Information on EC 3.4.23.B5 - murine leukemia virus protease

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
murine leukemia virus protease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GAG-POL protein
UniProt
Manually annotated by BRENDA team
Gag-Pol polyprotein
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
APOBEC3 (A3G) + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
fluorescent substrate, contains a p12/CA cleavage site
-
-
?
DELILPVKRK + H2O
DELIL + PVKRK
show the reaction diagram
-
-
-
-
?
DSKAFLARDW + H2O
DSKAF + LARDW
show the reaction diagram
-
-
-
?
FLAG-pr55Gag + H2O
?
show the reaction diagram
-
-
-
?
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
human tumor suppressor protein ARL11 + H2O
?
show the reaction diagram
-
-
-
?
human tumor suppressor protein BAX + H2O
?
show the reaction diagram
-
-
-
?
human tumor suppressor protein DKK3 + H2O
?
show the reaction diagram
-
-
-
?
human tumor suppressor protein PTEN + H2O
?
show the reaction diagram
-
-
-
?
KARVnLNphEAnLG + H2O
KARVnL + NphEAnLG
show the reaction diagram
-
-
-
-
?
LTFTFPVVFMRR + H2O
LTFTF + PVVFMRR
show the reaction diagram
-
-
-
?
Lys-Ala-Arg-Val-Nle-Phe(4-nitro)-Glu-Ala-Nle-amide + H2O
?
show the reaction diagram
-
commercial chromogenic substrate
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
show the reaction diagram
PKDIFPVTET + H2O
PKDIF + PVTET
show the reaction diagram
-
-
-
?
PLQVLTLNIERR + H2O
PLQVL + TLNIERR
show the reaction diagram
-
contains a PR/RT cleavage site
-
-
?
PLQVLTLNIERR + H2O
PLQVLTL + NIERR
show the reaction diagram
-
-
-
?
PPAILPIISE + H2O
PPAIL + PIISE
show the reaction diagram
-
-
-
?
PRSSLYPALRTP + H2O
PRSSLY + PALRTP
show the reaction diagram
-
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
show the reaction diagram
PSEEYPIMID + H2O
PSEEY + PIMID
show the reaction diagram
-
-
-
?
QNYPIV + H2O
QNY + PIV
show the reaction diagram
-
-
-
?
R-peptide precursor Env + H2O
?
show the reaction diagram
-
-
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
show the reaction diagram
-
a P3 Leu-substituted peptide mimicking the MA/p12 cleavage site of Moloney murine leukemia virus proitease
-
-
?
SDLVLLSAEARR + H2O
SDLVL + LSAEARR
show the reaction diagram
-
-
-
?
SQNYPIV + H2O
SQNY + PIV
show the reaction diagram
-
-
-
?
SQNYPIVQ + H2O
SQNY + PIVQ
show the reaction diagram
-
-
-
?
TQTSLLIENSS + H2O
TQTSLL + IENSS
show the reaction diagram
-
contains a NC/PR cleavage site
-
-
?
TQTSLLTLDDQ + H2O
TQTSLL + TLDDQ
show the reaction diagram
-
-
-
?
TSQAFPLRAG + H2O
?
show the reaction diagram
-
-
-
-
?
TSQAFPLRAG + H2O
TSQAF + PLRAG
show the reaction diagram
TSTLLIENSS + H2O
TSTLL + IENSS
show the reaction diagram
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
-
?
VAQNYPIVQ-NH2 + H2O
VAQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VDQNYPIVQ + H2O
VDQNY + PIVQ
show the reaction diagram
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VFQNYPIVQ-NH2 + H2O
VFQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VGFAGAMAEAE + H2O
VGFAG + AMAEAE
show the reaction diagram
-
-
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
show the reaction diagram
VIQNYPIVQ-NH2 + H2O
VISQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VKQNYPIVQ-NH2 + H2O
VKQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VLQNYPIVQ-NH2 + H2O
VLQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VMQNYPIVQ-NH2 + H2O
VMQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VNQNYPIVQ-NH2 + H2O
VNQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
show the reaction diagram
VSANYPIVQ-NH2 + H2O
VSANY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSDNYPIVQ-NH2 + H2O
VSDNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSFNYPIVQ-NH2 + H2O
VSFNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSGNYPIVQ-NH2 + H2O
VSGNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSKNYPIVQ-NH2 + H2O
VSKNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSLNYPIVQ-NH2 + H2O
VSLNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSNNYPIVQ-NH2 + H2O
VSNNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQAYPIVQ-NH2 + H2O
VSQAY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQDYPIVQ-NH2 + H2O
VSQDY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQFYPIVQ-NH2 + H2O
VSQFY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQGYPIVQ-NH2 + H2O
VSQGY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQIYPIVQ-NH2 + H2O
VSQIY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQLNYPIVQ-NH2 + H2O
VSQLY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
show the reaction diagram
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
show the reaction diagram
VSQNLPIVQ + H2O
VSQNL + PIVQ
show the reaction diagram
VSQNMPIVQ + H2O
VSQNM + PIVQ
show the reaction diagram
VSQNYPAVQ-NH2 + H2O
VSQNY + PAVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPFVQ-NH2 + H2O
VSQNY + PFVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIAQ-NH2 + H2O
VSQNY + PIAQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIEQ-NH2 + H2O
VSQNY + PIWQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIFQ-NH2 + H2O
VSQNY + PIFQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIIQ-NH2 + H2O
VSQNY + PIIQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIKQ-NH2 + H2O
VSQNY + PIKQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPILQ-NH2 + H2O
VSQNY + PILQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIQQ-NH2 + H2O
VSQNY + PIQQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIRQ-NH2 + H2O
VSQNY + PIRQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPISQ-NH2 + H2O
VSQNY + PISQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPIV + H2O
VSQNY + PIV
show the reaction diagram
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
show the reaction diagram
VSQNYPIVQ-NH2 + H2O
VSQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPLVQ + H2O
VSQNY + PLVQ
show the reaction diagram
VSQNYPLVQ-NH2 + H2O
VSQNY + PLVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQNYPVVQ-NH2 + H2O
VSQNY + PVVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQTYPIVQ-NH2 + H2O
VSQTY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSQVYPIVQ-NH2 + H2O
VSQVY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VSVNYPIVQ-NH2 + H2O
VSVNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
show the reaction diagram
VTQNYPIVQ-NH2 + H2O
VTQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
VVQNYPIVQ-NH2 + H2O
VVQNY + PIVQ-NH2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gag polyprotein + H2O
?
show the reaction diagram
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
Gag-Pol polyprotein + H2O
?
show the reaction diagram
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-pepstatin A
-
IC50: 0.025 mM
amprenavir
atanazavir
-
-
-
atazanavir
-
-
pepstatin A
-
-
TL-3
-
universal inhibitor of retroviral proteases
UK88947
-
IC50: 0.0022 mM
additional information
-
inhibition profile
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
APQVLPVMHP
-
pH 6.0, 37C
0.0846
DELILPVKRK
-
pH 6.0, 37C
0.2
DSKAFLATDW
-
pH 6.0, 37C
0.0192
LTFTFPVVFMRR
-
pH 6.0, 37C
0.0299 - 0.05
MSKLLATVVS
0.51
PKDIFPVTET
-
pH 6.0, 37C
0.0166
PLQVLTLNIERR
-
pH 6.0, 37C
0.039
PPAILPIISE
-
pH 6.0, 37C
0.0804 - 0.26
PRSSLYPALTP
0.121
PSEEYPIMID
-
pH 6.0, 37C
0.315
QNYPIV
-
pH 6.0, 37C, wild-type enzyme
0.216
RSLLYPALTP
-
pH 5.6, 37C
0.0435
SDLVLLSAEARR
-
pH 6.0, 37C
0.478
SQNYPIV
-
pH 6.0, 37C, wild-type enzyme
1.022
SQNYPIVQ
-
pH 6.0, 37C, wild-type enzyme
0.05
TQTSLLIENSS
-
pH 5.6, 37C, recombinant enzyme
0.0445
TQTSLLTLDDQ
-
pH 6.0, 37C
0.098 - 0.22
TSQAFPLRAG
0.03 - 0.068
TSTLLIENSS
0.524
VAQNYPIVQ
-
pH 6.0, 37C
0.0384
VFQNYPIVQ
-
pH 6.0, 37C
0.166
VGFAGAMAEAR
-
pH 6.0, 37C
0.036 - 0.174
VIQNYPIVQ
0.484
VKQNYPIVQ
-
pH 6.0, 37C
0.0057
VLQNYPIVQ
-
pH 6.0, 37C
0.0403
VMQNYPIVQ
-
pH 6.0, 37C
0.514
VNQNYPIVQ
-
pH 6.0, 37C
0.0242 - 0.04
VQALVLTQ
0.327
VSANYPIVQ
-
pH 6.0, 37C
0.334
VSDNYPIVQ
-
pH 6.0, 37C
0.0137
VSFNYPIVQ
-
pH 6.0, 37C
0.233
VSGNYPIVQ
-
pH 6.0, 37C
0.978
VSKNYPIVQ
-
pH 6.0, 37C
0.0308
VSLQNYPIVQ
-
pH 6.0, 37C
0.475
VSNNYPIVQ
-
pH 6.0, 37C
0.154
VSQAYPIVQ
-
pH 6.0, 37C
0.436
VSQDYPIVQ
-
pH 6.0, 37C
0.0368
VSQFYPIVQ
-
pH 6.0, 37C
0.114
VSQGYPIVQ
-
pH 6.0, 37C
0.011
VSQIYPIVQ
-
pH 6.0, 37C
0.0187
VSQLYPIVQ
-
pH 6.0, 37C
0.242
VSQNFPIVQ
-
pH 6.0, 37C
0.0311
VSQNLPIVQ
-
pH 6.0, 37C
0.224
VSQNMPIVQ
-
pH 6.0, 37C
1.385
VSQNYPAVQ
-
pH 6.0, 37C
0.067
VSQNYPFVQ
-
pH 6.0, 37C
1.808
VSQNYPIAQ
-
pH 6.0, 37C
2.9
VSQNYPIEQ
-
pH 6.0, 37C
0.048
VSQNYPIFQ
-
pH 6.0, 37C
0.1396
VSQNYPIIQ
-
pH 6.0, 37C
0.0905 - 1.502
VSQNYPILQ
1.703
VSQNYPIQQ
-
pH 6.0, 37C
1.573
VSQNYPIRQ
-
pH 6.0, 37C
1.753
VSQNYPISQ
-
pH 6.0, 37C
0.405
VSQNYPIV
-
pH 6.0, 37C, wild-type enzyme
0.041 - 2.046
VSQNYPIVQ
0.01 - 0.467
VSQNYPLVQ
0.509
VSQNYPVVQ
-
pH 6.0, 37C
0.183
VSQTYPIVQ
-
pH 6.0, 37C
0.083
VSQVYPIVQ
-
pH 6.0, 37C
0.135
VSVNYPIVQ
-
pH 6.0, 37C
0.188
VTQNYPIVQ
-
pH 6.0, 37C
0.082
VVQNYPIVQ
-
pH 6.0, 37C
additional information
additional information
-
kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0963
APQVLPVMHP
Moloney murine leukemia virus
-
pH 6.0, 37C
0.027
Arg-Glu(EDANS)-Ser-Gln-Ala-Phe-Pro-Leu-Arg-Ala-Lys(dansyl)-Arg-OH
Moloney murine leukemia virus
-
pH 5.6, 37C, recombinant enzyme
0.209
DELILPVKRK
Moloney murine leukemia virus
-
pH 6.0, 37C
0.237
DSKAFLATDW
Moloney murine leukemia virus
-
pH 6.0, 37C
0.0882
LTFTFPVVFMRR
Moloney murine leukemia virus
-
pH 6.0, 37C
0.29 - 0.439
MSKLLATVVS
1.27
PKDIFPVTET
Moloney murine leukemia virus
-
pH 6.0, 37C
0.07
PLQVLTLNIERR
Moloney murine leukemia virus
-
pH 6.0, 37C
0.114
PPAILPIISE
Moloney murine leukemia virus
-
pH 6.0, 37C
0.164 - 0.53
PRSSLYPALTP
0.415
PSEEYPIMID
Moloney murine leukemia virus
-
pH 6.0, 37C
0.017
QNYPIV
Moloney murine leukemia virus
-
pH 6.0, 37C, wild-type enzyme
0.55
RSLLYPALTP
XMRV
-
pH 5.6, 37C
0.061
SDLVLLSAEARR
Moloney murine leukemia virus
-
pH 6.0, 37C
0.455
SQNYPIV
Moloney murine leukemia virus
-
pH 6.0, 37C, wild-type enzyme
0.159
SQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C, wild-type enzyme
0.12
TQTSLLIENSS
Moloney murine leukemia virus
-
pH 5.6, 37C, recombinant enzyme
0.114
TQTSSLTLDDQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.38 - 0.714
TSQAFPLRAG
0.17 - 0.294
TSTLLIENSS
0.262
VAQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.101
VFQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.08
VGFAGAMAEAR
Moloney murine leukemia virus
-
pH 6.0, 37C
0.012 - 0.48
VIQNYPIVQ
0.478
VISQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.042
VKQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.0147
VLQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.028
VMQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.077
VNQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.279 - 0.35
VQALVLTQ
0.182
VSANYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.068
VSDNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.183
VSFNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.1
VSGNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.466
VSKNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.023
VSLNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.293
VSNNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.185
VSQAYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.162
VSQDYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.087
VSQFYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.183
VSQIYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.017
VSQKYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.241
VSQLNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
2.12
VSQNFPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.037
VSQNLPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.051
VSQNMPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.036
VSQNYPAVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.0063
VSQNYPFVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.267
VSQNYPIAQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.124
VSQNYPIEQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.094
VSQNYPIFQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.266
VSQNYPIIQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.358
VSQNYPIKQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.081
VSQNYPILQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.209
VSQNYPIQQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.3
VSQNYPIRQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.15
VSQNYPISQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.852
VSQNYPIV
Moloney murine leukemia virus
-
pH 6.0, 37C, wild-type enzyme
0.0442 - 0.74
VSQNYPIVQ
0.003 - 1.9
VSQNYPLVQ
0.345
VSQNYPVVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.304
VSQTYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.054
VSQVYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.011
VSVNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.393
VTQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
0.549
VVQNYPIVQ
Moloney murine leukemia virus
-
pH 6.0, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.55
RSLLYPALTP
XMRV
-
pH 5.6, 37C
41948
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000002 - 0.00001
amprenavir
0.0000018 - 0.000022
atazanavir
0.00000014
DMP323
-
pH 5.6, 37C, recombinant enzyme
0.00000021
indinavir
-
pH 5.6, 37C, recombinant enzyme
0.0000019
KH-164
-
pH 5.6, 37C, recombinant enzyme
0.000002
nelfinavir
-
pH 5.6, 37C, recombinant enzyme
0.00144
pepstatin A
-
substrate RSLLYPALTP, pH 5.6, 37C
0.00000041
ritonavir
-
pH 5.6, 37C, recombinant enzyme
0.000028
saquinavir
-
pH 5.6, 37C, recombinant enzyme
0.000102
TL-3
-
substrate RSLLYPALTP, pH 5.6, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
acetyl-pepstatin A
Moloney murine leukemia virus
-
IC50: 0.025 mM
0.0022
UK88947
Moloney murine leukemia virus
-
IC50: 0.0022 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00054
-
purified recombinant non-tagged enzyme
0.00112
-
purified recombinant His-tagged enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 7.5
-
pH 4.3: about 60% of maximal activity, pH 7.5: about 40% of maximal activity, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13315
-
2 * 13315, sequence calculation, homodimer, structure molecular modeling
14000
x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends
14100
-
purified recombinant enzyme, MALDI-TOF mass spectrometry
17000
x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 17000 and x * 14000, SDS-PAGE, corresponding to the expected mobility of the full-length protease and the truncated form by auto-cleavage of the flanking 20 amino acids at both ends
dimer
-
2 * 13315, sequence calculation, homodimer, structure molecular modeling
additional information
-
structure molecular modeling, S2 subsite sequence comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the enzyme performs autolytic processing of precursor protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of protease in complex with amprenavir. The amino acids at the active site of HIV-1, HTLV proteases and those likely to be at the active site of XMRV protease are comparatively conserved. Amprenavir interacts with residue Asp32 of the catalytic domain, and also contacts the residues Val39, Lys61, Tyr90, and Leu92. A water molecule would intermediate interactions between amprenavir and Ala57
in complex with inhibitors amprenavir, pepstatin A and TL-3, to 1.75, 1.5 and 1.4 A resolution, respectively. TL-3 and amprenavir bind in a predictable manner, spanning the substrate-binding site of the enzyme, while two molecules of pepstatin A bind simultaneously, leaving the catalytic water molecule in place
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by acetobne precipitation and extraction, overview, recombinnat enzyme with C-terminal GGSIEGR
-
expression as His-tagged maltose-binding protein fusion enzyme from Escherichia coli, the fusion protein is cleaved off
-
native enzyme partially, recombinant enzyme to homogeneity from Escherichia coli
-
recombinant enzyme in fusion with the glutathione S-transferase from Schistosoma japonicum
-
recombinant maltose-binding protein fusion enzyme from Escherichia coli strains DH5alpha and BL21, with or without His-tag, by amylose or nickel affinity chromatography, the fusion protein is cleaved of by factor Xa followed by cation exchange chromatography, non-His-tagged MBP-fusion-enzyme 2.6fold and His-tagged MBP-fusion enzyme 16.6fold to homogeneity, optimization of the purification method to diminish protein degradation, overview
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the prokaryotic expression vector pGEX-2T, expression in fusion with the glutathione S-transferase from Schistosoma japonicum
-
expression as His-tagged maltose-binding protein fusion enzyme in Escherichia coli, phylogenetic tree
-
expression as His-tagged maltose-binding protein fusion protein in Escherichia coli strains DH5alpha, CAG597, and BL21, optimization of the expression method to diminish protein degradation, overview, expression of His-tagged mutant D32A
-
expression in Escherichia coli
-
expression in Escherichia coli fused to TrpE or to glutathione S-transferase from Schistosoma japonicum
-
expression in Escherichia coli, wild-type and mutant enzymes are expressed in fusion with the Schistosoma japonicum glutathione S-transferase
-
expression in wheat-germ cell-free system
expression of the enzyme with C-terminal GGSIEGR
-
tansmembrane ectodomain of of MuLV is expressed as a His-tagged fusion protein in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
L92I
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs; mutation has a strong influence on substrate specificity
V39I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme; mutation has a strong influence on substrate specificity
V39I/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; 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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of an in vitro enzymatic assay system to characterize XMRV protease-mediated cleavage of host-cell proteins