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Information on EC 3.4.23.B4 - Feline immunodeficiency virus protease
for references in articles please use BRENDA:EC3.4.23.B4preliminary BRENDA-supplied EC number
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3.4.23.B4 Feline immunodeficiency virus proteaseSpecify your search results
Word Map
- 3.4.23.B4
-
broad-based
- polyproteins
-
retroviral
-
drug-resistant
- gag-pol
- flap
-
subsites
- val
- calicivirus
- lopinavir
- lentivirus
- virions
- medicine
- molecular biology
- drug development
The enzyme appears in viruses and cellular organisms
Reaction Schemes
The enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
Synonyms
fiv pr, fiv protease, fcv protease, feline immunodeficiency virus protease, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
feline immunodeficiency virus protease
Feline immunodeficiency virus retropepsin
FIV PR
FIV protease
FIV retropepsin
FIV-PR
additional information
Feline immunodeficiency virus retropepsin
-
-
-
-
FIV PR
-
-
-
-
FIV protease
-
-
-
-
additional information
-
the enzyme belongs to the A2 peptidase family
additional information
-
the enzyme belongs to the A2 peptidase family
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
The enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
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-
-
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the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
structure-function relationship and analysis, Asp30 is the catalytic residue
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the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
structure-function relationship and analysis, Asp30 is the catalytic residue
-
-
the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
144114-21-6
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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
Ac-Lys-Ser-Gly-Val-Phe-Val-Val-Asn-Gly-Lys-NH2 + H2O
Ac-Lys-Ser-Gly-Val-Phe + Val-Val-Asn-Gly-Lys-NH2
-
-
-
?
Ac-RSQNYPIVQR-NH2 + H2O
Ac-RSQNY + PIVQR-NH2
-
specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of HIV-1
-
-
?
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln-p-NO2-Phe-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln + p-NO2-Phe-Val-Gln-Ser-Lys-Gly
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-Lys-Val-Gln + Val-Val-Gln-Ser-Lys-Gly
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln-Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2 + H2O
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln + Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2
-
-
?
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly + H2O
Ile-Arg-Lys-Ile-Leu + Phe-Leu-Asp-Gly
-
-
-
?
Lys-Gly-Ser-Gly-Ala-Leu-Thr-Asn-Ala-Val-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Ala-Leu-Thr-Asn + Ala-Val-Leu-Val-Pro-Lys
-
-
?
Lys-Gly-Ser-Gly-Ala-Met-Val-Asn-Gln-Ala-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Ala-Met-Val-Asn + Gln-Ala-Leu-Val-Pro-Lys
-
-
?
Lys-Gly-Ser-Gly-Gly-Arg-Ile-Asn-Val-Ala-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Gly-Arg-Ile-Asn + Val-Ala-Leu-Val-Pro-Lys
-
-
?
Lys-Gly-Ser-Gly-Ile-Tyr-Thr-Val-Gln-Ser-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Ile-Tyr + Thr-Val-Gln-Ser-Leu-Val-Pro-Lys
-
-
-
?
Lys-Gly-Ser-Gly-Leu-Thr-Met-Val-Thr-Gln-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Leu-Thr-Met + Val-Thr-Gln-Leu-Val-Pro-Lys
-
-
-
?
Lys-Gly-Ser-Gly-Thr-Trp-Met-Val-His-Ser-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Thr-Trp + Met-Val-His-Ser-Leu-Val-Pro-Lys
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-
?
Lys-Gly-Ser-Gly-Val-Phe-Ala-Val-Thr-Gln-Leu-Val-Pro-Lys + H2O
Lys-Gly-Ser-Gly-Val-Phe + Ala-Val-Thr-Gln-Leu-Val-Pro-Lys
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-
?
Lys-Gly-Ser-Gly-Val-Tyr-Gln-Leu-Ser-Ala-Leu-Val-Pro-Lys
?
two cleavage sites: Tyr-Gln and Leu-Ser
-
-
?
Lys-Ser-Gly-Ile-Phe-Val-Val-Asn-Gly-Leu-Val-Lys + H2O
Lys-Ser-Gly-Ile-Phe + Val-Val-Asn-Gly-Leu-Val-Lys
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-
?
Lys-Ser-Gly-Val-Phe-His-Val-Asn-Gly-Lys + H2O
Lys-Ser-Gly-Val-Phe + His-Val-Asn-Gly-Lys
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-
?
Lys-Ser-Gly-Val-Phe-Ser-Val-Asn-Gly-Leu-Val-Lys + H2O
Lys-Ser-Gly-Val-Phe + Ser-Val-Asn-Gly-Leu-Val-Lys
-
-
?
Lys-Ser-Gly-Val-Phe-Val-Val-Asn-Gly-Leu-Val-Lys + H2O
Lys-Ser-Gly-Val-Phe + Val-Val-Asn-Gly-Leu-Val-Lys
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-
?
Lys-Ser-Gly-Val-Phe-Val-Val-Asn-Gly-Lys + H2O
Lys-Ser-Gly-Val-Phe + Val-Val-Asn-Gly-Lys
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-
-
?
Lys-Ser-Gly-Val-Phe-Val-Val-Gln-Gly-Leu-Val-Lys + H2O
Lys-Ser-Gly-Val-Phe + Val-Val-Gln-Gly-Leu-Val-Lys
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-
?
Lys-Ser-Gly-Val-Phe-Val-Val-Thr-Gly-Leu-Val-Lys + H2O
Lys-Ser-Gly-Val-Phe + Val-Val-Thr-Gly-Leu-Val-Lys
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-
?
Lys-Ser-Phe-Val-Phe-Val-Val-Asn-Gly-Leu-Val-Lys + H2O
Lys-Ser-Phe-Val-Phe + Val-Val-Asn-Gly-Leu-Val-Lys
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-
?
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR + H2O
RALTK(epsilon-ABZ)VQ + F(NO2)VQSKGR
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the synthetic peptide substrate mimicks the capsid/nucleocapsid cleavage site
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-
?
RKEEGPPQAYPIQTVNGPQYR + H2O
RKEEGPPQAY + PIQTVNGPQYR
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the addition of Arg at the ends of the peptides subtrate increases the solubility, specific cleavage between Tyr and Pro, the peptide mimicks the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein in HIV-1
-
-
?
Thr-Ile-Met-Met-Gln-Arg + H2O
Thr-Ile-Met + Met-Gln-Arg
-
-
-
?
Ac-RPQAYPIQTR-NH2 + H2O
Ac-RPQAY + PIQTR-NH2
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specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of FIV
-
-
?
Ac-RPQAYPIQTR-NH2 + H2O
Ac-RPQAY + PIQTR-NH2
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specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of FIV
-
-
?
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln-p-NO2-Phe-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln + p-NO2-Phe-Val-Gln-Ser-Lys-Gly
-
-
-
-
?
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln-p-NO2-Phe-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-(4-aminobenzoic acid)-Lys-Val-Gln + p-NO2-Phe-Val-Gln-Ser-Lys-Gly
-
-
-
?
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-Lys-Val-Gln + Val-Val-Gln-Ser-Lys-Gly
-
-
-
?
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly + H2O
Ala-Leu-Thr-Lys-Val-Gln + Val-Val-Gln-Ser-Lys-Gly
-
-
?
feline apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 protein + H2O
?
APOBEC3, FIV protease cleaves feline APOBEC3, A3Z2Z3, in released virions. The leucine residue at position 232 of feline A3Z2Z3 is related to cleavage by FIV PR
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-
?
feline apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 protein + H2O
?
HA-tagged recombinantly expressed feline A3Z2Z3. The leucine residue at position 232 of feline A3Z2Z3 is related to cleavage by FIV PR
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-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein
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-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into several mature proteins
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-
?
Gag-Pol polyprotein + H2O
?
-
cleavage between Tyr and Pro in the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein
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-
?
Gag-Pol polyprotein + H2O
?
-
FIV PR cleaves Gag polyprotein into 5 individual proteins, including matrix, capsid, p1, nucleocapsid, and p2
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-
?
Gag-Pol polyprotein + H2O
?
-
the Gag precursor is cleaved into the final mature Gag proteins matrix, capsid, nucleocapsid, spacer peptides (SP1, SP2), flanking nucleocapsid, and the C-terminal peptide p2
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into several mature proteins
-
-
?
Gag-Pol polyprotein + H2O
?
-
cleavage between Tyr and Pro in the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein
-
-
?
additional information
?
-
cleavage of the HIV-1 protease substrate (4-aminobenzoic acid)-Thr-Ile-Nle-Phe-(NO2)-Gln-Arg-NH2 is undetectable after 1 h
-
-
?
additional information
?
-
-
cleavage of the HIV-1 protease substrate (4-aminobenzoic acid)-Thr-Ile-Nle-Phe-(NO2)-Gln-Arg-NH2 is undetectable after 1 h
-
-
?
additional information
?
-
-
the enzyme is essential for virion maturation and subsequent viral replication in that it cleaves the Gag and Gag/Pol polyproteins at eight sites to release the respective structural proteins and enzymes
-
-
?
additional information
?
-
-
feline immunodeficiency virus induces neurological deficits in the central nervous system of host cats which can be prevented by treatment with the feline immunodeficiency virus protease inhibitor TL-3, overview
-
-
?
additional information
?
-
-
the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa
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-
?
additional information
?
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-
substrate specificity, cleavage sites of synthetic peptides corresponding to the natural cleavage sites of the Gag-Pol polyprotein, overview
-
-
?
additional information
?
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-
both FIV and HIV-1 PRs recognize, the P4-P4 residues of peptide substrates via a long cavity in the middle of the protease. Both homodimeric PRs utilize an acid-base hydrolysis mechanism in which aspartic acids 30 and 30 activate a water molecule to perform a nucleophilic attack on the amide carbonyl between the P1 and P1 positions in various peptide substrates
-
-
?
additional information
?
-
-
FIV protease cleaves the FIV MA/CA cleavage junction efficiently. It does not cut the HIV-1 MA/CA cleavage junction, despite the presence of four identical residues in the P3-P3' position
-
-
?
additional information
?
-
-
there are three major structurally conserved regions that make up the substrate binding pockets of PR: (1) the active core region residues 30-38 for FIV (2) the flap residues 54-60 for FIV and (3) C-terminal 90s loop region residues 98-101 for FIV. Within these regions, there are 11 amino acids that differ between FIV and HIV-1 proteases. The 11 different amino acid residues in the S4-S4 subsites of FIV protease, Ile35, Ile37, Gln54, Asn55, Met56, Ile57, Val59, Ile98, Gln99, Pro100 and Leu101, most likely account for the specificity of the substrate/inhibitor binding
-
-
?
additional information
?
-
-
the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa
-
-
?
additional information
?
-
-
substrate specificity, cleavage sites of synthetic peptides corresponding to the natural cleavage sites of the Gag-Pol polyprotein, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
feline apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 protein + H2O
?
APOBEC3, FIV protease cleaves feline APOBEC3, A3Z2Z3, in released virions. The leucine residue at position 232 of feline A3Z2Z3 is related to cleavage by FIV PR
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into several mature proteins
-
-
?
Gag-Pol polyprotein + H2O
?
-
FIV PR cleaves Gag polyprotein into 5 individual proteins, including matrix, capsid, p1, nucleocapsid, and p2
-
-
?
Gag-Pol polyprotein + H2O
?
-
the Gag precursor is cleaved into the final mature Gag proteins matrix, capsid, nucleocapsid, spacer peptides (SP1, SP2), flanking nucleocapsid, and the C-terminal peptide p2
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into several mature proteins
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein
-
-
?
additional information
?
-
-
the enzyme is essential for virion maturation and subsequent viral replication in that it cleaves the Gag and Gag/Pol polyproteins at eight sites to release the respective structural proteins and enzymes
-
-
?
additional information
?
-
-
feline immunodeficiency virus induces neurological deficits in the central nervous system of host cats which can be prevented by treatment with the feline immunodeficiency virus protease inhibitor TL-3, overview
-
-
?
additional information
?
-
-
the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa
-
-
?
additional information
?
-
-
the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
NaCl
the protease activity is not inhibited with increasing NaCl concentrations up to 130 mM
NaCl
-
increasing salt concentration up to 1.5 M increases the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-[1-[1-(4-[2-[2-(2-Benzyloxycarbonylamino-3-hydroxy-propionylamino)-propionylamino]-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl)-2-methyl-propylcarbamoyl]-ethylcarbamoyl]-2-hydroxy-ethyl)-carbamic acid benzyl ester
-
IC50: 128 nM
(3S,4R,5R,6S)-3,4-di-O-(3'-fluorobenzyl)-N-methyl-3,4,5,6-tetrahydroxyazepane N-oxide
-
weak
(3S,4R,5R,6S)-3,6-di-O-(3',5'-difluorobenzyl)-3,4,5,6-tetrahydroxyazepane
-
IC50: 0.67 mM
(3S,4R,5R,6S)-3,6-di-O-(3'-fluorobenzyl)-3,4,5,6-tetrahydroxyazepane
-
IC50: 1.4 mM
2-(2-Benzenesulfonylamino-propionylamino)-N-[4-[2-(2-benzenesulfonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butyl]-3-methyl-butyramide
-
IC50: 138 nM
2-[2-(4-Bromo-benzenesulfonylamino)-propionylamino]-N-(4-[2-[2-(4-bromo-benzenesulfonylamino)-propionylamino]-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butyl)-3-methyl-butyramide
-
IC50: 141 nM
2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-N-(4-[2-[2-acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-1-benzyl-2,3-dihydroxy-5-phenyl-pentyl)-3-methyl-butyramide
-
IC50: 212 nM
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-3-phenyl-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
-
IC50: 48 nM
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-3-phenyl-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (3-methyl-2-methylamino-butyryl)-amide
-
IC50: 117 nM
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
-
IC50: 182 nM
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
-
IC50: 256 nM
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (3-methyl-2-methylamino-butyryl)-amide
-
IC50: 80 nM
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
-
IC50: 0.0012 mM
Ac-Gly-Ser-Gly-Val-Phe-Psi[CH2NH2]-Val-Val-Asn-Gly-Leu
-
Ac-GSGVFPSI[CH2NH]VVNGL-NH2
-
strong inhibition of FIV retropepsin
Ac-naphthylalanine-Val-statine-Glu-naphthylalanine-NH2
-
an inhibitor derived from aspartic proteinase inhibitors, statine is 3-hydroxy-4-amino-7-methylheptanoic acid
Gly-Ser-Gly-Val-Phe[CH2NH]-Val-Val-Asn-Gly-Leu
IC50: 0.0004 mM
Gly-Ser-Gly-Val-Phe[CHOHCH2]-Val-Val-Asn-Gly-Leu
IC50: 0.005 mM
N-(2,3-Dihydroxy-4-[2-[2-(4-methoxy-benzenesulfonylamino)-propionylamino]-3-methyl-butyrylamino]-1,4-diphenyl-butyl)-2-[2-(4-methoxy-benzenesulfonylamino)-propionylamino]-3-methyl-butyramide
-
IC50: 310 nM
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(3-p-tolyl-ureido)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(3-p-tolyl-ureido)-propionylamino]-butyramide
-
IC50: 0.2 mM
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(toluene-4-sulfonylamino)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(4-methyl-cyclohexa-1,3-dienesulfonylamino)-propionylamino]-butyramide
-
IC50: 17 nM
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(toluene-4-sulfonylamino)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(4-nitro-cyclohexa-1,3-dienesulfonylamino)-propionylamino]-butyramide
-
IC50: 228 nM
N-[1-(1-[2,3-Dihydroxy-4-[3-methyl-2-(2-nicotinylamino-propionylamino)-butyrylamino]-1,4-diphenyl-butylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-nicotinamide
-
62 nM
N-[1-(1-[4-[2-(2-Benzoylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-benzamide
-
IC50: 156 nM
N-[2,3-Dihydroxy-4-(2-[2-[3-(4-methoxy-phenyl)-ureido]-propionylamino]-3-methyl-butyrylamino)-1,4-diphenyl-butyl]-2-[2-[3-(4-methoxy-phenyl)-ureido]-propionylamino]-3-methyl-butyramide
-
IC50: 0.2 mM
N-[2,3-Dihydroxy-4-(3-methyl-2-[2-[3-(4-trifluoromethoxy-phenyl)-ureido]-propionylamino]-butyrylamino)-1,4-diphenyl-butyl]-3-methyl-2-[2-[3-(4-trifluoromethoxy-phenyl)-ureido]-propionylamino]-butyramide
-
IC50: 0.119 mM
N-[2,3-Dihydroxy-4-(3-methyl-2-[2-[3-(4-trifluoromethyl-phenyl)-ureido]-propionylamino]-butyrylamino)-1,4-diphenyl-butyl]-3-methyl-2-[2-[3-(4-trifluoromethyl-phenyl)-ureido]-propionylamino]-butyramide
-
IC50: 0.2 mM
N-[2,3-Dihydroxy-4-[3-methyl-2-(2-phenylmethanesulfonylamino-propionylamino)-butyrylamino]-1,4-diphenyl-butyl]-3-methyl-2-(2-phenylmethanesulfonylamino-propionylamino)-butyramide
-
IC50: 118 nM
N-[benzyloxycarbonyl]-L-Ala-N-[(1S)-1-benzyl-2-hydroxyethyl]-L-valinamide
ie. TL-3
protease inhibitor AB-2
-
a HIV-1 protease inhibitor, IC50: 0.0011 mM
protease inhibitor AB-6
-
a HIV-1 protease inhibitor, IC50: 0.001 mM
protease inhibitor AB-8
-
a HIV-1 protease inhibitor, IC50: 0.008 mM
protease inhibitor APV-1
-
a HIV-1 protease inhibitor, IC50: 0.001 mM
protease inhibitor RTV
-
a HIV-1 protease inhibitor, weak inhibition of wild-type FIV protease, IC50: 0.045 mM
[(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-acetylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-methyl]-carbamic acid benzyl ester
-
-
[1-(1-[1-Benzyl-2,3,3-trihydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
IC50: 200 nM
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-3-oxo-propylcarbamoyl]-2-methyl-propylcarbamoyl)-2-(1H-indol-3-yl)-ethyl]-carbamic acid benzyl ester
-
IC50: 0.001 mM
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-3-oxo-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
IC50: 0.019 mM
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
IC50: 0.0052 mM
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-3-phenyl-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-2-phenyl-ethyl]-carbamic acid benzyl ester
-
IC50: 0.0092
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-4-methyl-pentanoylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester
-
-
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
-
[1-(1-[4-[2-(2-Benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
IC50: 100 nM
[1-[1-(1-Benzyl-3-[4-[2-(2-benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylcarbamoyl]-5,5-dimethyl-thiazolidin-3-yl]-2,3,3-trihydroxy-propylcarbamoyl)-2-methyl-propylcarbamoyl]-ethyl]-carbamic acid benzyl ester
-
IC50: 95 nM
protease inhibitor TL-3
-
the inhibitor of the feline immunodeficiency virus protease can prevent virus-induced deficits in the central nervous system of cats, overview
additional information
using cell culture assays, PPNDS, quercetagetin and GC376 do not display antiviral effects, while nitazoxanide and 2'-C-methylcytidine (2CMC) are potent inhibitors of FCV replication
-
additional information
-
using cell culture assays, PPNDS, quercetagetin and GC376 do not display antiviral effects, while nitazoxanide and 2'-C-methylcytidine (2CMC) are potent inhibitors of FCV replication
-
additional information
-
C2-symmetric inhibitor TL-3, which contains (1S,2R,3R,4S)-1,4-diamino-1,4-dibenzyl-2,3-diol as the P1-P1' unit and Ala at p3/p3' positions
-
additional information
KI-values for multiple-substitution mutants constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease. Non of the potent HIV-1 inhibitors - saquinavir, ritonavir, nelfinavir and JE-2147 - are good inhibitors for the wild-type enzyme
-
additional information
-
KI-values for multiple-substitution mutants constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease. Non of the potent HIV-1 inhibitors - saquinavir, ritonavir, nelfinavir and JE-2147 - are good inhibitors for the wild-type enzyme
-
additional information
-
structural features of compounds with high inhibitory potency, overview, e.g. small P3 residues results in highly inhibitory compounds
-
additional information
-
FIV PR exchange mutants are much more susceptible to HIV-1 protease inhibitors than the wild-type FIV protease
-
additional information
-
inhibitors of HIV-1 protease currently employed in clinic do not inhibit FIV protease despite similarities between HIV-1 PR and FIV PR
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Analysis of the S3 and S3' subsite specificities of feline immunodeficiency virus (FIV) protease: development of a broad-based protease inhibitor efficacious against FIV, SIV, and HIV in vitro and ex vivo.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln-Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2
-
0.033
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR
-
pH 5.3, 0.2 M NaCl, 0.1 mM EDTA, 1 mM DTT
0.0056
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/V59I
0.01
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V
0.0114
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme V59I
0.0156
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme N55M
0.0159
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/N55M
0.018
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme Q99V
0.0193
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme L97T/I98P/Q99V/P100N/L101I
0.0204
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
pH 5.25, wild-type enzyme
0.0205
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/M56I
0.0244
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme L101I
0.0256
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, wild-type enzyme
0.0278
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme M56I
0.0351
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I98P
0.0372
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/Q54K
0.156
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme Q54K
0.271
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I57G/G62F
0.462
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme Q99V
0.542
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V
0.582
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme N55M
0.739
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V/N55M
0.832
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V/V59I
1.183
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme V59I
1.4
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, wild-type enzyme
1.845
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme M56I
additional information
additional information
Km-values for multiple-substitution mutants constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease
-
additional information
additional information
-
Km-values for multiple-substitution mutants constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln-Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2
-
0.29
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR
-
pH 5.3, 0.2 M NaCl, 0.1 mM EDTA, 1 mM DTT
0.0015
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I57G/G62F
0.002
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme L101I
0.0035
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme L97T/I98P/Q99V/P100N/L101I
0.00367
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme Q54K
0.00533
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/Q54K
0.00617
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/V59I
0.00833
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme V59I
0.00983
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V
0.0102
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/N55M
0.0113
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I98P
0.0123
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme N55M
0.0142
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme M56I
0.0165
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme Q99V
0.0173
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, wild-type enzyme
0.0223
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
-
pH 5.25, mutant enzyme I37V/V59I
3.01
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
pH 5.25, wild-type enzyme
0.945
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme M56I
1.81
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, wild-type enzyme
2.27
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V/V59I
2.51
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme V59I
2.65
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme Q99V
2.69
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme N55M
3.56
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V
4
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
-
pH 5.25, mutant enzyme I37V/N55M
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00026
Ac-naphthylalanine-Val-statine-Glu-naphthylalanine-NH2
-
-
0.000156
[(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-acetylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-methyl]-carbamic acid benzyl ester
-
-
0.007
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-3-phenyl-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-2-phenyl-ethyl]-carbamic acid benzyl ester
-
-
0.000159
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-4-methyl-pentanoylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester
-
-
0.000041
[1-(1-[1-benzyl-4-[2-(2-benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-5-phenyl-pentylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000128
(1-[1-[1-(4-[2-[2-(2-Benzyloxycarbonylamino-3-hydroxy-propionylamino)-propionylamino]-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl)-2-methyl-propylcarbamoyl]-ethylcarbamoyl]-2-hydroxy-ethyl)-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 128 nM
0.67
(3S,4R,5R,6S)-3,6-di-O-(3',5'-difluorobenzyl)-3,4,5,6-tetrahydroxyazepane
feline immunodeficiency virus
-
IC50: 0.67 mM
1.4
(3S,4R,5R,6S)-3,6-di-O-(3'-fluorobenzyl)-3,4,5,6-tetrahydroxyazepane
feline immunodeficiency virus
-
IC50: 1.4 mM
0.000138
2-(2-Benzenesulfonylamino-propionylamino)-N-[4-[2-(2-benzenesulfonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butyl]-3-methyl-butyramide
feline immunodeficiency virus
-
IC50: 138 nM
0.000141
2-[2-(4-Bromo-benzenesulfonylamino)-propionylamino]-N-(4-[2-[2-(4-bromo-benzenesulfonylamino)-propionylamino]-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butyl)-3-methyl-butyramide
feline immunodeficiency virus
-
IC50: 141 nM
0.000212
2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-N-(4-[2-[2-acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-1-benzyl-2,3-dihydroxy-5-phenyl-pentyl)-3-methyl-butyramide
feline immunodeficiency virus
-
IC50: 212 nM
0.000048
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-3-phenyl-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
feline immunodeficiency virus
-
IC50: 48 nM
0.000117
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-3-phenyl-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (3-methyl-2-methylamino-butyryl)-amide
feline immunodeficiency virus
-
IC50: 117 nM
0.000182
3-(2-Hydroxy-3-[2-[2-(hydroxy-methyl-amino)-propionylamino]-3-methyl-butyrylamino]-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
feline immunodeficiency virus
-
IC50: 182 nM
0.000256
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
feline immunodeficiency virus
-
IC50: 256 nM
0.00008
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-5,5-dimethyl-thiazolidine-4-carboxylic acid (3-methyl-2-methylamino-butyryl)-amide
feline immunodeficiency virus
-
IC50: 80 nM
0.0012
3-(3-[2-[2-Acetylamino-3-(1H-indol-3-yl)-propionylamino]-3-methyl-butyrylamino]-2-hydroxy-4-phenyl-butyryl)-thiazolidine-4-carboxylic acid (2-methoxyamino-3-methyl-butyryl)-amide
feline immunodeficiency virus
-
IC50: 0.0012 mM
0.0004
Gly-Ser-Gly-Val-Phe[CH2NH]-Val-Val-Asn-Gly-Leu
feline immunodeficiency virus
IC50: 0.0004 mM
0.005
Gly-Ser-Gly-Val-Phe[CHOHCH2]-Val-Val-Asn-Gly-Leu
feline immunodeficiency virus
IC50: 0.005 mM
0.00031
N-(2,3-Dihydroxy-4-[2-[2-(4-methoxy-benzenesulfonylamino)-propionylamino]-3-methyl-butyrylamino]-1,4-diphenyl-butyl)-2-[2-(4-methoxy-benzenesulfonylamino)-propionylamino]-3-methyl-butyramide
feline immunodeficiency virus
-
IC50: 310 nM
0.2
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(3-p-tolyl-ureido)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(3-p-tolyl-ureido)-propionylamino]-butyramide
feline immunodeficiency virus
-
IC50: 0.2 mM
0.000017
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(toluene-4-sulfonylamino)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(4-methyl-cyclohexa-1,3-dienesulfonylamino)-propionylamino]-butyramide
feline immunodeficiency virus
-
IC50: 17 nM
0.000228
N-(2,3-Dihydroxy-4-[3-methyl-2-[2-(toluene-4-sulfonylamino)-propionylamino]-butyrylamino]-1,4-diphenyl-butyl)-3-methyl-2-[2-(4-nitro-cyclohexa-1,3-dienesulfonylamino)-propionylamino]-butyramide
feline immunodeficiency virus
-
IC50: 228 nM
0.000156
N-[1-(1-[4-[2-(2-Benzoylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-benzamide
feline immunodeficiency virus
-
IC50: 156 nM
0.2
N-[2,3-Dihydroxy-4-(2-[2-[3-(4-methoxy-phenyl)-ureido]-propionylamino]-3-methyl-butyrylamino)-1,4-diphenyl-butyl]-2-[2-[3-(4-methoxy-phenyl)-ureido]-propionylamino]-3-methyl-butyramide
feline immunodeficiency virus
-
IC50: 0.2 mM
0.119
N-[2,3-Dihydroxy-4-(3-methyl-2-[2-[3-(4-trifluoromethoxy-phenyl)-ureido]-propionylamino]-butyrylamino)-1,4-diphenyl-butyl]-3-methyl-2-[2-[3-(4-trifluoromethoxy-phenyl)-ureido]-propionylamino]-butyramide
feline immunodeficiency virus
-
IC50: 0.119 mM
0.2
N-[2,3-Dihydroxy-4-(3-methyl-2-[2-[3-(4-trifluoromethyl-phenyl)-ureido]-propionylamino]-butyrylamino)-1,4-diphenyl-butyl]-3-methyl-2-[2-[3-(4-trifluoromethyl-phenyl)-ureido]-propionylamino]-butyramide
feline immunodeficiency virus
-
IC50: 0.2 mM
0.000118
N-[2,3-Dihydroxy-4-[3-methyl-2-(2-phenylmethanesulfonylamino-propionylamino)-butyrylamino]-1,4-diphenyl-butyl]-3-methyl-2-(2-phenylmethanesulfonylamino-propionylamino)-butyramide
feline immunodeficiency virus
-
IC50: 118 nM
0.0011
protease inhibitor AB-2
feline immunodeficiency virus
-
a HIV-1 protease inhibitor, IC50: 0.0011 mM
0.001
protease inhibitor AB-6
feline immunodeficiency virus
-
a HIV-1 protease inhibitor, IC50: 0.001 mM
0.008
protease inhibitor AB-8
feline immunodeficiency virus
-
a HIV-1 protease inhibitor, IC50: 0.008 mM
0.001
protease inhibitor APV-1
feline immunodeficiency virus
-
a HIV-1 protease inhibitor, IC50: 0.001 mM
0.045
protease inhibitor RTV
feline immunodeficiency virus
-
a HIV-1 protease inhibitor, weak inhibition of wild-type FIV protease, IC50: 0.045 mM
0.0002
[1-(1-[1-Benzyl-2,3,3-trihydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 200 nM
0.001
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-3-oxo-propylcarbamoyl]-2-methyl-propylcarbamoyl)-2-(1H-indol-3-yl)-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 0.001 mM
0.019
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-3-oxo-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 0.019 mM
0.0052
[1-(1-[1-Benzyl-2-hydroxy-3-[4-(2-methoxyamino-3-methyl-butyrylcarbamoyl)-5,5-dimethyl-thiazolidin-3-yl]-propylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 0.0052 mM
0.0001
[1-(1-[4-[2-(2-Benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylamino]-2,3-dihydroxy-1,4-diphenyl-butylcarbamoyl]-2-methyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 100 nM
0.000095
[1-[1-(1-Benzyl-3-[4-[2-(2-benzyloxycarbonylamino-propionylamino)-3-methyl-butyrylcarbamoyl]-5,5-dimethyl-thiazolidin-3-yl]-2,3,3-trihydroxy-propylcarbamoyl)-2-methyl-propylcarbamoyl]-ethyl]-carbamic acid benzyl ester
feline immunodeficiency virus
-
IC50: 95 nM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
mammalian apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3) proteins act as intrinsic restriction factors against lentiviruses. Viral infectivity factor (Vif) degrades host APOBEC3 proteins via a ubiquitin/proteasome-dependent pathway. FIV protease cleaves feline APOBEC3 in released virions. Thus, lentivirus encodes two types of anti-APOBEC3 factors, Vif and viral protease
physiological function
FIV protease cleaves feline APOBEC3 A3Z2Z3 in released virions. FIV PR-mediated cleavage of feline A3Z2Z3 potently contributes to counteracting the antiviral effect mediated by feline A3Z2Z3
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A059UHW3_9RETR
1135
0
129895
TrEMBL
-
POL_FIVPE
1124
0
127494
Swiss-Prot
-
POLG_FCVUR
Feline calicivirus (strain Cat/United States/Urbana/1960)
1763
0
194911
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 78000, recombinant C-terminally His-tagged viral polyprotein, SDS-PAGE
dimer
homodimer
dimer
-
enzyme structure analysis, the FIV retropepsin contains three large surface loops, the central core is exposed, flaps cover the active-site cleft, structure comparison with the HIV-1 retropepsin, overview
dimer
-
enzyme structure analysis, the FIV retropepsin contains three large surface loops, the central core is exposed, flaps cover the active-site cleft, structure comparison with the HIV-1 retropepsin, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
the enzyme is expressed in vivo as part of the Gag/Pol polyprotein and, after autoprocessing out of the polyprotein, has a unit length of 116 amino acids, N-terminal Tyr, C-terminal Met
proteolytic modification
-
the enzyme performs autolytic processing of precursor protein
proteolytic modification
-
the enzyme performs autolytic processing of precursor protein
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of the D30N mutant enzyme with the statine-based inhibitor LP-149 as well as with a substrate based on a modification of the inhibitor, LP-149S
crystal structure (1.7 A) of FIV protease is obtained in which 12 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR (12XFIV PR). The chimeric PR is crystallized in complex with inhibitor TL-3. Comparison of the crystal structures of the TL-3 complexes of 12X FIV and wild-type FIV PR reveal the information of additional van der Waals interactions between the enzyme inhibitor in the mutant PR
crystal structure determination and analysis, recombinant enzyme
-
hanging-drop vapor diffusion technique, crystals are grown at 4°C, crystal structure of the enzyme in complex with LP-130
mutant I37V/N55M/V59I/I98S/Q99V/P100N in complex with HIV inhibitors darunavir and lopinavir, to 1.7 and 1.8 A resolution, respectively. A flexible 90s loop and residue 98 play roles in supporting Gag processing and infectivity, residue 37 is involved in the active site and residues 55, 57 and 59 in the flap in conferring the ability to specifically recognize HIV PR drugs. Ile37Val preserves tertiary structure but prevents steric clashes with the inhibitors. Asn55Met and Val59Ile induce a distinct kink in the flap and a new hydrogen bond to darunavir. Ile98Pro-Ser and Pro100Asn increase 90s loop flexibility, Gln99Val contributes hydrophobic contacts to the inhibitors, and Pro100Asn forms compensatory hydrogen bonds
the two enzymes FIV protease and HIV-1 protease are strikingly similar at the crystallographic level, particularly within the substrate binding region
-
wild-type and mutant enzymes V59I and Q99V are cocrystallized with the C2-symmetric inhibitor TL-3, which contains (1S,2R,3R,4S)-1,4-diamino-1,4-dibenzyl-2,3-diol as the P1-P1' unit and Ala at P3/P3' positions
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D30N
G5I/N55T
-
only 25% loss of activity after 16 h at pH 7.0, 37°C, in 0.2 M NaCl, compared to 65% loss of the wild-type enzyme
G5I/N55T/C84K
-
autoproteolysis-resistant mutant, no significant change in Km or turnover number values between the mutant enzyme and the wild-type enzyme
I35D
I35D/I37V
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/I37V/L97T/I98P/Q99V/P100N/L101I
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/I37V/Q54K/N55M/M56I/I57G/V59I
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/I37V/Q54K/N55M/M56I/I57G/V59I/L97T/I98P/Q99V/
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/I57G
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/M56I
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/Q54K
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D/V59I
-
mutant enzyme shows no activity against either FIV or HIV substrates
I37V
I37V/N55M/M56I/I57G/V59I/G62F/K63I/L97T/I98P/Q99V/P100N/L101I
crystal structure (1.7 A) of FIV protease is obtained in which 12 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR (12XFIV PR). The chimeric PR is crystallized in complex with inhibitor TL-3. Comparison of the crystal structures of the TL-3 complexes of 12X FIV and wild-type FIV PR reveal the information of additional van der Waals interactions between the enzyme inhibitor in the mutant PR. The 12X FIV PR retains the hydrogen bonding interactions between residues in the flap regions and active site involving the enzyme and the TL-3 inhibitor in comparison to both FIV PR and HIV PR. However, the flap regions of the 12X FIV PR more closely resemble those of HIV PR, having gained several stabilizing intra-flap interactions not present in wild type FIV PR
I37V/N55M/V59I/I98P/Q99V/P100N
-
the mutant shows low-level infectivity ex vivo, and after passage, progeny that exhibits a higher growth rate emerged. The mutant enzyme is sensitive to the HIV-1 PR inhibitors lopinavir and darunavir, as well as to the broad-based inhibitor TL-3
I37V/N55M/V59I/I98S/Q99V/P100N
chimeric feline immunodeficiency virus protease that supports infectivity but confers sensitivity to the human immunodeficiency virus protease inhibitors darunavir and lopinavir. The protease has five replacements mimicking homologous residues in HIV protease and a sixth which mutated from Pro to Ser during selection
I57G
I98P
L97T
-
in addition to poor/delayed cleavage at the FIV NC-p2 junction, inefficient processing at the FIV matrix-capsid cleavage junction by the L97T mutant is also observed
M56I
N55D
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
N55M
N55T
-
only 25% loss of activity after 16 h at pH 7.0, 37°C, in 0.2 M NaCl, compared to 65% loss of the wild-type enzyme
Q99V
V59I
D30N
I35D
-
site-directed mutagenesis, the mutant shows about 30% reduced activity compared to the wild-type enzyme
-
I57G
-
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
-
N55D
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
-
additional information
D30N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
I35D
-
mutant enzyme shows no activity against either FIV or HIV substrates
I35D
-
site-directed mutagenesis, the mutant shows about 30% reduced activity compared to the wild-type enzyme
I37V
-
mutant enzyme with full activity. Significant increase in activity against the HIV-I reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type enzyme. Increase in activity against two rapidly cleaved peptides selected by cleavage of phage display library with HIV-I protease. Mutant enzyme compared with wild-type enzyme shows inhibitor specificity more similar to that of the HIV-1 protease
I57G
-
mutant enzyme shows no activity against either FIV or HIV substrates
I57G
-
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
M56I
-
mutant enzyme with full activity. Mutant enzyme compared with wild-type enzyme shows inhibitor specificity more similar to that of the HIV-1 protease
N55M
-
mutant enzyme with full activity. Significant increase in activity against the HIV-I reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type enzyme. Mutant enzyme compared with wild-type enzyme shows inhibitor specificity more similar to that of the HIV-1 protease
N55M
-
the mutant gives processing patterns essentially identical to that of wild type enzyme
Q99V
-
mutant enzyme shows decreased inhibition constant with C2-symmetric inhibitor TL-3 compared to wild-type enzyme
Q99V
-
mutant enzyme with full activit. Significant increase in activity against the HIV-I reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type enzyme. Increase in activity against two rapidly cleaved peptides selected by cleavage of phage display library with HIV-I protease. Mutant enzyme compared with wild-type enzyme shows inhibitor specificity more similar to that of the HIV-1 protease
V59I
-
mutant enzyme shows decreased inhibition constant with C2-symmetric inhibitor TL-3 compared to wild-type enzyme
V59I
-
mutant enzyme with full activity. Significant increase in activity against the HIV-I reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type enzym. Increase in activity against two rapidly cleaved peptides selected by cleavage of phage display library with HIV-I protease. Mutant enzyme compared with wild-type enzyme shows inhibitor specificity more similar to that of the HIV-1 protease
V59I
-
the mutant gives processing patterns essentially identical to that of wild type enzyme
D30N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
additional information
multiple-substitution mutants are constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease. The findings indicate that maintainance of both substrate and inhibitor specificity as a function of interactions between residues both inside and outside the active site
additional information
-
multiple-substitution mutants are constructed by replacing the residues in and around the active site of the enzyme with structurally equivalent residues of HIV-1 protease. The findings indicate that maintainance of both substrate and inhibitor specificity as a function of interactions between residues both inside and outside the active site
additional information
-
construction of cleavage-resistant mutants which have Km-values and turnover numbers similar to those of the wild-type enzyme
additional information
-
generation of autolysis defective mutant enzymes
additional information
-
generation of different FIV PR mutants, by single point mutations and exchange of several amino acids comprising fragments, which show altered substrate specificity to Gag-Pol polyprotein precursor and an altered processing order compared to wild-type enzyme assessed in pseudovirions in transduced cells, FIV PR exchange mutants are much more susceptible to HIV-1 protease inhibitors than the wild-type FIV protease, overview
additional information
-
generation of autolysis defective mutant enzymes
-
additional information
-
generation of different FIV PR mutants, by single point mutations and exchange of several amino acids comprising fragments, which show altered substrate specificity to Gag-Pol polyprotein precursor and an altered processing order compared to wild-type enzyme assessed in pseudovirions in transduced cells, FIV PR exchange mutants are much more susceptible to HIV-1 protease inhibitors than the wild-type FIV protease, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
37°C, 0.2 M NaCl, wild-type enzyme loses 65% of ist activity
647835
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
pH 7.0, 0.2 M NaCl, wild-type enzyme loses 65% of its activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
during purification the recombinant enzyme underwent autoproteolysis to give discrete cleavage products. Construction of cleavage-resistant proteases which have Km and turnover-values similar to thoses of wild-type enzyme
-
recombinant C-terminally His-tagged viral polyprotein from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, unit-length enzyme with the addition of a Met and Ala at the N-terminus. This results in an enzyme with only an additional Ala on the N-terminus with respect to the wild-type enzyme. The N-terminal Met is removed during expression presumably by an Escherichia coli methionine amino peptidase
-
expression of wild-type and mutant FIV PRs in human 293T cells
-
mutant enzmyes V59I, Q99V and G5I/N55T/C84K, expression in Escherichia coli BL21 cells
-
ORF1, recombinant expression of the C-terminally His-tagged viral polyprotein in Escherichia coli strain BL21 (DE3), quantitative RT-PCR expression analysis
the enzyme is encoded in the 5' end of the pol gene of FIV, nucleotide sequence determination, high-level recombinant expression, expression in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
-
PR is an important target for antiviral therapies since PR is reponsible for the processing of viral Gag and Gag-Pol polyproteins into individual structural and enzymatic proteins during assembly and maturation. This proteolytic step is highly specific, ordered and essential for producing mature and infectious retrovirus particles
molecular biology
drug development
-
the enzyme is a model target for development of inhibitors due to its similarity with the HIV-1 retropepsin, overview
drug development
-
the enzyme is a model target for development of inhibitors due to its similarity with the HIV-1 retropepsin, overview
-
molecular biology
-
the FIV-PR mutant is a mutational model system to study the molecular basis of substrate-inhibitor specificity for lentivirus proteases, especially HIV-1 protease
molecular biology
-
the FIV-PR mutant is a mutational model system to study the molecular basis of substrate-inhibitor specificity for lentivirus proteases, especially HIV-1 protease
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
feline immunodeficiency virus, feline immunodeficiency virus (P16088)
brenda
Laco G.S.; Schalk-Hihi C.; Lubkowski J.; Morris G.; Zdanov A.; Olson A.; Elder J.H.; Wlodawer A.; Gustchina A.
Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor
Biochemistry
36
10696-10708
1997
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Lee, T.; Laco, G.S.; Torbett, B.E.; Fox, H.S.; Lerner, D.L.; Elder, J.H.; Wong, C.H.
Analysis of the S3 and S3' subsite specificities of feline immunodeficiency virus (FIV) protease: development of a broad-based protease inhibitor efficacious against FIV, SIV, and HIV in vitro and ex vivo
Proc. Natl. Acad. Sci. USA
95
939-944
1998
feline immunodeficiency virus
brenda
Lee, T.; Le, V.D.; Lim, D.; Lin, Y.C.; Morris, G.M.; Wong, A.L.; Olson, A.J.; Elder, J.H.; Wong, C.H.
Development of a new type of protease inhibitors, efficacious against FIV and HIV variants
J. Am. Chem. Soc.
121
1145-1155
1999
feline immunodeficiency virus (P16088)
-
brenda
Qian, X.; Moris-Varas, F.; Fitzgerald, M.C.; Wong, C.H.
C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases
Bioorg. Med. Chem.
4
2055-2069
1996
feline immunodeficiency virus
brenda
Li, M.; Morris, G.M.; Lee, T.; Laco, G.S.; Wong, C.H.; Olson, A.J.; Elder, J.H.; Wlodawer, A.; Gustchina, A.
Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease
Proteins
38
29-40
2000
feline immunodeficiency virus
brenda
Lin, Y.C.; Beck, Z.; Morris, G.M.; Olson, A.J.; Elder, J.H.
Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases
J. Virol.
77
6589-6600
2003
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Beck, Z.Q.; Lin, Y.C.; Elder, J.H.
Molecular basis for the relative substrate specificity of human immunodeficiency virus type 1 and feline immunodeficiency virus proteases
J. Virol.
75
9458-9469
2001
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Laco, G.S.; Fitzgerald, M.C.; Morris, G.M.; Olson, A.J.; Kent, S.B.; Elder, J.H.
Molecular analysis of the feline immunodeficiency virus protease: generation of a novel form of the protease by autoproteolysis and construction of cleavage-resistant proteases
J. Virol.
71
5505-5511
1997
feline immunodeficiency virus
brenda
Lin, Y.C.; Beck, Z.; Lee, T.; Le, V.D.; Morris, G.M.; Olson, A.J.; Wong, C.H.; Elder, J.H.
Alteration of substrate and inhibitor specificity of feline immunodeficiency virus protease
J. Virol.
74
4710-4720
2000
feline immunodeficiency virus
brenda
Le, V.D.; Mak, C.C.; Lin, Y.C.; Elder, J.H.; Wong, C.H.
Structure-activity studies of FIV and HIV protease inhibitors containing allophenylnorstatine
Bioorg. Med. Chem.
9
1185-1195
2001
feline immunodeficiency virus
brenda
Talbott, R.L.; Sparger E.E.; Lovelace K.M.; Fitch W.M.; Pedersen N.C.; Luciw P.A.; Elder J.H.
Nucleotide sequence and genomic organization of feline immunodeficiency virus
Proc. Natl. Acad. Sci. USA
86
5743-5747
1989
feline immunodeficiency virus (P16088)
brenda
Wlodawer, A.; Gustchina, A.; Reshetnikova, L.; Lubkowski, J.; Zdanov, J.A.; Hui, K.Y.; Angleton, E.L.; Farmerie, W.G.; Goodenow, M.M.; Bhatt, D.; Zhang, L.; Dunn, B.M.
Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus
Nat. Struct. Biol.
2
480-488
1995
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Dunn, B.M.
Feline immunodeficiency virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
178-182
2004
feline immunodeficiency virus, feline immunodeficiency virus FIV
-
brenda
Huitron-Resendiz, S.; De Rozieres, S.; Sanchez-Alavez, M.; Buehler, B.; Lin, Y.C.; Lerner, D.L.; Henriksen, N.W.; Burudi, M.; Fox, H.S.; Torbett, B.E.; Henriksen, S.; Elder, J.H.
Resolution and prevention of feline immunodeficiency virus-induced neurological deficits by treatment with the protease inhibitor TL-3
J. Virol.
78
4525-4532
2004
feline immunodeficiency virus
brenda
Lin, Y.C.; Brik, A.; de Parseval, A.; Tam, K.; Torbett, B.E.; Wong, C.H.; Elder, J.H.
Altered Gag polyprotein cleavage specificity of feline immunodeficiency virus/human immunodeficiency virus mutant proteases as demonstrated in a cell-based expression system
J. Virol.
80
7832-7843
2006
feline immunodeficiency virus, feline immunodeficiency virus FIV
brenda
Heaslet, H.; Lin, Y.C.; Tam, K.; Torbett, B.E.; Elder, J.H.; Stout, C.D.
Crystal structure of an FIV/HIV chimeric protease complexed with the broad-based inhibitor, TL-3
Retrovirology
4
1
2007
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Elder, J.H.; Sundstrom, M.; de Rozieres, S.; de Parseval, A.; Grant, C.K.; Lin, Y.C.
Molecular mechanisms of FIV infection
Vet. Immunol. Immunopathol.
123
3-13
2008
feline immunodeficiency virus
brenda
Lin, Y.C.; Torbett, B.E.; Elder, J.H.
Generation of infectious feline immunodeficiency virus (FIV) encoding FIV/human immunodeficiency virus chimeric protease
J. Virol.
84
6799-6809
2010
feline immunodeficiency virus
brenda
Luttge, B.G.; Freed, E.O.
FIV Gag: virus assembly and host-cell interactions
Vet. Immunol. Immunopathol.
134
3-13
2010
feline immunodeficiency virus
brenda
Lin, Y.C.; Perryman, A.L.; Olson, A.J.; Torbett, B.E.; Elder, J.H.; Stout, C.D.
Structural basis for drug and substrate specificity exhibited by FIV encoding a chimeric FIV/HIV protease
Acta Crystallogr. Sect. D
67
540-548
2011
feline immunodeficiency virus (P16088), feline immunodeficiency virus
brenda
Yoshikawa, R.; Takeuchi, J.S.; Yamada, E.; Nakano, Y.; Misawa, N.; Kimura, Y.; Ren, F.; Miyazawa, T.; Koyanagi, Y.; Sato, K.
Feline immunodeficiency virus evolutionarily acquires two proteins, Vif and protease, capable of antagonizing feline APOBEC3
J. Virol.
91
e00250-17
2017
feline immunodeficiency virus (A0A059UHW3), feline immunodeficiency virus
brenda
Fumian, T.; Tuipulotu, D.; Netzler, N.; Lun, J.; Russo, A.; Yan, G.; White, P.
Potential therapeutic agents for feline calicivirus infection
Viruses
10
433
2018
feline calicivirus (Q66914), feline calicivirus
brenda
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