3.4.23.B11: spumapepsin
This is an abbreviated version!
For detailed information about spumapepsin, go to the full flat file.
Word Map on EC 3.4.23.B11
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3.4.23.B11
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polyproteins
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leukemia
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envelope
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thymocytes
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retroviral
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virion
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spumaretrovirus
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viruses
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antisera
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sarcoma
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nonviral
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maltose
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preleukemic
- 3.4.23.B11
- polyproteins
- leukemia
- envelope
-
thymocytes
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retroviral
- virion
- spumaretrovirus
- viruses
- antisera
- sarcoma
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nonviral
- maltose
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preleukemic
Reaction
Good cleavage at the peptide bonds: Asn-Thr, Asn-Gln, Asn-Cys and Asn-Ala =
Synonyms
core polyprotein, Gag polyprotein, HFV PR, HSRV protease, human foamy virus protease, human foamy virus protease PR, human foamy virus proteinase, More, spumapepsin
ECTree
3.4.23.B11 spumapepsinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.B11 - spumapepsin
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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
Gag protein + H2O
?
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recombinant His6-tagged spumaretroviral Gag proteins expressed in Escherichia coli strain BL21, determination of cleavage/processing sites by N-terminal sequence determination and mass spectrometry, overview
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?
Gag protein-derived peptides + H2O
?
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recombinant peptide substrate derived from spumaretroviral Gag protein
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?
HSRV pr71Gag + H2O
?
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efficiently but not completely cleaved at the p68gag/p3 cleavage site
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-
?
SRAVNTVTOS + H2O
SRAVN + TVTOS
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oligopeptide representing the Gag(nucleocapsi)-cleavage site in human foamy virus
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?
SRAVNTVTQS + H2O
SRAVN + TVTQS
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molecular model of Human foamy virus protease PR indicated, role of residues being close to the catalytic aspartates in the higher pH optimum and in the lower dimer stability of Human foamy virus protease PR in comparison with Human immunodeficiency virus type 1 protease PR analyzed
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-
?
VSQAYPIVG + H2O
VSQAY + PIVG
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X: Cys and Ala are preferred at P2 position
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-
?
VSQCYPIVG + H2O
VSQCY + PIVG
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X: Cys and Ala are preferred at P2 position
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?
GB1-GFP + H2O
?
prototype foamy virus
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peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein, GFP
cleavage occurs at YVVH-CNTT
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?
GB1-GFP + H2O
?
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peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein, GFP
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-
?
GB1-GFP + H2O
?
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peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein, GFP
cleavage occurs at YVVH-CNTT
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?
GB1-GFP + H2O
?
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peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein,GFP
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-
?
Pol protein precursor + H2O
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analysis of cleavage sites of Human foamy virus protease PR, mutations around the cleavage site of the Human foamy virus Pol precursor protein shown to affect enzymatic activities of the protease PR
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?
pr74 + H2O
?
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the cleavage site that leads to the formation of the HFV gag proteins p70 and p3 is located 27 amino acid residues upstream of the carboxy terminus of the p74 gag precursor
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?
pr74 + H2O
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Pr74 is the gag precursor protein with a molecular mass of 74000 Da from which a 70000 Da protein, p70, is cleaved by the viral protease. Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle, absolute requirement for viral infectivity
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?
PRAVNTVTQR + H2O
PRAVN + TVTQR
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analysis of cleavage sites and kinetics with synthetic peptide substrates
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-
?
additional information
?
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the Glu54 residue of the enzyme is an essential specificity determinant for proteolytic processing of the structural proteins
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?
additional information
?
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the enzyme is essential for infectivity but not for formation of the 120000 Da Pol polyprotein
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?
additional information
?
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spumaretroviruses produce separate Pol and Gag precursor proteins from spliced mRNA in contrast to other retroviruses
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?
additional information
?
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positions P2' and P2 of the cleavage site are invariant and Gag and Pol cleavage sites are processed with similar efficiencies. Pol cleavage is independent of Gag cleavage efficiency. Mutant Gag N621G is almost completely processed, whereas the infectivity of the virus particles is decreased by more than one order of magnitude. Mutations Gag V620G and Gag V623G result in impaired Gag maturation. Overall, Gag cleavaeg efficiency correlates with viral infectivity
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?
PAIDGVFPVTTPDLRCRIINAILGGNI + H2O
additional information
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two cleavage sites: PAIDGVF-PVTTPDLRCRIIN-AILGGNI
?
