3.4.23.B5: murine leukemia virus protease
This is an abbreviated version!
For detailed information about murine leukemia virus protease, go to the full flat file.
Word Map on EC 3.4.23.B5
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3.4.23.B5
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mulvs
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readthrough
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polyproteins
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oligopeptides
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envelope
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pr65gag
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single-chain
-
pseudotyped
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subsites
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amber
-
cell-cell
-
junction
-
leukaemia
-
analysis
- 3.4.23.B5
- mulvs
-
readthrough
- polyproteins
- oligopeptides
- envelope
-
pr65gag
-
single-chain
-
pseudotyped
-
subsites
-
amber
-
cell-cell
- junction
-
leukaemia
- analysis
Reaction
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins =
Synonyms
MLV PR, MLV protease, MLV retropepsin, MMLV protease, Mo-MuLV PR, Mo-MuLV protease, Moloney MLV retropepsin, Moloney murine leukemia virus protease, Moloney murine leukemia virus retropepsin, More, MuLV 4070A, MuLV proteinase, murine leukemia virus protease, viral protease, vPR
ECTree
3.4.23.B5 murine leukemia virus proteaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.B5 - murine leukemia virus protease
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
APOBEC3 (A3G) + H2O
?
-
viral protease cleaves antiviral host factor APOBEC3 (A3) after maturation of virions in mice and thereby escapes from its antiviral activity
-
-
?
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
-
-
?
human tumor suppressor protein ARL11 + H2O
?
-
-
-
?
human tumor suppressor protein DKK3 + H2O
?
-
-
-
?
human tumor suppressor protein PTEN + H2O
?
-
-
-
?
Lys-Ala-Arg-Val-Nle-Phe(4-nitro)-Glu-Ala-Nle-amide + H2O
?
-
commercial chromogenic substrate
-
-
?
PLQVLTLNIERR + H2O
PLQVL + TLNIERR
-
contains a PR/RT cleavage site
-
-
?
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
-
-
?
TQTSLLIENSS + H2O
TQTSLL + IENSS
-
contains a NC/PR cleavage site
-
-
?
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
-
-
-
-
?
VDQNYPIVQ + H2O
VDQNY + PIVQ
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
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
?
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
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contains a CA/NC cleavage site
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
-
contains a CA/NC cleavage site
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
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contains a MA/p12 cleavage site, low activity
-
-
?
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
-
contains a RT/IN cleavage site
-
-
?
TSTLLIENSS + H2O
TSTLL + IENSS
-
contains a RT/IN cleavage site
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
-
contains a p12E/p2E cleavage site
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
-
contains a p12E/p2E cleavage site
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
-
Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
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
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
-
medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
additional information
?
-
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activity of recombinant enzyme with recombinant Gag protein fragments, overview
-
-
?
additional information
?
-
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cleavage site and substrate specificity, overview
-
-
?
additional information
?
-
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study of influence of the P2 position residue on cleavage site specificity, overview
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-
?
additional information
?
-
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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
-
-
?
