3.4.23.B6: Mason-Pfizer monkey virus proteinase
This is an abbreviated version!
For detailed information about Mason-Pfizer monkey virus proteinase, go to the full flat file.
Word Map on EC 3.4.23.B6
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3.4.23.B6
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retroviral
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polyproteins
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capsid
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virion
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retropepsins
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flap
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g-patch
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d-type
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retroviruses
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glycine-rich
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gag-related
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pepsin-like
- 3.4.23.B6
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retroviral
- polyproteins
-
capsid
- virion
- retropepsins
- flap
-
g-patch
-
d-type
- retroviruses
-
glycine-rich
-
gag-related
-
pepsin-like
Reaction
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 leukemia virus retropepsin, Mason-Pfizer monkey virus retropepsin, More, MPMV protease, P-MPV poteinase, P-MPV PR
ECTree
3.4.23.B6 Mason-Pfizer monkey virus proteinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.B6 - Mason-Pfizer monkey virus proteinase
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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
ATHQVYNphVRKA + H2O
hydrolyzed peptid
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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
ATPQVY + F(NO2)VRKA
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-
-
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?
capsid protein + H2O
?
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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
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-
-
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?
IQVHYHRLEQ + H2O
IQVH + YHRLEQ
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gp22-derived peptide, peptide derived from the cytoplasmic domain of transmembrane protein TM
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-
?
NC protein + H2O
?
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cleaved in several sites at the N-terminus
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-
?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
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-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
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-
-
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?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
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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
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-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
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-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
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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
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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
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-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
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-
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
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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
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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
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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
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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
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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
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large aromatic residues (Phe and Tyr) are preferred at position P1
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?
VSQNYPIVQ + H2O
VSQNY + PIVQ
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large aromatic residues (Phe and Tyr) are preferred at position P1
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?
Gag polyprotein + H2O
?
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processing of the precursor protein into mature proteins and the functional protease
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?
Gag-Pol polyprotein + H2O
?
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processing of the precursor protein into mature proteins and the functional protease
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?
transmembrane glycoprotein + H2O
?
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cleavage site is in the cytoplasmic domain of the protein
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?
transmembrane glycoprotein + H2O
?
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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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peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
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?
additional information
?
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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
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?
additional information
?
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the individual forms of M-PMV proteinase may be responsible for cleavage at different locations in the virion or at different stages of maturation
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?
additional information
?
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individual forms of M-PMV proteinase may be responsible for cleavage at different parts of the budding virion, or at different stages of maturation
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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cleavage site specificity, overview
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?
additional information
?
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study of influence of the P2 position residue on cleavage site specificity of isozyme p12, overview
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?
vimetin + H2O
additional information
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the 12000 Da enzyme form detectably cleaves vimetin only after 10 h
major cleavage product of 48000 Da
?
