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Information on EC 3.4.23.B5 - murine leukemia virus protease and Organism(s) Moloney murine leukemia virus and UniProt Accession P03355
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3.4.23.B5 murine leukemia virus proteaseSpecify your search results
Word Map
- 3.4.23.B5
- mulvs
-
readthrough
- polyproteins
- oligopeptides
- envelope
-
pr65gag
-
single-chain
-
pseudotyped
-
subsites
-
amber
-
cell-cell
- junction
-
leukaemia
- analysis
The taxonomic range for the selected organisms is: Moloney murine leukemia virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mo-mulv pr, mlv protease, mlv pr, mulv 4070a, moloney murine leukemia virus protease, mo-mulv protease, murine leukemia virus protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mo-MuLV PR
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-
-
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Mo-MuLV protease
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-
-
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Moloney murine leukemia virus protease
-
-
-
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MuLV proteinase
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-
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additional information
-
the enzyme belongs to the A2 peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
structure-based molecular modeling of reaction mechanism and substrate binding
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processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
substrate binding pocket residues are His37, Val39, and Ala57
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
144114-21-6
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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
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
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fluorescent substrate, contains a p12/CA cleavage site
-
-
?
Lys-Ala-Arg-Val-Nle-Phe(4-nitro)-Glu-Ala-Nle-amide + H2O
?
-
commercial chromogenic substrate
-
-
?
PLQVLTLNIERR + H2O
PLQVL + TLNIERR
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contains a PR/RT cleavage site
-
-
?
TQTSLLIENSS + H2O
TQTSLL + IENSS
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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
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medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
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Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
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-
?
Gag polyprotein + H2O
?
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processing to mature proteins, autolysis of the retropepsin
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-
?
Gag polyprotein + H2O
?
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autolysis of the retropepsin from the precursor protein
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-
?
Gag-Pol polyprotein + H2O
?
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processing to mature proteins, autolysis of the retropepsin
-
-
?
MSKLLATVVS + H2O
MSKLL + ATVVS
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contains a CA/NC cleavage site
-
-
?
PRSSLYPALTP + H2O
PRSSLY + PALTP
-
contains a MA/p12 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
-
-
?
VQALVLTQ + H2O
VQAL + VLTQ
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contains a p12E/p2E cleavage site
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
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Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
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Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
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Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
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a HIV-1 retropepsin substrate
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
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medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
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Phe, Tyr, Leu or Met, Ala in order of decreasing efficiency, at position P1
-
-
?
VTQNYPIVQ + H2O
VTQNY + PIVQ
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medium-sized polar residues (Ser, Thr, and Asp) are preferred at position P4
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-
?
additional information
?
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activity of recombinant enzyme with recombinant Gag protein fragments, overview
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-
?
additional information
?
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cleavage site and substrate specificity, overview
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?
additional information
?
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study of influence of the P2 position residue on cleavage site specificity, overview
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-
?
NATURAL SUBSTRATE
NATURAL 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
Gag polyprotein + H2O
?
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing to mature proteins, autolysis of the retropepsin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis
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0.052
VSQNYPLVQ
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pH 6.0, 37°C, mutant enzyme V39I/V54I and V39I/A57I
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
Arg-Glu(EDANS)-Ser-Gln-Ala-Phe-Pro-Leu-Arg-Ala-Lys(dansyl)-Arg-OH
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pH 5.6, 37°C, recombinant enzyme
0.55
VSQNYPIVQ
-
pH 6.0, 37°C, wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13315
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2 * 13315, sequence calculation, homodimer, structure molecular modeling
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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2 * 13315, sequence calculation, homodimer, structure molecular modeling
additional information
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structure molecular modeling, S2 subsite sequence comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme performs autolytic processing of precursor protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
V39I
V39I/V54I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
V54I
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
additional information
-
construction of truncation mutant protein Gag_DELTA1
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by acetobne precipitation and extraction, overview, recombinnat enzyme with C-terminal GGSIEGR
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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
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recombinant enzyme in fusion with the glutathione S-transferase from Schistosoma japonicum
-
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 in Escherichia coli fused to TrpE or to glutathione S-transferase from Schistosoma japonicum
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expression in Escherichia coli, wild-type and mutant enzymes are expressed in fusion with the Schistosoma japonicum glutathione S-transferase
-
tansmembrane ectodomain of of MuLV is expressed as a His-tagged fusion protein in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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)
Georgiadis, M.M.; Jessen, S.M.; Ogata, C.M.; Telesnitsky, A.; Goff, S.P.; Hendrickson W.A.
: 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)
Menendez-Arias, L.; Weber, I.T.; Oroszlan, S.
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
Menendez-Arias, L.; Weber, I.T.; Soss, J.; Harrison, R.W.; Gotte, D.; Oroszlan, S.
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
Menendez-Arias, L.; Gotte, D.; Oroszlan, S.
Moloney murine leukemia virus protease: bacterial expression and characterization of the purified enzyme
Virology
196
557-563
1993
Moloney murine leukemia virus
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
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
-
Feher, A.; Boross, P.; Sperka, T.; Miklossy, G.; Kadas, J.; Bagossi, P.; Oroszlan, S.; Weber, I.T.; Toezser, J.
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
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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