3.4.23.B10: Rous sarcoma virus retropepsin
This is an abbreviated version!
For detailed information about Rous sarcoma virus retropepsin, go to the full flat file.
Word Map on EC 3.4.23.B10
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3.4.23.B10
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polyproteins
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virion
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viruses
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retroviruses
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retroviral
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nucleocapsid
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transcriptase
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leukemia
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virus-like
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antiretroviral
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gag-pol
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sars-cov-2
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noninfectious
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moloney
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proviral
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mason-pfizer
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poliovirus
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pr55gag
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integrase
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nonstructural
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lentiviruses
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dengue
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encapsidation
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coronavirus
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virological
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ns2b
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ns2b-ns3
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nelfinavir
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lopinavir
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fiv
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coxsackievirus
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picornaviruses
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m-mulv
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virion-associated
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flaviviruses
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autoprocessing
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boceprevir
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noroviruses
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3cpro
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vp4
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saquinavir
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picornaviral
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indinavir
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myristylation
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3c-like
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mulvs
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conical
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amprenavir
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analysis
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ritonavir
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telaprevir
- 3.4.23.B10
- polyproteins
- virion
- viruses
- retroviruses
-
retroviral
-
nucleocapsid
- transcriptase
- leukemia
-
virus-like
-
antiretroviral
- gag-pol
- sars-cov-2
-
noninfectious
-
moloney
-
proviral
-
mason-pfizer
- poliovirus
-
pr55gag
-
integrase
-
nonstructural
- lentiviruses
- dengue
-
encapsidation
- coronavirus
-
virological
- ns2b
-
ns2b-ns3
- nelfinavir
- lopinavir
- fiv
- coxsackievirus
- picornaviruses
- m-mulv
-
virion-associated
- flaviviruses
-
autoprocessing
- boceprevir
- noroviruses
- 3cpro
- vp4
- saquinavir
-
picornaviral
- indinavir
-
myristylation
-
3c-like
- mulvs
-
conical
- amprenavir
- analysis
- ritonavir
- telaprevir
Reaction
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 =
Synonyms
AMV PR, AMV/RSV PR, avian myeloblastosis virus protease, avian myeloblastosis virus retropepsin, capsid protein P27, core protein P10, core protein P19, core protein P2A, core protein P2B, Gag polyprotein, Gag polyprotein p10 sequence, inner coat protein P12, More, p10-CA protease, p10-capsid protease, p15 protein, protease P15, Rous sarcoma virus protease, Rous sarcoma virus retropepsin, RSV PR, RSV protease, RSV/AMV retropepsin, viral protease
ECTree
3.4.23.B10 Rous sarcoma virus retropepsinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.B10 - Rous sarcoma virus retropepsin
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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
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
-
?
PATIMMORERR + H2O
PATIM + MORERR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
PGNFLQSRR + H2O
PGNF + LQSRR
-
reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
-
?
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
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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
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVSLAYMRR + H2O
PPAVS + LAYTMRR
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVWLAMTMRR + H2O
PPAVW + LAMTMRR
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPAVYLAMTMRR + H2O
PPAVY + LAMTMRR
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPDVSLAMTMRR + H2O
PPDVS + LAMTMRR
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slight increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPFVSLAMTMRR + H2O
PPFVS + LAMTMRR
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increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
PPRVSLAMTMRR + H2O
PPRVS + LAMTMRR
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
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
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
TLNFPISPKK + H2O
TLNF + PISPKK
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slow cleavage with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
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medium-sized or large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VSFNFPQITKK + H2O
VSFNF + PQITKK
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reaction with mutant enzyme S38T/I42D/I44V/M73V/A100L/L104T/R105P/G106V/S107N
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
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Phe and Leu are preferred at position P3
-
-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
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Phe and Leu are preferred at position P3
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
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preference order for P1 position is Phe > Tyr > Leu, Met > Ala
-
-
?
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
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
synthetic peptide substrate, required features, overview
-
-
?
PPAVSLAMTMRR + H2O
PPAVS + LAMTMRR
-
synthetic peptide substrate, required features, overview
-
-
?
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
-
increase in activity of wild-type enzyme compared to PPAVSLAMTMRR
-
-
?
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
?
-
-
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
-
-
?
