Information on EC 3.4.23.B6 - Mason-Pfizer monkey virus proteinase

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The expected taxonomic range for this enzyme is: Mason-Pfizer monkey virus

EC NUMBER
COMMENTARY hide
3.4.23.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Mason-Pfizer monkey virus proteinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme cleaves 17 amino acids of the C-terminal 38-amino-acid cytoplasmic tail of the transmembrane protein TM of the released immature virus.
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATHQVYNphVRKA + H2O
hydrolyzed peptid
show the reaction diagram
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the cysteine residues in M-PMV protease form an intramolecular disulfide bridge and that increases the proteolytic activity significantly
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?
ATPQVYF(NO2)VRKA + H2O
?
show the reaction diagram
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-
-
-
?
ATPQVYF(NO2)VRKA + H2O
ATPQVY + F(NO2)VRKA
show the reaction diagram
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-
-
-
?
CA-NC fusion protein + H2O
?
show the reaction diagram
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-
-
-
?
capsid protein + H2O
?
show the reaction diagram
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cleaved in vitro within the major homology region
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-
?
capsid-nucleocapsid fusion protein + H2O
capsid protein + nucleocapsid protein
show the reaction diagram
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-
-
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?
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
GPEPPAVSLAMTDHK + H2O
GPEPPAVS + LAMTDHK
show the reaction diagram
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-
-
-
?
IMMCSPNDI + H2O
IMMCS + PNDI
show the reaction diagram
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-
-
-
?
IQVHYHRLEQ + H2O
IQVH + YHRLEQ
show the reaction diagram
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gp22-derived peptide, peptide derived from the cytoplasmic domain of transmembrane protein TM
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-
?
NC protein + H2O
?
show the reaction diagram
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cleaved in several sites at the N-terminus
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-
?
PKDIFPVTET + H2O
PKDIF + PVTET
show the reaction diagram
PKQAYGAVFV + H2O
PKQAY + GAVFV
show the reaction diagram
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-
-
-
?
PKSIFPVTET + H2O
PKSIF + PVTET
show the reaction diagram
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-
-
-
?
QGTVSFNFPQITLVWOK + H2O
QGTVSFNF + PQITLVWOK
show the reaction diagram
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-
-
-
?
SSDIYWVQPI + H2O
SSDIY + WVQPI
show the reaction diagram
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-
-
-
?
TGPPVVAMPVVIKTEG + H2O
TGPPVVAM + PVVIKTEG
show the reaction diagram
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-
-
-
?
transmembrane glycoprotein + H2O
?
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
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-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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low activity
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-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
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-
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?
VFQNYPIVQ + H2O
VFQNY + PIVQ
show the reaction diagram
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large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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?
VIQNYPIVQ + H2O
VIQNY + PIVQ
show the reaction diagram
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large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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?
VLQNYPIVQ + H2O
VLQNY + PIVQ
show the reaction diagram
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large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
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?
VSFNYPIVQ + H2O
VSFNY + PIVQ
show the reaction diagram
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pronounced preference for the large hydrophobic residues Phe and Leu at position P3
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?
VSLNYPIVQ + H2O
VSLNY + PIVQ
show the reaction diagram
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pronounced preference for the large hydrophobic residues Phe and Leu at position P3
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?
VSQNFPIVQ + H2O
VSQNF + PIVQ
show the reaction diagram
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large aromatic residues (Phe and Tyr) are preferred at position P1
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?
VSQNYPIVQ + H2O
VSQNY + PIVQ
show the reaction diagram
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large aromatic residues (Phe and Tyr) are preferred at position P1
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?
additional information
?
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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
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processing of the precursor protein into mature proteins and the functional protease
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?
Gag-Pol polyprotein + H2O
?
show the reaction diagram
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processing of the precursor protein into mature proteins and the functional protease
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?
transmembrane glycoprotein + H2O
?
show the reaction diagram
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cleavage site is in the cytoplasmic domain of the protein. Cleavage takes place as a postbudding event
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PCV-phenylstatine-AMT
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PMV-phenylstatine-VRP
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PPAV-cysteinestatine-AMTM
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PPCV-phenylstatine-AMTM
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PPYV-phenylstatine-AMTM
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PYV-phenylstatine-AMT
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RPMV-phenylstatine-VMP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
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activates at 2 M
additional information
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proteolytic activity within the M-PMV Pr95Gag-Pro precursor is effectively suppressed within an assembled immature capsid, but with addition of dithiothreitol, there is a dramatic increase in protease activity. The activation of the protease results in the cleavage of p17 from the Pr95 precursor as a primary event, followed by processing of the Gag polyproteins into other mature viral proteins
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.417
APTVMAVVNP
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pH 5.3, 37°C
0.386 - 0.42
ATHQVYNphVRKA
0.0034 - 1.7
ATPQVYF(NO2)VRKA
0.136 - 1.076
IQVHYHRLEQ
0.517
PKDIFPVTET
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pH 5.3, 37°C
0.298
PKQAYGAVFV
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pH 5.3, 37°C
0.038
SSDIYWVQPI
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pH 5.3, 37°C
additional information
additional information
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Km-values for peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.65
APTVMAVVNP
Mason-Pfizer monkey virus
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pH 5.3, 37°C
0.1 - 7
ATPQVYF(NO2)VRKA
0.053 - 0.43
IQVHYHRLEQ
7.6
PKDIFPVTET
Mason-Pfizer monkey virus
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pH 5.3, 37°C
7.7
PKQAYGAVFV
Mason-Pfizer monkey virus
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pH 5.3, 37°C
4.56
SSDIYWVQPI
Mason-Pfizer monkey virus
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pH 5.3, 37°C
additional information
additional information
Mason-Pfizer monkey virus
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turnover-numbers for peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006
PCV-phenylstatine-AMT
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pH 5.3, 37°C
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0.00028
PMV-phenylstatine-VRP
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pH 5.3, 37°C
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0.013
PPAV-cysteinestatine-AMTM
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pH 5.3, 37°C
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0.0031
PPCV-phenylstatine-AMTM
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pH 5.3, 37°C
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0.00003
PPYV-phenylstatine-AMTM
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pH 5.3, 37°C
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0.000003
PYV-phenylstatine-AMT
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pH 5.3, 37°C
0.00005
RPMV-phenylstatine-VMP
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pH 5.3, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
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enzyme form p13, isoelectric focusing
8.1
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enzyme form p12, isoelectric focusing
9.2
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enzyme form p17, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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transfection of COS-1 cells with the proviral construct
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12250
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three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscopy: 12246 Da, 12956 Da and 16965 Da
12960
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three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscop: 12246 Da, 12956 Da and 16965 Da
16970
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three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscop: 12246 Da, 12956 Da and 16965 Da
26000
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x * 26000, recombinant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 12000, isozyme p12, 2 * 13000, isozyme p13, 2 * 17000, isozyme p17
homodimer
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The active form of the protease is a homodimer with a single active site. The two subunits are stabilized by hydrogen bonding interactions within the fourstranded antiparallel beta-sheet. Substrate binding stabilizes the dimer.
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure determination of p12 mutant D26N/C7A/C106A
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NMR structure of a fully folded monomer of a 12000 Da M-PMV protease and of a C7A/D26N/C106A mutant
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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the 13000 Da enzyme is stable
646010
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
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the 13000 Da wild-type enzyme (which exhibits higher catalytic activity) loses 50% activity at 3.4 M urea, the midpoint of the urea unfolding curve of the 12000 Da truncated enzyme is at 1.9 M urea, the denaturation curve for the C7A/C106A mutant is no longer sigmoidal in character, confirming that this mutant is very unstable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 13000 Da enzyme form is stable at pH 6.4 and at salt concentrations lower than 0.1 M
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4°C, pH 5.5, the 17000 Da species is self-processed slowly into the 12000 Da form and the 5000 Da peptide
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the mixture of 17000 Da and 13000 Da enzyme, purified on QAE-Sephadex, is stable in Tris-HCl buffer, pH 7.5, at 4°C for at least 1 year
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dialysis and batch chromatography on QAE-Sephadex A25
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and expression of the 3'-region of the Mason-Pfizer monkey virus pro gene in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli BL21
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expression in Escherichia coli in inclusion bodies
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expression of wild-type and mutant enzymes in COS-1 cells
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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phylogenetic tree
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A114R
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site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
C7A/C106A
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the midpoint of the urea unfolding curve for 12000 Da truncated enzyme is at 1.9 M urea, the denaturation curve for the C7A/C106A mutant is no longer sigmoidal in character, confirming that this mutant is very unstable
C7A/D26N/C106A
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triple mutant of the 12000 Da truncated enzyme form shows significantly decreased capacity to dimerize
D26N/C7A/C106A
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mutant of isozyme p12 showing altered structure and low target functions
H21A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N109I/Q115I
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site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
Q115I
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site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
Q9A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and mutant virions show reduced incorporation of the viral glycoprotein Env during virus assembly
Q9A/V20A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and mutant virions show reduced incorporation of the viral glycoprotein Env during virus assembly
V20A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and mutant virions show reduced incorporation of the viral glycoprotein Env during virus assembly
additional information
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mutation of the cytoplasmic tail amino acids of the transmembrane protein TM, analysis of effects on the fusion to glycoprotein Env involving he protease activity, overview