Any feedback?
Information on EC 3.4.23.B6 - Mason-Pfizer monkey virus proteinase and Organism(s) Mason-Pfizer monkey virus and UniProt Accession P07570
for references in articles please use BRENDA:EC3.4.23.B6preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.23.B6 Mason-Pfizer monkey virus proteinaseSpecify your search results
Word Map
- 3.4.23.B6
-
retroviral
- polyproteins
-
capsid
- virion
- retropepsins
- flap
-
g-patch
-
d-type
- retroviruses
-
glycine-rich
-
gag-related
-
pepsin-like
The taxonomic range for the selected organisms is: Mason-Pfizer monkey virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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.
Synonyms
m-pmv pr, m-pmv protease, mason-pfizer monkey virus proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M-PMV PR
M-PMV protease
Mason-Pfizer leukemia virus retropepsin
additional information
-
the enzyme belongs to the A2 peptidase family
M-PMV PR
-
-
-
-
M-PMV protease
-
-
-
-
Mason-Pfizer leukemia virus retropepsin
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
144114-21-6
-
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
ATHQVYNphVRKA + H2O
hydrolyzed peptid
-
-
the cysteine residues in M-PMV protease form an intramolecular disulfide bridge and that increases the proteolytic activity significantly
-
?
ATPQVYF(NO2)VRKA + H2O
ATPQVY + F(NO2)VRKA
-
-
-
-
?
capsid protein + H2O
?
-
cleaved in vitro within the major homology region
-
-
?
capsid-nucleocapsid fusion protein + H2O
capsid protein + nucleocapsid protein
-
-
-
-
?
IQVHYHRLEQ + H2O
IQVH + YHRLEQ
-
gp22-derived peptide, peptide derived from the cytoplasmic domain of transmembrane protein TM
-
-
?
NC protein + H2O
?
-
cleaved in several sites at the N-terminus
-
-
?
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
-
low activity
-
-
?
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
-
-
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
-
pronounced preference for the large hydrophobic residues Phe and Leu at position P3
-
-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
-
pronounced preference for the large hydrophobic residues Phe and Leu at position P3
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
large aromatic residues (Phe and Tyr) are preferred at position P1
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
large aromatic residues (Phe and Tyr) are preferred at position P1
-
-
?
Gag polyprotein + H2O
?
-
processing of the precursor protein into mature proteins and the functional protease
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into mature proteins and the functional protease
-
-
?
transmembrane glycoprotein + H2O
?
-
cleavage site is in the cytoplasmic domain of the protein
-
-
?
transmembrane glycoprotein + H2O
?
-
cleavage site is in the cytoplasmic domain of the protein. Cleavage takes place as a postbudding event
-
-
?
additional information
?
-
-
peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
-
-
?
additional information
?
-
-
processing of Gag polyproteins leads to reorganization of immature retroviral particles and formation of a ribonucleoprotein core. Protease catalyzed cleavage is involved in core disintegration
-
-
?
additional information
?
-
-
the individual forms of M-PMV proteinase may be responsible for cleavage at different locations in the virion or at different stages of maturation
-
-
?
additional information
?
-
-
individual forms of M-PMV proteinase may be responsible for cleavage at different parts of the budding virion, or at different stages of maturation
-
-
?
additional information
?
-
-
the enzyme is released by the autocatalytic cleavage of Gag-Pro and Gag-Pro-POl polypeptide precursors. The enzyme catalyzes the processing of viral precursors to yield the structural proteins and enzymes of the virion
-
-
?
additional information
?
-
-
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, analysis of the cleavage site recognition and specificity for individual amino acids, this processing mediates the fusion with the envelope glycoprotein Env
-
-
?
additional information
?
-
-
the enzyme is involved in core disintegration cleaving the capsid protein within the major homology region, the enzyme also converts the cell-associated transmembrane protein to a virus-associated gp20
-
-
?
additional information
?
-
-
the enzyme is involved in incorporation of the viral glycoprotein Env during virus assembly, the enzyme also converts the cell-associated transmembrane protein TM to a virus-associated gp20, effect of mutation in the cytoplasmic domain of TM, overview
-
-
?
additional information
?
-
-
cleavage site specificity, overview
-
-
?
additional information
?
-
-
study of influence of the P2 position residue on cleavage site specificity of isozyme p12, overview
-
-
?
vimetin + H2O
additional information
-
-
the 12000 Da enzyme form detectably cleaves vimetin only after 10 h
major cleavage product of 48000 Da
?
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 of the precursor protein into mature proteins and the functional protease
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into mature proteins and the functional protease
-
-
?
transmembrane glycoprotein + H2O
?
-
cleavage site is in the cytoplasmic domain of the protein. Cleavage takes place as a postbudding event
-
-
?
additional information
?
-
-
processing of Gag polyproteins leads to reorganization of immature retroviral particles and formation of a ribonucleoprotein core. Protease catalyzed cleavage is involved in core disintegration
-
-
?
additional information
?
-
-
the individual forms of M-PMV proteinase may be responsible for cleavage at different locations in the virion or at different stages of maturation
-
-
?
additional information
?
-
-
individual forms of M-PMV proteinase may be responsible for cleavage at different parts of the budding virion, or at different stages of maturation
-
-
?
additional information
?
-
-
the enzyme is released by the autocatalytic cleavage of Gag-Pro and Gag-Pro-POl polypeptide precursors. The enzyme catalyzes the processing of viral precursors to yield the structural proteins and enzymes of the virion
-
-
?
additional information
?
-
-
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, analysis of the cleavage site recognition and specificity for individual amino acids, this processing mediates the fusion with the envelope glycoprotein Env
-
-
?
additional information
?
-
-
the enzyme is involved in core disintegration cleaving the capsid protein within the major homology region, the enzyme also converts the cell-associated transmembrane protein to a virus-associated gp20
-
-
?
additional information
?
-
-
the enzyme is involved in incorporation of the viral glycoprotein Env during virus assembly, the enzyme also converts the cell-associated transmembrane protein TM to a virus-associated gp20, effect of mutation in the cytoplasmic domain of TM, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values for peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
-
0.386
ATHQVYNphVRKA
-
13 kDa protease in 0.05% beta-mercaptoethanol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numbers for peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
transfection of COS-1 cells with the proviral construct
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
12250
-
three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscopy: 12246 Da, 12956 Da and 16965 Da
12960
-
three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscop: 12246 Da, 12956 Da and 16965 Da
13000
16970
-
three active forms of a retroviral enzyme are determined by electrospray ionization mass spectroscop: 12246 Da, 12956 Da and 16965 Da
17000
12000
-
2 * 12000, isozyme p12, 2 * 13000, isozyme p13, 2 * 17000, isozyme p17
13000
-
the 13000 Da enzyme form flows through the support from pH 5 to 7, gel filtration
13000
-
SDS-PAGE, the protease is excised autocatalytically from Gag polyprotein precursors in a 17 kDa form that undergoes further C-terminal self-processing to yield the 13 kDa protease.
13000
-
2 * 12000, isozyme p12, 2 * 13000, isozyme p13, 2 * 17000, isozyme p17
17000
-
the 17000 Da enzyme form flows through the support from pH 5 to 5.5, gel filtration
17000
-
2 * 12000, isozyme p12, 2 * 13000, isozyme p13, 2 * 17000, isozyme p17
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 12000, isozyme p12, 2 * 13000, isozyme p13, 2 * 17000, isozyme p17
homodimer
-
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
additional information
-
isozyme p12: structure molecular modeling, S2 subsite sequence comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
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
proteolytic modification
-
the 26000 Da precursor undergoes rapid self-processing both in Escherichia coli and in vitro at the NH2 terminus, yielding a proteolytically active 17000 Da protein, p17. This initial cleavage is followed in vitro by a much slower self-processing that leads to emergence of proteolytically active P12 and a COOH-terminal cleavage product, p5
proteolytic modification
-
processing of the 26000 Da precursor results in the first product of autocatalytic cleavage of 17000 Da, that can be processed further into truncated but still proteolytically active enzymes of 13000 Da and 120000 Da
proteolytic modification
-
when expressed in bacteria as a 26000 Da precursor, the proteinase is first processed at the N-terminus, yielding a proteolytically active 17000 Da form of proteinase. This initial cleavage is followed by a self-processing that leads to the emergence of an active 13000 Da form. Under acidic conditions, an autocatalytic cleavage of 17000 and 13000 Da forms occurs to generate the mature 12000 Da form. At pH 5, in the presenceof 2 M NaCl and 4°C the complete processing of p17 and p13 into the mature 12 000 Da form is complete in six days. At pH 7 without sodium chloride, 17000 Da and 13000 Da proteinases are stable for about one year
proteolytic modification
-
the first M-PMV protease sequence that excises autocatalytically from the precursor at the N terminus of the protease domain, is a 17000 Da protein, which undergoes further self-processing at the C terminus yielding a 13000 Da protease. These proteases are identified in virions. In vitro, wild-type 13000 Da protease cleaves off another stretch of seven amino acid residues from the C terminus resulting in the shortest 12000 Da form protease. The truncation of the protease decreases its proteolytic activity, however the activity of wild-type 12000 Da protease is sufficient for processing of Gag-polyproteins in vivo
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMR structure of a fully folded monomer of a 12000 Da M-PMV protease and of a C7A/D26N/C106A mutant
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A114R
-
site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
C7A/C106A
-
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
-
triple mutant of the 12000 Da truncated enzyme form shows significantly decreased capacity to dimerize
D26N/C7A/C106A
-
mutant of isozyme p12 showing altered structure and low target functions
H21A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N109I/Q115I
-
site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
Q115I
-
site-directed mutagenesis, the mutation alters the substrate specificity and reduces the enzyme activity and viral infectivity of COS-1 cells
Q9A
-
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
-
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
-
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
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
-
4°C, pH 5.5, the 17000 Da species is self-processed slowly into the 12000 Da form and the 5000 Da peptide
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of the 3'-region of the Mason-Pfizer monkey virus pro gene in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sonigo, P.; Barker, C.; Hunter, E.; Wain-Hobson, S.
Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-type retrovirus
Cell
45
375-385
1986
Mason-Pfizer monkey virus (P07570)
Rumlova, M.; Ruml, T.; Pohl, J.; Pichova, I.
Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein: evidence for a potential role of retroviral protease in early stages of infection
Virology
310
310-318
2003
Mason-Pfizer monkey virus
Snasel, J.; Shoeman, R.; Horejsi, M.; Hruskova-Heidingsfeldova, O.; Sedlacek, J.; Ruml, T.; Pichova, I.
Cleavage of vimentin by different retroviral proteases
Arch. Biochem. Biophys.
377
241-245
2000
Mason-Pfizer monkey virus
Zabransky, A.; Andreansky, M.; Hruskova-Heidingsfeldova, O.; Havlicek, V.; Hunter, E.; Ruml, T.; Pichova, I.
Three active forms of aspartic proteinase from Mason-Pfizer monkey virus
Virology
245
250-256
1998
Mason-Pfizer monkey virus
Hruskova-Heidingsfeldova, O.; Andreansky, M.; Fabry, M.; Blaha, I.; Strop, P.; Hunter, E.
Cloning, bacterial expression, and characterization of the Mason-Pfizer monkey virus proteinase
J. Biol. Chem.
270
15053-15058
1995
Mason-Pfizer monkey virus
Brody, B.A.; Rhee, S.S.; Sommerfelt, M.A.; Hunter, E.
A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein
Proc. Natl. Acad. Sci. USA
89
3443-3447
1992
Mason-Pfizer monkey virus
Sommerfelt, M.A.; Petteway, S.R., Jr.; Dreyer, G.B.; Hunter, E.
Effect of retroviral proteinase inhibitors on Mason-Pfizer monkey virus maturation and transmembrane glycoprotein cleavage
J. Virol.
66
4220-4227
1992
Mason-Pfizer monkey virus
Parker, S.D.; Hunter, E.
Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro
Proc. Natl. Acad. Sci. USA
98
14631-14636
2001
Mason-Pfizer monkey virus
Pichova, I.; Zabransky, A.; Kost'alova, I.; Hruskova-Heidingsfeldova, O.; Andreansky, M.; Hunter, E.; Ruml, T.
Analysis of autoprocessing of Mason-Pfizer monkey virus proteinase in vitro. Three active forms of proteinase
Adv. Exp. Med. Biol.
436
105-108
1998
Mason-Pfizer monkey 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
Mason-Pfizer monkey virus
Pichova, I.
Mason-Pfizer monkey virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
172-174
2004
Mason-Pfizer monkey virus
-
Bauerova-Zabranska, H.; Stokrova, J.; Strisovsky, K.; Hunter, E.; Ruml, T.; Pichova, I.
The RNA binding G-patch domain in retroviral protease is important for infectivity and D-type morphogenesis of Mason-Pfizer monkey virus
J. Biol. Chem.
280
42106-42112
2005
Mason-Pfizer monkey virus
Song, C.; Micoli, K.; Bauerova, H.; Pichova, I.; Hunter, E.
Amino acid residues in the cytoplasmic domain of the Mason-Pfizer monkey virus glycoprotein critical for its incorporation into virions
J. Virol.
79
11559-11568
2005
Mason-Pfizer monkey virus
Song, C.; Micoli, K.; Hunter, E.
Activity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail
J. Virol.
79
11569-11579
2005
Mason-Pfizer monkey virus
Zbransk, H.; Tuma, R.; Kluh, I.; Svato, A.; Ruml, T.; Hrabal, R.; Pichov, I.
The role of the S-S bridge in retroviral protease function and virion maturation
J. Mol. Biol.
365
1493-1504
2007
Mason-Pfizer monkey virus
Veverka, V.; Bauerova, H.; Zabransky, A.; Lang, J.; Ruml, T.; Pichova, I.; Hrabal, R.
Three-dimensional structure of a monomeric form of a retroviral protease
J. Mol. Biol.
333
771-780
2003
Mason-Pfizer monkey virus
Eizert, H.; Bander, P.; Bagossi, P.; Sperka, T.; Miklossy, G.; Boross, P.; Weber, I.T.; Toezser, J.
Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site
J. Virol.
82
10111-10117
2008
Mason-Pfizer monkey virus
Macek, P.; Chmelik, J.; Krizova, I.; Kaderavek, P.; Padrta, P.; Zidek, L.; Wildova, M.; Hadravova, R.; Chaloupkova, R.; Pichova, I.; Ruml, T.; Rumlova, M.; Sklenar, V.
NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus
J. Mol. Biol.
392
100-114
2009
Mason-Pfizer monkey virus
EXTERNAL LINKS (specific for EC-Number 3.4.23.B6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
