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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-
-
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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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-
-
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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, 37C
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, 37C
0.298
PKQAYGAVFV
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pH 5.3, 37C
0.038
SSDIYWVQPI
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pH 5.3, 37C
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, 37C
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, 37C
7.7
PKQAYGAVFV
Mason-Pfizer monkey virus
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pH 5.3, 37C
4.56
SSDIYWVQPI
Mason-Pfizer monkey virus
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pH 5.3, 37C
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, 37C
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0.00028
PMV-phenylstatine-VRP
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pH 5.3, 37C
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0.013
PPAV-cysteinestatine-AMTM
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pH 5.3, 37C
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0.0031
PPCV-phenylstatine-AMTM
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pH 5.3, 37C
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0.00003
PPYV-phenylstatine-AMTM
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pH 5.3, 37C
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0.000003
PYV-phenylstatine-AMT
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pH 5.3, 37C
0.00005
RPMV-phenylstatine-VMP
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pH 5.3, 37C
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
4C, 13000 Da enzyme form is stable at pH 6.4 and at salt concentrations lower than 0.1 M
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4C, 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 4C 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