
-
?
additional information
?
-
-
the enzyme is an intrinsic part of the virus assembly responsible for coordination of the process
-
-
?
additional information
?
-
-
the enzyme is an intrinsic part of the virus assembly responsible for coordination of the process, enzyme inhibition blocks the virus replication
-
-
?
additional information
?
-
-
the Rous sarcoma virus retropepsin differs by only two amino acid residues from the avian myeloblastosis virus retropepsin, both are biochemically indistinguishable, overview
-
-
?
additional information
?
-
-
the soluble export receptor Crm1, and the nuclear pore proteins Nup214 and Nup98 are important cofactors of the enzyme involved in the export of the RSV GAg protein from the nucleus, overview
-
-
?
additional information
?
-
-
the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs)
-
-
?
additional information
?
-
-
the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs). Structure determination of in vitro-assembled, immature virus-like Rous sarcoma virus (RSV) Gag particles, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gag polyprotein precursor + H2O
?
gag precursor polyprotein + H2O
?
Gag-Pol precursor polyprotein + H2O
?
additional information
?
-
Gag polyprotein precursor + H2O
?
-
cleavage into several different mature proteins, processing by the p10 sequence portion of the Gag-polyprotein C-terminus
-
-
?
Gag polyprotein precursor + H2O
?
-
maturation, processing by the p10-capsid protease sequence of the Gag-polyprotein C-terminus
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the avian myoblastosis retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the avian myoblastosis retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
gag precursor polyprotein + H2O
?
-
the p2 region of RSV Gag, particularly the Pro-Pro-Pro-Tyr motif is important in the processing of the gag precursor polyprotein, most probably by controlling the activation of the virally encoded protease
-
-
?
gag precursor polyprotein + H2O
?
-
viral protein maturation occurs after protease subunits are released from the Gag polyprotein
-
-
?
gag precursor polyprotein + H2O
?
-
cleavage into several different mature proteins, processing by the p15 protein or rous sarcoma virus retropepsin, which is part of the Gag-polyprotein and located at the C-terminus
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
Gag-Pol precursor polyprotein + H2O
?
-
cleavage into several different mature proteins
-
-
?
additional information
?
-
-
the enzyme is an intrinsic part of the virus assembly responsible for coordination of the process
-
-
?
additional information
?
-
-
the enzyme is an intrinsic part of the virus assembly responsible for coordination of the process, enzyme inhibition blocks the virus replication
-
-
?
additional information
?
-
-
the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.244
KARVLAEAMS
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.366
PARVLAEAMRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.111
PARVLFLDGRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.132
PATIMMORERR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
24.5
PAVYLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.283
PGNFLQSRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.006 - 0.077
PPAVSLAMTMRR
0.037
TFQAYPLREA
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.538
VSFNFPQITKK
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
additional information
-
0.011
GAVSLAMT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
0.064
GAVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.006
PASSLAMT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
2.4
PASSLAMT
-
pH 5.9, 37°C
0.009
PAVSLAMT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
0.056
PAVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.004
PFVSLAMT
-
pH 5.9, 37°C, mutant enzyme R105P/G106V/S107N
0.0054
PFVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.006
PPAVSLAMTMRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.0416
PPAVSLAMTMRR
-
pH 5.9
0.045
PPAVSLAMTMRR
-
pH 5.9, 37°C, mutant enzyme R105P/G106V mutant enzyme
0.049
PPAVSLAMTMRR
-
pH 5.9, 37°C, AMV protease
0.077
PPAVSLAMTMRR
-
pH 5.9, 37°C, mutant enzyme H65G/R105P/G106V mutant enzyme
0.095
PRKILFLDGRR
-
pH 5.9, 37°C, mutant enzyme H65G/R105P/G106V
0.098
PRKILFLDGRR
-
pH 5.9, 37°C, AMV protease
0.1
PRKILFLDGRR
-
pH 5.9, 37°C, mutant enzyme R105P/G106V
0.072
TSCYHCGT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
427
TSCYHCGT
-
pH 5.9, 37°C, wild-type enzyme
additional information
additional information
-
relative KM-value for various modified substrates compared to the substrates PPAVSLAMTMRR
-
additional information
additional information
-
relative KM-values for the mutant enzymes R105P/106V and R105P/G106V/H65G with PPAVSLAMTMRR compared to the wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.167
KARVLAEAMS
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
1.63
PARVLAEAMRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
8.2
PARVLFLDGRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
2.98
PATIMMORERR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
4.07
PAVYLAMT
-
pH 5.9, 37°C
0.283
PGNFLQSRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.0183 - 1.6
PPAVSLAMTMRR
0.0217 - 0.193
PRKILFLDGRR
0.183
TFQAYPLREA
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.25
VSFNFPQITKK
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
additional information
additional information
-
0.0483
GAVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.36
GAVSLAMT
-
pH 5.9, 37°C, mutant enzyme R105P/G106V/S107N
0.0717
PASSLAMT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
0.217
PASSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.273
PAVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.613
PAVSLAMT
-
pH 5.9, 37°C, mutant enzyme R105P/G106V/S107N
0.248
PFVSLAMT
-
pH 5.9, 37°C, wild-type enzyme
0.437
PFVSLAMT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
0.0183
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme A100L
0.0667
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme M73V
0.102
PPAVSLAMTMRR
-
pH 5.9, 37°C, mutant enzyme H65G/R105P/G106V mutant enzyme
0.133
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme I42D
0.19
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme M73V/A100L
0.212
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme R105P/G106V
0.217
PPAVSLAMTMRR
-
pH 5.9, wild-type enzyme
0.332
PPAVSLAMTMRR
-
pH 5.9, 37°C, mutant enzyme R105P/G106V
0.36
PPAVSLAMTMRR
-
pH 5.9, 37°C, AMV protease
0.457
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme I44V
0.497
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme V104T
0.53
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme DELTAN61-Q63
0.717
PPAVSLAMTMRR
-
pH 5.9, 37°C, reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
0.817
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme S107N
0.94
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme N61P/P62L/Q63M
0.97
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme Q63M
1.08
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme V104T/R105P/G106V/S107N
1.6
PPAVSLAMTMRR
-
pH 5.9, mutant enzyme R105P/G106V/S107N
0.0217
PRKILFLDGRR
-
pH 5.9, 37°C, AMV protease
0.0917
PRKILFLDGRR
-
pH 5.9, 37°C, mutant enzyme H65G/R105P/G106V
0.193
PRKILFLDGRR
-
pH 5.9, 37°C, mutant enzyme R105P/G106V
0.147
TSCYHCGT
-
pH 5.9, 37°C, wild-type enzyme
1.23
TSCYHCGT
-
pH 5.9, 37°C, mutant enzymeR105P/G106V/S107N
additional information
additional information
-
relative turnover-numbers for various modified substrates compared to the substrates PPAVSLAMTMRR
-
additional information
additional information
-
relative turnover numbers for the mutant enzymes R105P/106V and R105P/G106V/H65G with PPAVSLAMTMRR compared to the wild-type enzyme
-
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S38T/I42D/I44V/M73V/A100L/V104T/R105P/G106V/S107N
A40S
-
mutant enzyme shows 23% of the activity compared to wild-type enzyme with PPAVSLAMTMRR
A40T
-
mutant enzyme is inactive with PPAVSLAMTMRR
D37S
-
mutant enzyme is inactive with PPAVSLAMTMRR
H65G
-
mutant enzyme is inactive with PPAVSLAMTMRR
H65G/R105P/G106V
-
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
-
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
-
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
-
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
-
site-directed mutagenesis of the p10-capsid protease sequence of Gag polyprotein does not affect the enzyme activity and virus replication
M239G
-
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
-
mutant enzyme shows 434% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
P240F
-
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
-
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
-
200% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
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
-
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
-
mutant enzyme shows 496% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
V225A
-
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
-
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
-
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
-
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
-
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
-
A100L
-
less than 1% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
A100L
-
mutant enzyme shows 1% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
DELTAN61-Q63
-
245% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
DELTAN61-Q63
-
mutant enzyme shows 245% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
I42D
-
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
-
62% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
I44V
-
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
-
211% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V
-
31% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V
-
mutant enzyme shows 31% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
M73V/A100L
-
96% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
M73V/A100L
-
mutant enzyme shows 88% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
Q63M
-
448% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
Q63M
-
mutant enzyme shows 447% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V
-
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
-
mutant enzyme shows 98% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V
-
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
-
mutant enzyme shows 738% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
R105P/G106V/S107N
-
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
-
377% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
S107N
-
mutant enzyme shows 370% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
V104T
-
229% of the activity relative to wild-type enzyme with PPAVSLAMTMRR
V104T
-
mutant enzyme shows 229% of the activity with PPAVSLAMTMRR as substrate compared to activity of the wild-type enzyme
additional information
-
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
-
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
-
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
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