3.4.23.B3: equine infectious anemia virus proteinase
This is an abbreviated version!
For detailed information about equine infectious anemia virus proteinase, go to the full flat file.
Word Map on EC 3.4.23.B3
Reaction
Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-/-PIVQ- cleavage site. =
Synonyms
EIAV PR, EIAV proteinase, EIAV retropepsin, EIAV-PR, equine infectious anemia virus retropepsin, More
ECTree
3.4.23.B3 equine infectious anemia virus proteinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.B3 - equine infectious anemia virus proteinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
EIAV Gag-Pol polypeptide + H2O
?
-
several cleavage sites
-
-
?
EIAV Gag-Pol polypetide + H2O
?
-
several cleavage sites
-
-
?
Gln-Lys-2-aminohexanoic acid-2-aminohexanoic acid-Leu-p-nitrophenylalanine-Ala-Lys-Ala-Leu + H2O
Gln-Lys-2-aminohexanoic acid-2-aminohexanoic acid-Leu + p-nitrophenylalanine-Ala-Lys-Ala-Leu
-
-
-
?
Lys-Ala-Arg-Ile-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2 + H2O
Lys-Ala-Arg-Ile-2-aminohexanoic acid + p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
-
-
-
?
Lys-Ala-Arg-Leu-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2 + H2O
Lys-Ala-Arg-Leu-2-aminohexanoic acid + p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
-
-
-
?
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Asn-Ala-2-aminohexanoic acid-NH2 + H2O
Lys-Ala-Arg-Val-2-aminohexanoic acid + p-nitrophenylalanine-Asn-Ala-2-aminohexanoic acid-NH2
-
-
-
?
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Gln-Ala-2-aminohexanoic acid-NH2 + H2O
Lys-Ala-Arg-Val-2-aminohexanoic acid + p-nitrophenylalanine-Gln-Ala-2-aminohexanoic acid-NH2
-
-
-
?
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2 + H2O
Lys-Ala-Arg-Val-2-aminohexanoic acid + p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Thr-Ala-2-aminohexanoic acid-NH2 + H2O
Lys-Ala-Arg-Val-2-aminohexanoic acid + p-nitrophenylalanine-Thr-Ala-2-aminohexanoic acid-NH2
-
-
-
?
Lys-Ala-Arg-Val-Asn-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Asn + p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-L-2-naphthylalanine-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-L-2-naphthylalanine + p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-Leu-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Leu + p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Phe + p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Phe + p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-Trp-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Trp + p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
-
-
?
Lys-Ala-Arg-Val-Tyr-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Tyr + p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
-
-
?
Pro-Ser-Glu-Glu-Tyr-Pro-Ile-2-aminohexanoic acid-Ile-Asn + H2O
Pro-Ser-Glu-Glu-Tyr + Pro-Ile-2-aminohexanoic acid-Ile-Asn
-
-
-
-
?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
good substrate
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
best peptide substrate
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
low activity
-
-
?
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
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VPQNYPIVQ + H2O
VPQNY + PIVQ
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VSANYPIVQ + H2O
VSANY + PIVQ
-
Gln is preferred at position P3. The second-best residue at P3 position is Phe. Gly and Ala are also tolerated
-
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
-
Gln is preferred at position P3. The second-best residue at P3 position is Phe. Gly and Ala are also tolerated
-
-
?
VSGNYPIVQ + H2O
VSGNY + PIVQ
-
Gln is preferred at position P3. The second-best residue at P3 position is Phe. Gly and Ala are also tolerated
-
-
?
VSQNAPIVQ + H2O
VSQNA + PIVQ
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VVQNYPIVQ + H2O
VVQNY + PIVQ
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
EIAV nucleocapsid protein + H2O
?
-
processing in the early phase of virus replication
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
commercial substrate
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
Gln is preferred at position P3. The second-best residue at P3 position is Phe. Gly and Ala are also tolerated
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
additional information
?
-
the enzyme does not favor P2' Glu in either the matrix protein/capsid protein
-
-
?
additional information
?
-
-
the enzyme is essential for processing gag and gal-pol polyproteins in order to generate new infectious viral particles
-
-
?
additional information
?
-
-
the enzyme processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection
-
-
?
additional information
?
-
-
the retropepsin is expressed as part of the Gag-Pol polyprotein precursor, the enzyme cleaves the precursor into functional proteins during or after assembly and budding of the virions, thereby releasing itself
-
-
?
additional information
?
-
-
an oligopeptide substrate representing the cleavage site between the matrix and capsid proteins of HIV-1 is highly active, while its P1'-pipecolic acid-substituted derivative is a specific inhibitor
-
-
?
additional information
?
-
P2 position preference with peptide substrate Val-Ser-Gln-Xaa-Tyr-Pro-Ile-Val-Gln, comparison to other retroviruses, overview
-
-
?
