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Information on EC 3.4.23.B3 - equine infectious anemia virus proteinase and Organism(s) Equine infectious anemia virus and UniProt Accession P32542

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Equine infectious anemia virus
UNIPROT: P32542
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Word Map
The taxonomic range for the selected organisms is: Equine infectious anemia virus
The expected taxonomic range for this enzyme is: Equine infectious anemia virus
Reaction Schemes
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 proteinase, eiav pr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
equine infectious anemia virus retropepsin
-
EIAV PR
-
-
-
-
EIAV proteinase
-
-
-
-
EIAV retropepsin
-
-
EIAV-PR
-
-
-
-
equine infectious anemia virus retropepsin
additional information
-
the enzyme belongs to the A2 peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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.
show the reaction diagram
structure-based molecular modeling of reaction mechanism and substrate binding
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.
show the reaction diagram
substrate binding sites and mechanism, characterization by type 1 substrates, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
good substrate
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
best peptide substrate
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
low activity
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
low activity
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
-
-
?
AAQTCYNCGK + H2O
AAQTC + YNCGK
show the reaction diagram
-
-
-
?
AKLVLAQLSK + H2O
AKLVL + AQLSK
show the reaction diagram
-
-
-
?
APKVCFKCKQ + H2O
APKVC + FKCKQ
show the reaction diagram
-
-
-
?
EIAV Gag-Pol polypeptide + H2O
?
show the reaction diagram
-
several cleavage sites
-
-
?
EIAV Gag-Pol polypetide + H2O
?
show the reaction diagram
-
several cleavage sites
-
-
?
EIAV nucleocapsid protein + H2O
?
show the reaction diagram
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
show the reaction diagram
-
-
-
?
GQFVGVTYNL + H2O
GQFVG + VTYNL
show the reaction diagram
-
-
-
?
HIV-1 Gag-Pol polypeptide + H2O
?
show the reaction diagram
-
low activity
-
-
?
KEEIMLAYQG + H2O
KEEIM + LAYQG
show the reaction diagram
-
-
-
?
KMVKCFNCGK + H2O
KMVKCF + NCGK
show the reaction diagram
-
-
-
?
KPIKCWNCGK + H2O
KPIKCW + NCGK
show the reaction diagram
-
-
-
?
LAKALQTGLA + H2O
LAKAL + QTGLA
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
Lys-Ala-Arg-Val-Asn-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Asn + p-nitrophenylalanine-Glu-Ala-Gly-NH2
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Phe + p-nitrophenylalanine-Glu-Ala-Gly-NH2
show the reaction diagram
-
-
-
?
Lys-Ala-Arg-Val-Trp-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Trp + p-nitrophenylalanine-Glu-Ala-Gly-NH2
show the reaction diagram
-
-
-
?
Lys-Ala-Arg-Val-Tyr-p-nitrophenylalanine-Glu-Ala-Gly-NH2 + H2O
Lys-Ala-Arg-Val-Tyr + p-nitrophenylalanine-Glu-Ala-Gly-NH2
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
PSEEYPIMID + H2O
PSEEY + PIMID
show the reaction diagram
-
-
-
?
QKMMLLAKAL + H2O
QKMML + LAKAL
show the reaction diagram
-
-
-
?
QKQTFPIQQK + H2O
QKQTF + PIQQK
show the reaction diagram
-
-
-
?
SQNYPIVQ + H2O
SQNY + PIVQ
show the reaction diagram
-
-
-
?
STGVFWVENI + H2O
STGVF + WVENI
show the reaction diagram
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
show the reaction diagram
-
commercial substrate
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
show the reaction diagram
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
show the reaction diagram
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VPQNYPIVQ + H2O
VPQNY + PIVQ
show the reaction diagram
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
VSANYPIVQ + H2O
VSANY + PIVQ
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
show the reaction diagram
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNLPIVQ + H2O
VSQNL + PIVQ
show the reaction diagram
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNMPIVQ + H2O
VSQNM + PIVQ
show the reaction diagram
-
Phe, Tyr, Leu or Met, Ala are preferred at position P1 in order of decreasing efficiency
-
-
?
VSQNYPIV + H2O
VSQNY + PIV
show the reaction diagram
-
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
show the reaction diagram
VVQNYPIVQ + H2O
VVQNY + PIVQ
show the reaction diagram
-
at P4 position the hydrophobic residues Val, Leu, Phe and Pro are preferred
-
-
?
additional information
?
-
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
EIAV Gag-Pol polypetide + H2O
?
show the reaction diagram
-
several cleavage sites
-
-
?
EIAV nucleocapsid protein + H2O
?
show the reaction diagram
-
processing in the early phase of virus replication
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
enzyme assay in presence of 2 M NaCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35
AAQTCYNCGK
-
pH 5.6, 37°C
0.02
AKLVLAQLSK
-
pH 5.6, 37°C
0.6
APKVCFKCKQ
-
pH 5.6, 37°C
0.01
Gln-Lys-2-aminohexanoic acid-2-aminohexanoic acid-Leu-p-nitrophenylalanine-Ala-Lys-Ala-Leu
-
pH 4.7, wild-type enzyme
0.47
KMVKCFNCGK
-
pH 5.6, 37°C
0.02
KPIKCWNCGK
-
pH 5.6, 37°C
0.02 - 0.075
Lys-Ala-Arg-Ile-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
0.01 - 0.105
Lys-Ala-Arg-Leu-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
0.01 - 0.03
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Asn-Ala-2-aminohexanoic acid-NH2
0.1
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Gln-Ala-2-aminohexanoic acid-NH2
-
pH 4.7, 25°C, wild-type enzyme
0.02 - 0.07
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
0.04 - 0.21
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Thr-Ala-2-aminohexanoic acid-NH2
0.007
Lys-Ala-Arg-Val-Asn-p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
pH 4.7, 25°C, wild-type enzyme
0.025 - 0.05
Lys-Ala-Arg-Val-Leu-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
0.035 - 0.045
Lys-Ala-Arg-Val-Nal-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.035 - 0.07
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
0.075 - 0.205
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.05 - 0.55
Lys-Ala-Arg-Val-Trp-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.06 - 0.165
Lys-Ala-Arg-Val-Tyr-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.1
Pro-Ser-Glu-Glu-Tyr-Pro-Ile-2-aminohexanoic acid-Ile-Asn
-
pH 4.7, wild-type enzyme and mutant enzyme T30D
0.08
PSEEYPIMID
-
pH 5.6, 37°C
0.27
QKQTFPIQQK
-
pH 5.6, 37°C
2.2
SQNYPIVQ
-
pH 5.6, 37°C
0.04
VSQNYPIV
-
pH 5.6, 37°C
0.31
VSQNYPIVQ
-
pH 5.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
AAQTCYNCGK
-
pH 5.6, 37°C
0.4
AKLVLAQLSK
-
pH 5.6, 37°C
0.2
APKVCFKCKQ
-
pH 5.6, 37°C
1.9 - 3
Gln-Lys-2-aminohexanoic acid-2-aminohexanoic acid-Leu-p-nitrophenylalanine-Ala-Lys-Ala-Leu
2.5
KEEIMLAYQG
-
pH 5.6, 37°C
1.2
KMVKCFNCGK
-
pH 5.6, 37°C
0.02
KPIKCWNCGK
-
pH 5.6, 37°C
1.4 - 7.2
Lys-Ala-Arg-Ile-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
1 - 6.3
Lys-Ala-Arg-Leu-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-NH2
0.2 - 1.5
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Asn-Ala-2-aminohexanoic acid-NH2
2.6
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Gln-Ala-2-aminohexanoic acid-NH2
-
pH 4.7, 25°C, wild-type enzyme
0.8 - 8.2
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
1.3 - 4.2
Lys-Ala-Arg-Val-2-aminohexanoic acid-p-nitrophenylalanine-Thr-Ala-2-aminohexanoic acid-NH2
0.1
Lys-Ala-Arg-Val-Asn-p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
pH 4.7, 25°C, wild-type enzyme
1.3 - 12.5
Lys-Ala-Arg-Val-Leu-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
1.5 - 1.6
Lys-Ala-Arg-Val-Nal-p-nitrophenylalanine-Glu-Ala-Gly-NH2
2.2 - 12.5
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-2-aminohexanoic acid-Gly-NH2
1 - 4.2
Lys-Ala-Arg-Val-Phe-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.5 - 0.8
Lys-Ala-Arg-Val-Trp-p-nitrophenylalanine-Glu-Ala-Gly-NH2
0.3
Lys-Ala-Arg-Val-Tyr-p-nitrophenylalanine-Glu-Ala-Gly-NH2
-
pH 4.7, 25°C, mutant enzyme I54G
0.6 - 1.7
Pro-Ser-Glu-Glu-Tyr-Pro-Ile-2-aminohexanoic acid-Ile-Asn
6.1
PSEEYPIMID
-
pH 5.6, 37°C
1.3
QKMMLLAKAL
-
pH 5.6, 37°C
10.4
QKQTFPIQQK
-
pH 5.6, 37°C
1.7
SQNYPIVQ
-
pH 5.6, 37°C
3.7
VSQNYPIVQ
-
pH 5.6, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
activity range with peptide substrates in presence of NaCl
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11431
-
2 * 10000-12000, SDS-PAGE, 2 * 11431, sequence calculation and mass spectrometry
12000
-
x * 12000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 12000, SDS-PAGE
dimer
additional information
structure molecular modeling, S2 subsite sequence comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, structure-sequence comparison, molecular modeling, comparison to other retroviruses, overview
complex of the 154G mutant enzyme with the inhibitor HBY-793, hanging-drop vapor diffusion method
-
crystal structure determination and analysis
-
crystal structure of the enzyme in complex with LP-130, hanging-drop vapor diffusion method, crystals grown at room temperature
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I54G/Y48H
-
specificity constant is only 3fold lower than that measured for the single mutant I54G enzyme, towards the long, pseudosymmetrical peptide substrate Ac-Tyr-Arg-Ala-Arg-Val-Phe-4-nitrophenylalanyl-Val-Arg-Ala-Ala-Lys. The potency of the shorter HBY-793 inhibitor is reduced by 60fold compared to the Ki values measured against the wild-type or the I54G mutant enzyme
T30D
-
mutant enzyme is only marginally different from wild-type enzyme in its susceptibility to most of the inhibitors of the HIV-1/HIV-2 proteinases, except that HBY-793 has a potency that is reduced by ten-fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from virus grown in chronically infected dog thymus cells, ATCC CRL 1430, recombinant enzyme from Escherichia coli by several different steps of ion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, comparison to other retroviruses, overview
expression in Escherichia coli
-
expression in Escherichia coli as a Pol precursor protein
-
expression of the mutant enzyme I54G in Escherichia coli. The wild-type enzyme does not accumulate in Escherichia coli at a level sufficient for purifying enough material to homogeneity for crystallization
-
the enzyme is encoded in the 5' part of the pol gene, expression as part of the Gag-Pol polyprotein precursor, expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stephens, R.M.; Casey, J.W.; Rice, N.R.
Equine infectious anemia virus gag and pol genes: relatedness to visna and AIDS virus
Science
231
589-594
1986
equine infectious anemia virus (P03371)
Manually annotated by BRENDA team
Rushlow, K.; Olsen, K.; Stiegler, G.; Payne, S.L.; Montelaro, R.C.
Issel C.J.: Lentivirus genomic organization: the complete nucleotide sequence of the env gene region of equine infectious anemia virus
Virology
155
309-321
1986
equine infectious anemia virus (P03371)
Manually annotated by BRENDA team
Powell, D.J.; Bur, D.; Wlodawer, A.; Gustchina, A.; Payne, S.L.; Dunn, B.M.; Kay, J.
Expression, characterisation and mutagenesis of the aspartic proteinase from equine infectious anaemia virus
Eur. J. Biochem.
241
664-674
1996
equine infectious anemia virus
Manually annotated by BRENDA team
Kervinen, J.; Lubkowski, J.; Zdanov, A.; Bhatt, D.; Dunn, B.M.; Hui, K.Y.; Powell, D.J.; Kay, J.; Wlodawer, A.; Gustchina, A.
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV
Protein Sci.
7
2314-2323
1998
equine infectious anemia virus
Manually annotated by BRENDA team
Gustchina, A.; Kervinen, J.; Powell, D.J.; Zdanov, A.; Kay, J.; Wlodawer, A.
Structure of equine infectious anemia virus proteinase complexed with an inhibitor
Protein Sci.
5
1453-1465
1996
equine infectious anemia virus
Manually annotated by BRENDA team
Boross, P.; Bagossi, P.; Copeland, T.D.; Oroszlan, S.; Louis, J.M.; Tozser, J.
Effect of substrate residues on the P2' preference of retroviral proteinases
Eur. J. Biochem.
264
921-929
1999
equine infectious anemia virus (P32542)
Manually annotated by BRENDA team
Powell, D.J.; Bur, D.; Wlodawer, A.; Gustchina, A.; Dunn, B.M.; Kay, J.
The aspartic proteinase from equine infectious anaemia virus
Adv. Exp. Med. Biol.
436
41-45
1998
equine infectious anemia virus
Manually annotated by BRENDA team
Rushlow, K.; Peng, X.X.; Montelaro, R.C.; Shih, D.S.
Expression of the protease gene of equine infectious anemia virus in Escherichia coli: Formation of the mature processed enzyme and specific cleavage of the gag precursor
Virology
188
396-401
1992
equine infectious anemia virus
Manually annotated by BRENDA team
Tozser, J.; Friedman, D.; Weber, I.T.; Blaha, I.; Oroszlan, S.
Studies on the substrate specificity of the proteinase of equine infectious anemia virus using oligopeptide substrates
Biochemistry
32
3347-3353
1993
equine infectious anemia virus
Manually annotated by BRENDA team
Bagossi, P.; Sperka, T.; Feher, A.; Kadas, J.; Zahuczky, G.; Miklossy, G.; Boross, P.; Toezser, J.
Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites
J. Virol.
79
4213-4218
2005
equine infectious anemia virus (P32542)
Manually annotated by BRENDA team
Tozser, J.; Menendez-Arias, L.; Oroszlan, S.
Equine infectious anemia virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
160-163
2004
equine infectious anemia virus
-
Manually annotated by BRENDA team
Eizert, H.; Bander, P.; Bagossi, P.; Sperka, T.; Miklossy, G.; Boross, P.; Weber, I.T.; Toezser, J.
Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site
J. Virol.
82
10111-10117
2008
equine infectious anemia virus
Manually annotated by BRENDA team