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APOBEC3 (A3G) + H2O
?
-
viral protease cleaves antiviral host factor APOBEC3 (A3) after maturation of virions in mice and thereby escapes from its antiviral activity
-
-
?
APQVLPVMHP + H2O
APQVL + PVMHP
-
-
-
?
Arg-Glu(EDANS)-Ser-Gln-Ala-Phe-Pro-Leu-Arg-Ala-Lys(dansyl)-Arg-OH + H2O
Arg-Glu(EDANS)-Ser-Gln-Ala-Phe + Pro-Leu-Arg-Ala-Lys(dansyl)-Arg-OH
-
fluorescent substrate, contains a p12/CA cleavage site
-
-
?
DELILPVKRK + H2O
DELIL + PVKRK
-
-
-
-
?
DSKAFLARDW + H2O
DSKAF + LARDW
-
-
-
?
DSKAFLATDW + H2O
DSKAF + LATDW
-
-
-
-
?
FLAG-pr55Gag + H2O
?
-
-
-
?
Gag-Pol polyprotein + H2O
?
human tumor suppressor protein ARL11 + H2O
?
-
-
-
?
human tumor suppressor protein BAX + H2O
?
-
-
-
?
human tumor suppressor protein DKK3 + H2O
?
-
-
-
?
human tumor suppressor protein PTEN + H2O
?
-
-
-
?
KARVnLNphEAnLG + H2O
KARVnL + NphEAnLG
-
-
-
-
?
LTFTFPVVFMRR + H2O
LTFTF + PVVFMRR
-
-
-
?
Lys-Ala-Arg-Val-Nle-Phe(4-nitro)-Glu-Ala-Nle-amide + H2O
?
-
commercial chromogenic substrate
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
PKDIFPVTET + H2O
PKDIF + PVTET
-
-
-
?
PLQVLTLNIERR + H2O
PLQVL + TLNIERR
-
contains a PR/RT cleavage site
-
-
?
PLQVLTLNIERR + H2O
PLQVLTL + NIERR
-
-
-
?
PPAILPIISE + H2O
PPAIL + PIISE
-
-
-
?
PRSSLYPALRTP + H2O
PRSSLY + PALRTP
-
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
PSEEYPIMID + H2O
PSEEY + PIMID
-
-
-
?
QNYPIV + H2O
QNY + PIV
-
-
-
?
R-peptide precursor Env + H2O
?
-
-
the viral protease removes a 16-residue peptide, the R-peptide from the endodomain of the transmembrane subunit. The legs of the R-peptide Env are held together by trimeric interactions at the very bottom of Env. It is the transmembrane leg separation, normally caused by R-peptide cleavage, that primes Env for receptor triggering
-
?
RSLLYPALTP + H2O
RSLLY + PALTP
-
a P3 Leu-substituted peptide mimicking the MA/p12 cleavage site of Moloney murine leukemia virus proitease
-
-
?
SDLVLLSAEARR + H2O
SDLVL + LSAEARR
-
-
-
?
SQNYPIV + H2O
SQNY + PIV
-
-
-
?
SQNYPIVQ + H2O
SQNY + PIVQ
-
-
-
?
TQTSLLIENSS + H2O
TQTSLL + IENSS
-
contains a NC/PR cleavage site
-
-
?
TQTSLLTLDDQ + H2O
TQTSLL + TLDDQ
-
-
-
?
TQTSSLTLDDQ + H2O
TQTSSL + TLDDQ
-
-
-
-
?
TSQAFPLRAG + H2O
?
-
-
-
-
?
TSQAFPLRAG + H2O
TSQAF + PLRAG
TSTLLIENSS + H2O
TSTLL + IENSS
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
VAQNYPIVQ + H2O
VAQNY + PIVQ
-
-
-
-
?
VAQNYPIVQ-NH2 + H2O
VAQNY + PIVQ-NH2
-
-
-
-
?
VDQNYPIVQ + H2O
VDQNY + PIVQ
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
-
-
-
-
?
VFQNYPIVQ-NH2 + H2O
VFQNY + PIVQ-NH2
-
-
-
-
?
VGFAGAMAEAE + H2O
VGFAG + AMAEAE
-
-
-
-
?
VGFAGAMAEAR + H2O
VGFAG + AMAEAR
-
-
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
VIQNYPIVQ-NH2 + H2O
VISQNY + PIVQ-NH2
-
-
-
-
?
VISQNYPIVQ + H2O
VISQNY + PIVQ
-
-
-
-
?
VKQNYPIVQ + H2O
VKQNY + PIVQ
-
-
-
-
?
VKQNYPIVQ-NH2 + H2O
VKQNY + PIVQ-NH2
-
-
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
-
-
-
-
?
VLQNYPIVQ-NH2 + H2O
VLQNY + PIVQ-NH2
-
-
-
-
?
VMQNYPIVQ + H2O
VMQNY + PIVQ
-
-
-
-
?
VMQNYPIVQ-NH2 + H2O
VMQNY + PIVQ-NH2
-
-
-
-
?
VNQNYPIVQ + H2O
VNQNY + PIVQ
-
-
-
-
?
VNQNYPIVQ-NH2 + H2O
VNQNY + PIVQ-NH2
-
-
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
VSANYPIVQ + H2O
VSANY + PIVQ
-
-
-
-
?
VSANYPIVQ-NH2 + H2O
VSANY + PIVQ-NH2
-
-
-
-
?
VSDNYPIVQ + H2O
VSDNY + PIVQ
-
-
-
-
?
VSDNYPIVQ-NH2 + H2O
VSDNY + PIVQ-NH2
-
-
-
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
-
-
-
-
?
VSFNYPIVQ-NH2 + H2O
VSFNY + PIVQ-NH2
-
-
-
-
?
VSGNYPIVQ + H2O
VSGNY + PIVQ
-
-
-
-
?
VSGNYPIVQ-NH2 + H2O
VSGNY + PIVQ-NH2
-
-
-
-
?
VSKNYPIVQ + H2O
VSKNY + PIVQ
-
-
-
-
?
VSKNYPIVQ-NH2 + H2O
VSKNY + PIVQ-NH2
-
-
-
-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
-
-
-
-
?
VSLNYPIVQ-NH2 + H2O
VSLNY + PIVQ-NH2
-
-
-
-
?
VSLQNYPIVQ + H2O
VSLQNY + PIVQ
-
-
-
-
?
VSNNYPIVQ + H2O
VSNNY + PIVQ
-
-
-
-
?
VSNNYPIVQ-NH2 + H2O
VSNNY + PIVQ-NH2
-
-
-
-
?
VSQAYPIVQ + H2O
VSQAY + PIVQ
-
-
-
-
?
VSQAYPIVQ-NH2 + H2O
VSQAY + PIVQ-NH2
-
-
-
-
?
VSQDYPIVQ + H2O
VSQDY + PIVQ
-
-
-
-
?
VSQDYPIVQ-NH2 + H2O
VSQDY + PIVQ-NH2
-
-
-
-
?
VSQFYPIVQ + H2O
VSQFY + PIVQ
-
-
-
-
?
VSQFYPIVQ-NH2 + H2O
VSQFY + PIVQ-NH2
-
-
-
-
?
VSQGYPIVQ + H2O
VSQGY + PIVQ
-
-
-
-
?
VSQGYPIVQ-NH2 + H2O
VSQGY + PIVQ-NH2
-
-
-
-
?
VSQIYPIVQ + H2O
VSQIY + PIVQ
-
-
-
-
?
VSQIYPIVQ-NH2 + H2O
VSQIY + PIVQ-NH2
-
-
-
-
?
VSQKYPIVQ + H2O
VSQKY + PIVQ
-
-
-
-
?
VSQLNYPIVQ + H2O
VSQLNY + PIVQ
-
-
-
-
?
VSQLNYPIVQ-NH2 + H2O
VSQLY + PIVQ-NH2
-
-
-
-
?
VSQLYPIVQ + H2O
VSQLY + PIVQ
-
-
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
VSQNLPIVQ + H2O
VSQNL + PIVQ
VSQNMPIVQ + H2O
VSQNM + PIVQ
VSQNYPAVQ + H2O
VSQNY + PAVQ
-
-
-
-
?
VSQNYPAVQ-NH2 + H2O
VSQNY + PAVQ-NH2
-
-
-
-
?
VSQNYPFVQ + H2O
VSQNY + PFVQ
-
-
-
-
?
VSQNYPFVQ-NH2 + H2O
VSQNY + PFVQ-NH2
-
-
-
-
?
VSQNYPIAQ + H2O
VSQNY + PIAQ
-
-
-
-
?
VSQNYPIAQ-NH2 + H2O
VSQNY + PIAQ-NH2
-
-
-
-
?
VSQNYPIEQ + H2O
VSQNY + PIEQ
-
-
-
-
?
VSQNYPIEQ-NH2 + H2O
VSQNY + PIWQ-NH2
-
-
-
-
?
VSQNYPIFQ + H2O
VSQNY + PIFQ
-
-
-
-
?
VSQNYPIFQ-NH2 + H2O
VSQNY + PIFQ-NH2
-
-
-
-
?
VSQNYPIIQ + H2O
VSQNY + PIIQ
-
-
-
-
?
VSQNYPIIQ-NH2 + H2O
VSQNY + PIIQ-NH2
-
-
-
-
?
VSQNYPIKQ + H2O
VSQNY + PIKQ
-
-
-
-
?
VSQNYPIKQ-NH2 + H2O
VSQNY + PIKQ-NH2
-
-
-
-
?
VSQNYPILQ + H2O
VSQNY + PILQ
-
-
-
-
?
VSQNYPILQ-NH2 + H2O
VSQNY + PILQ-NH2
-
-
-
-
?
VSQNYPIQQ + H2O
VSQNY + PIQQ
-
-
-
-
?
VSQNYPIQQ-NH2 + H2O
VSQNY + PIQQ-NH2
-
-
-
-
?
VSQNYPIRQ + H2O
VSQNY + PIRQ
-
-
-
-
?
VSQNYPIRQ-NH2 + H2O
VSQNY + PIRQ-NH2
-
-
-
-
?
VSQNYPISQ + H2O
VSQNY + PISQ
-
-
-
-
?
VSQNYPISQ-NH2 + H2O
VSQNY + PISQ-NH2
-
-
-
-
?
VSQNYPIV + H2O
VSQNY + PIV
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
VSQNYPIVQ-NH2 + H2O
VSQNY + PIVQ-NH2
-
-
-
-
?
VSQNYPLVQ + H2O
VSQNY + PLVQ
VSQNYPLVQ-NH2 + H2O
VSQNY + PLVQ-NH2
-
-
-
-
?
VSQNYPVVQ + H2O
VSQNY + PVVQ
-
-
-
-
?
VSQNYPVVQ-NH2 + H2O
VSQNY + PVVQ-NH2
-
-
-
-
?
VSQTYPIVQ + H2O
VSQTY + PIVQ
-
-
-
-
?
VSQTYPIVQ-NH2 + H2O
VSQTY + PIVQ-NH2
-
-
-
-
?
VSQVYPIVQ + H2O
VSQVY + PIVQ
-
-
-
-
?
VSQVYPIVQ-NH2 + H2O
VSQVY + PIVQ-NH2
-
-
-
-
?
VSVNYPIVQ-NH2 + H2O
VSVNY + PIVQ-NH2
-
-
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
VTQNYPIVQ-NH2 + H2O
VTQNY + PIVQ-NH2
-
-
-
-
?
VVQNYPIVQ + H2O
VVQNY + PIVQ
-
-
-
-
?
VVQNYPIVQ-NH2 + H2O
VVQNY + PIVQ-NH2
-
-
-
-
?
additional information
?
-
Gag polyprotein + H2O
?
-
-
-
-
?
Gag polyprotein + H2O
?
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
Gag polyprotein + H2O
?
-
autolysis of the retropepsin from the precursor protein
-
-
?
Gag-Pol polyprotein + H2O
?
-
-
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
-
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
-
contains a CA/NC cleavage site
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
-
contains a CA/NC cleavage site
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
-
-
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
-
contains a MA/p12 cleavage site, low activity
-
-
?
TSQAFPLRAG + H2O
TSQAF + PLRAG
-
-
-
?
TSQAFPLRAG + H2O
TSQAF + PLRAG
-
contains a p12/CA cleavage site, low activity
-
-
?
TSQAFPLRAG + H2O
TSQAF + PLRAG
-
contains a p12/CA cleavage site, low activity
-
-
?
TSTLLIENSS + H2O
TSTLL + IENSS
-
-
-
?
TSTLLIENSS + H2O
TSTLL + IENSS
-
contains a RT/IN cleavage site
-
-
?
TSTLLIENSS + H2O
TSTLL + IENSS
-
contains a RT/IN cleavage site
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
-
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
-
-
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
-
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
-
contains a p12E/p2E cleavage site
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
-
contains a p12E/p2E cleavage site
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
-
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
-
-
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
-
-
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
a HIV-1 retropepsin substrate
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNYPLVQ + H2O
VSQNY + PLVQ
-
-
-
?
VSQNYPLVQ + H2O
VSQNY + PLVQ
-
-
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
-
-
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
additional information
?
-
-
activity of recombinant enzyme with recombinant Gag protein fragments, overview
-
-
?
additional information
?
-
-
cleavage site and substrate specificity, overview
-
-
?
additional information
?
-
-
study of influence of the P2 position residue on cleavage site specificity, overview
-
-
?
additional information
?
-
-
activity of recombinant enzyme with recombinant Gag protein fragments, overview
-
-
?
additional information
?
-
-
the enzyme is active with the peptide representing the HIV-1 reverse transcriptase/integrase cleavage site, kinetics
-
-
?
additional information
?
-
-
the enzyme is active with the peptide representing the HIV-1 reverse transcriptase/integrase cleavage site, kinetics
-
-
?
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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0.15
APQVLPVMHP
-
pH 6.0, 37°C
0.0846
DELILPVKRK
-
pH 6.0, 37°C
0.2
DSKAFLATDW
-
pH 6.0, 37°C
0.0192
LTFTFPVVFMRR
-
pH 6.0, 37°C
0.51
PKDIFPVTET
-
pH 6.0, 37°C
0.0166
PLQVLTLNIERR
-
pH 6.0, 37°C
0.039
PPAILPIISE
-
pH 6.0, 37°C
0.0804 - 0.26
PRSSLYPALTP
0.121
PSEEYPIMID
-
pH 6.0, 37°C
0.315
QNYPIV
-
pH 6.0, 37°C, wild-type enzyme
0.216
RSLLYPALTP
-
pH 5.6, 37°C
0.0435
SDLVLLSAEARR
-
pH 6.0, 37°C
0.478
SQNYPIV
-
pH 6.0, 37°C, wild-type enzyme
1.022
SQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.05
TQTSLLIENSS
-
pH 5.6, 37°C, recombinant enzyme
0.0445
TQTSLLTLDDQ
-
pH 6.0, 37°C
0.524
VAQNYPIVQ
-
pH 6.0, 37°C
0.0384
VFQNYPIVQ
-
pH 6.0, 37°C
0.166
VGFAGAMAEAR
-
pH 6.0, 37°C
0.484
VKQNYPIVQ
-
pH 6.0, 37°C
0.0057
VLQNYPIVQ
-
pH 6.0, 37°C
0.0403
VMQNYPIVQ
-
pH 6.0, 37°C
0.514
VNQNYPIVQ
-
pH 6.0, 37°C
0.327
VSANYPIVQ
-
pH 6.0, 37°C
0.334
VSDNYPIVQ
-
pH 6.0, 37°C
0.0137
VSFNYPIVQ
-
pH 6.0, 37°C
0.233
VSGNYPIVQ
-
pH 6.0, 37°C
0.978
VSKNYPIVQ
-
pH 6.0, 37°C
0.0308
VSLQNYPIVQ
-
pH 6.0, 37°C
0.475
VSNNYPIVQ
-
pH 6.0, 37°C
0.154
VSQAYPIVQ
-
pH 6.0, 37°C
0.436
VSQDYPIVQ
-
pH 6.0, 37°C
0.0368
VSQFYPIVQ
-
pH 6.0, 37°C
0.114
VSQGYPIVQ
-
pH 6.0, 37°C
0.011
VSQIYPIVQ
-
pH 6.0, 37°C
0.0187
VSQLYPIVQ
-
pH 6.0, 37°C
0.242
VSQNFPIVQ
-
pH 6.0, 37°C
0.0311
VSQNLPIVQ
-
pH 6.0, 37°C
0.224
VSQNMPIVQ
-
pH 6.0, 37°C
1.385
VSQNYPAVQ
-
pH 6.0, 37°C
0.067
VSQNYPFVQ
-
pH 6.0, 37°C
1.808
VSQNYPIAQ
-
pH 6.0, 37°C
2.9
VSQNYPIEQ
-
pH 6.0, 37°C
0.048
VSQNYPIFQ
-
pH 6.0, 37°C
0.1396
VSQNYPIIQ
-
pH 6.0, 37°C
1.703
VSQNYPIQQ
-
pH 6.0, 37°C
1.573
VSQNYPIRQ
-
pH 6.0, 37°C
1.753
VSQNYPISQ
-
pH 6.0, 37°C
0.405
VSQNYPIV
-
pH 6.0, 37°C, wild-type enzyme
0.509
VSQNYPVVQ
-
pH 6.0, 37°C
0.183
VSQTYPIVQ
-
pH 6.0, 37°C
0.083
VSQVYPIVQ
-
pH 6.0, 37°C
0.135
VSVNYPIVQ
-
pH 6.0, 37°C
0.188
VTQNYPIVQ
-
pH 6.0, 37°C
0.082
VVQNYPIVQ
-
pH 6.0, 37°C
additional information
additional information
-
kinetic analysis
-
0.0299
MSKLLATVVS
-
pH 6.0, 37°C
0.05
MSKLLATVVS
-
pH 5.6, 37°C, recombinant enzyme
0.0804
PRSSLYPALTP
-
pH 6.0, 37°C
0.26
PRSSLYPALTP
-
pH 5.6, 37°C, recombinant enzyme
0.098
TSQAFPLRAG
-
pH 6.0, 37°C
0.22
TSQAFPLRAG
-
pH 5.6, 37°C, recombinant enzyme
0.03
TSTLLIENSS
-
pH 5.6, 37°C, recombinant enzyme
0.068
TSTLLIENSS
-
pH 6.0, 37°C
0.036
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.0388
VIQNYPIVQ
-
pH 6.0, 37°C
0.039
VIQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.061
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/A57I
0.134
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.174
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme L92I
0.0242
VQALVLTQ
-
pH 6.0, 37°C
0.04
VQALVLTQ
-
pH 5.6, 37°C, recombinant enzyme
0.0905
VSQNYPILQ
-
pH 6.0, 37°C
1.502
VSQNYPILQ
-
pH 6.0, 37°C
0.041
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme H37D
0.234
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V54I
0.261
VSQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.265
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme E15R
0.268
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.287
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/V54I
0.29
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme Y63V
0.356
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.456
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/A57I
1.238
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme L92I
2.046
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme W53I
0.01
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V54I
0.019
VSQNYPLVQ
-
pH 6.0, 37°C, wild-type enzyme
0.029
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.049
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.052
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V39I/V54I and V39I/A57I
0.074
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme L92I
0.467
VSQNYPLVQ
-
pH 6.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0963
APQVLPVMHP
-
pH 6.0, 37°C
0.027
Arg-Glu(EDANS)-Ser-Gln-Ala-Phe-Pro-Leu-Arg-Ala-Lys(dansyl)-Arg-OH
-
pH 5.6, 37°C, recombinant enzyme
0.209
DELILPVKRK
-
pH 6.0, 37°C
0.237
DSKAFLATDW
-
pH 6.0, 37°C
0.0882
LTFTFPVVFMRR
-
pH 6.0, 37°C
1.27
PKDIFPVTET
-
pH 6.0, 37°C
0.07
PLQVLTLNIERR
-
pH 6.0, 37°C
0.114
PPAILPIISE
-
pH 6.0, 37°C
0.415
PSEEYPIMID
-
pH 6.0, 37°C
0.017
QNYPIV
-
pH 6.0, 37°C, wild-type enzyme
0.55
RSLLYPALTP
-
pH 5.6, 37°C
0.061
SDLVLLSAEARR
-
pH 6.0, 37°C
0.455
SQNYPIV
-
pH 6.0, 37°C, wild-type enzyme
0.159
SQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.12
TQTSLLIENSS
-
pH 5.6, 37°C, recombinant enzyme
0.114
TQTSSLTLDDQ
-
pH 6.0, 37°C
0.262
VAQNYPIVQ
-
pH 6.0, 37°C
0.101
VFQNYPIVQ
-
pH 6.0, 37°C
0.08
VGFAGAMAEAR
-
pH 6.0, 37°C
0.478
VISQNYPIVQ
-
pH 6.0, 37°C
0.042
VKQNYPIVQ
-
pH 6.0, 37°C
0.0147
VLQNYPIVQ
-
pH 6.0, 37°C
0.028
VMQNYPIVQ
-
pH 6.0, 37°C
0.077
VNQNYPIVQ
-
pH 6.0, 37°C
0.182
VSANYPIVQ
-
pH 6.0, 37°C
0.068
VSDNYPIVQ
-
pH 6.0, 37°C
0.183
VSFNYPIVQ
-
pH 6.0, 37°C
0.1
VSGNYPIVQ
-
pH 6.0, 37°C
0.466
VSKNYPIVQ
-
pH 6.0, 37°C
0.023
VSLNYPIVQ
-
pH 6.0, 37°C
0.293
VSNNYPIVQ
-
pH 6.0, 37°C
0.185
VSQAYPIVQ
-
pH 6.0, 37°C
0.162
VSQDYPIVQ
-
pH 6.0, 37°C
0.087
VSQFYPIVQ
-
pH 6.0, 37°C
0.183
VSQIYPIVQ
-
pH 6.0, 37°C
0.017
VSQKYPIVQ
-
pH 6.0, 37°C
0.241
VSQLNYPIVQ
-
pH 6.0, 37°C
2.12
VSQNFPIVQ
-
pH 6.0, 37°C
0.037
VSQNLPIVQ
-
pH 6.0, 37°C
0.051
VSQNMPIVQ
-
pH 6.0, 37°C
0.036
VSQNYPAVQ
-
pH 6.0, 37°C
0.0063
VSQNYPFVQ
-
pH 6.0, 37°C
0.267
VSQNYPIAQ
-
pH 6.0, 37°C
0.124
VSQNYPIEQ
-
pH 6.0, 37°C
0.094
VSQNYPIFQ
-
pH 6.0, 37°C
0.266
VSQNYPIIQ
-
pH 6.0, 37°C
0.358
VSQNYPIKQ
-
pH 6.0, 37°C
0.081
VSQNYPILQ
-
pH 6.0, 37°C
0.209
VSQNYPIQQ
-
pH 6.0, 37°C
0.3
VSQNYPIRQ
-
pH 6.0, 37°C
0.15
VSQNYPISQ
-
pH 6.0, 37°C
0.852
VSQNYPIV
-
pH 6.0, 37°C, wild-type enzyme
0.345
VSQNYPVVQ
-
pH 6.0, 37°C
0.304
VSQTYPIVQ
-
pH 6.0, 37°C
0.054
VSQVYPIVQ
-
pH 6.0, 37°C
0.011
VSVNYPIVQ
-
pH 6.0, 37°C
0.393
VTQNYPIVQ
-
pH 6.0, 37°C
0.549
VVQNYPIVQ
-
pH 6.0, 37°C
0.29
MSKLLATVVS
-
pH 5.6, 37°C, recombinant enzyme
0.439
MSKLLATVVS
-
pH 6.0, 37°C
0.164
PRSSLYPALTP
-
pH 6.0, 37°C
0.53
PRSSLYPALTP
-
pH 5.6, 37°C, recombinant enzyme
0.38
TSQAFPLRAG
-
pH 5.6, 37°C, recombinant enzyme
0.714
TSQAFPLRAG
-
pH 6.0, 37°C
0.17
TSTLLIENSS
-
pH 5.6, 37°C, recombinant enzyme
0.294
TSTLLIENSS
-
pH 6.0, 37°C
0.012
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme H37D
0.065
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/A57I
0.12
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme L92I
0.22
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.4
VIQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.48
VIQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.279
VQALVLTQ
-
pH 6.0, 37°C
0.35
VQALVLTQ
-
pH 5.6, 37°C, recombinant enzyme
0.0442
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme L92I
0.072
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/A57I
0.075
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme H37D
0.2
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme Y63V
0.23
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.3
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzymes E15R and W53I
0.35
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V54I
0.46
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I/V54I
0.55
VSQNYPIVQ
-
pH 6.0, 37°C
0.55
VSQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
0.74
VSQNYPIVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.003
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V39I/A57I
0.023
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme H37D
0.062
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme A57I
0.11
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V39I/V54I
0.2
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V39I
0.24
VSQNYPLVQ
-
pH 6.0, 37°C, wild-type enzyme
0.34
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme L92I
0.661
VSQNYPLVQ
-
pH 6.0, 37°C
1.9
VSQNYPLVQ
-
pH 6.0, 37°C, mutant enzyme V54I
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.
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.
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.
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.
A57I
-
mutation has a strong influence on substrate specificity
C88T
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
E15R
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
G541R
-
size exclusion chromatography shows that the multimerization properties are similar among expressed wild-type and mutant ectodomain peptides. Circular dichroism measurements reveal decreased thermal stability of the G541R mutant as compared to wild-type. The G541R mutant also renders the peptide more susceptible to Lys-C protease cleavage. A monoclonal antibody does not bind to the G541R mutant peptide, suggesting a structural difference from wild-type
G60F
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
H37D
-
mutation has a strong influence on substrate specificity
V39I/V54I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
W53I
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
W53I/Q55G
-
mutant enzyme does not cleave the wild-type substrates: VSQNYPIVQ, VIQNYPIVQ and VSQNYPLVQ
A57V
99.7% of wild-type activity, 26.6% residual activity in presence of 1 microM amprenavir
K61L
10.3% of wild-type activity, 95% residual activity in presence of 1 microM amprenavir
V39I
23.5% of wild-type activity, 53% residual activity in presence of 1 microM amprenavir
V39I/A57V
27% of wild-type activity, no residual activity in presence of 1 microM amprenavir
Y90A/L92V
15.6% of wild-type activity, 81.7% residual activity in presence of 1 microM amprenavir
L92I
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
L92I
-
mutation has a strong influence on substrate specificity
V39I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
V39I
-
mutation has a strong influence on substrate specificity
V54I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
V54I
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
D32A
-
construction of an active site mutant which is inactive and more stable to degradation during recombinant expression and purification
D32A
-
construction of an active site mutant which is inactive and more stable to degradation during recombinant expression and purification
-
additional information
-
construction of truncation mutant protein Gag_DELTA1
additional information
-
construction of truncation mutant protein Gag_DELTA1
-
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.
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Boross, P.; Bagossi, P.; Copeland, T.D.; Oroszlan, S.; Louis, J.M.; Tozser, J.
Effect of substrate residues on the P2' preference of retroviral proteinases
Eur. J. Biochem.
264
921-929
1999
Moloney murine leukemia virus
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Shinnick, T.M.; Lerner, R.A.; Sutcliffe, J.G.
Nucleotide sequence of Moloney murine leukaemia virus
Nature
293
543-548
1981
Moloney murine leukemia virus (P03355)
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: Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase
Structure
3
879-892
1995
Moloney murine leukemia virus (P03355)
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Mutational analysis of the substrate binding pocket of murine leukemia virus protease and comparison with human immunodeficiency virus proteases
J. Biol. Chem.
270
29162-29168
1995
Moloney murine leukemia virus
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Kinetic and modeling studies of subsites S4-S3' of Moloney murine leukemia virus protease
J. Biol. Chem.
269
16795-16801
1994
Moloney murine leukemia virus
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Moloney murine leukemia virus protease: bacterial expression and characterization of the purified enzyme
Virology
196
557-563
1993
Moloney murine leukemia virus
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Bagossi, P.; Sperka, T.; Feher, A.; Kadas, J.; Zahuczky, G.; Miklossy, G.; Boross, P.; Toezser, J.
Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites
J. Virol.
79
4213-4218
2005
Moloney murine leukemia virus
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Menendez-Arias, L.; Tozser, J.; Oroszlan, S.
Moloney murine leukemia virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
176-178
2004
Moloney murine leukemia virus
-
brenda
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Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease
J. Gen. Virol.
87
1321-1330
2006
Moloney murine leukemia virus, Moloney murine leukemia virus MLV
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Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli
Protein Expr. Purif.
35
62-68
2004
murine leukemia virus, murine leukemia virus MLV
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Murine retrovirus escapes from murine APOBEC3 via two distinct novel mechanisms
Curr. Biol.
16
1565-1570
2006
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Schneider, W.M.; Zheng, H.; Cote, M.L.; Roth, M.J.
The MuLV 4070A G541R Env mutation decreases the stability and alters the conformation of the TM ectodomain
Virology
371
165-174
2008
Moloney murine leukemia virus
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Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site
J. Virol.
82
10111-10117
2008
Moloney murine leukemia virus
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Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease
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278
4413-4424
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Xenotropic MuLV-related virus
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NMR study of xenotropic murine leukemia virus-related virus protease in a complex with amprenavir
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425
284-289
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Xenotropic MuLV-related virus (A1Z651), Xenotropic MuLV-related virus isolate VP62 (A1Z651)
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Molecular and enzymatic characterization of XMRV protease by a cell-free proteolytic analysis
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75
4863-4873
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Maturation cleavage of the murine leukemia virus Env precursor separates the transmembrane subunits to prime it for receptor triggering
Proc. Natl. Acad. Sci. USA
109
7735-7740
2012
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