3.4.23.B9: bovine leukemia virus protease
This is an abbreviated version!
For detailed information about bovine leukemia virus protease, go to the full flat file.
Word Map on EC 3.4.23.B9
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3.4.23.B9
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virion
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oligopeptide
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cooh-terminal
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htlv-1
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retroviruses
- 3.4.23.B9
- virion
- oligopeptide
-
cooh-terminal
- htlv-1
- retroviruses
Reaction
The best substrate YDPPAILPII is bearing the natural cleavage site between the matrix and the capsid proteins of BLV Gag precursor. polyprotein. Good cleavage of the peptide bonds: Leu-Pro, Leu-Val, Gly-Val and Leu-Pro =
Synonyms
BLV endopeptidase, BLV PR, BLV protease, bovine leukemia virus protease, bovine leukemia virus retropepsin, BVL PR, More
ECTree
3.4.23.B9 bovine leukemia virus proteaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.B9 - bovine leukemia virus protease
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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
AELE-aminobutyric acid-LLSIPLA + H2O
AELE-aminobutyric acid-L + LSIPLA
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70% of the activity with YDPPAILPII
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-
?
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
-
-
-
-
?
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
-
-
-
-
?
VAQNYPIVQ + H2O
VAQNY + PIVQ
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Ala and Pro are preferred at position P4
-
-
?
VPQNYPIVQ + H2O
VPQNY + PIVQ
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Ala and Pro are preferred at position P4
-
-
?
VSANYPIVQ + H2O
VSANY + PIVQ
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Ala and Lys are preferred at position P3
-
-
?
VSKNYPIVQ + H2O
VSKNY + PIVQ
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Ala and Lys are preferred at position P3
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
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highest preference for Leu at position P1, followed by Phe or Met
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
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highest preference for Leu at position P1, followed by Phe or Met
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
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highest preference for Leu at position P1, followed by Phe or Met
-
-
?
Gag polyprotein + H2O
?
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processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease
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-
?
Gag polyprotein + H2O
?
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processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease
-
-
?
YDPPAILPII + H2O
YDPPAIL + PII
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best substrate, bearing the natural cleavage site between the matrix and the capsid proteins of BLV Gag precursor polyprotein
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-
?
YDPPAILPII + H2O
YDPPAIL + Pro-Ile-Ile
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represents the CA/NC cleavage site of the Gag polyprotein
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-
?
YDPPAILPII + H2O
YDPPAIL + Pro-Ile-Ile
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represents the CA/NC cleavage site of the Gag polyprotein
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-
?
additional information
?
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the enzyme is responsible for processing both the initial translation products - precursors Gag-Pro-Pol, Gag-Pro and Gag into functional enzymes - protease, reverse transcriptase and integrase - and the mature structural proteins of the matrix, capsid and nucleocapsid
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-
?
additional information
?
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study of influence of the P2 position residue on cleavage site specificity, overview
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-
?
