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Information on EC 3.4.23.B11 - spumapepsin

for references in articles please use BRENDA:EC3.4.23.B11
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B11 spumapepsin
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This record set is specific for:
UNIPROT: P14349
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Good cleavage at the peptide bonds: Asn-Thr, Asn-Gln, Asn-Cys and Asn-Ala
Synonyms
core polyprotein, hfv pr, hsrv protease, human foamy virus proteinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
human foamy virus protease PR
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core polyprotein
-
-
-
-
Gag polyprotein
-
-
-
-
HFV PR
-
-
-
-
HSRV protease
-
-
-
-
human foamy virus protease
-
-
-
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human foamy virus proteinase
-
-
-
-
spumapepsin
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-92-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Gag protein precursor + H2O
?
show the reaction diagram
-
-
-
?
Pol protein precursor + H2O
?
show the reaction diagram
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gag protein precursor + H2O
?
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
sequence at the cleavage sites in wild-type Human foamy virus and in cleavage site mutants indicated, generation of Pol cleavage site mutants, expression and cleavage activity of Human foamy virus protease PR analyzed by Western Blot, reduced levels of PR activity observed, association between reduced enzyme activity and defects in replication of cleavage site mutant viruses shown
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GAG_FOAMV
648
0
70591
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PCR mutagenesis, cleavage site mutants of Human foamy virus protease PR generated using the full-length viral clone pcHFV13
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant forms, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Virion-associated RT assay is performed in BHK cells, ATCC CCL-10. Analysis of titers of wild-type and mutant proviruses transiently transfected into HEK-293T cells. Titers of Pol cleavage site mutants after infection measured in HEL cells.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mauere, B.; Bannert, H.; Darai, G.; Fluegel, R.M.
Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus
J. Virol.
62
1590-1597
1988
Human spumaretrovirus (P14349)
Manually annotated by BRENDA team
Roy, J.; Linial, M.L.
Role of the foamy virus Pol cleavage site in viral replication
J. Virol.
81
4956-4962
2007
Human spumaretrovirus (P14349)
Manually annotated by BRENDA team