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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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Lys-Ser-Gly-Val-Phe-His-Val-Asn-Gly-Lys + H2O
Lys-Ser-Gly-Val-Phe + His-Val-Asn-Gly-Lys
-
-
?
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
-
-
?
Lys-Ser-Gly-Val-Phe-Val-Val-Asn-Gly-Lys + H2O
Lys-Ser-Gly-Val-Phe + Val-Val-Asn-Gly-Lys
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Thr-Ile-Met-Met-Gln-Arg + H2O
Thr-Ile-Met + Met-Gln-Arg
-
-
-
?
Ac-RPQAYPIQTR-NH2 + H2O
Ac-RPQAY + PIQTR-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 FIV
-
-
?
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
-
-
-
?
feline apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 protein + H2O
?
Gag-Pol polyprotein + H2O
?
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly + H2O
Ile-Arg-Lys-Ile-Leu + Phe-Leu-Asp-Gly
-
-
-
?
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR + H2O
RALTK(epsilon-ABZ)VQ + F(NO2)VQSKGR
-
the synthetic peptide substrate mimicks the capsid/nucleocapsid cleavage site
-
-
?
RKEEGPPQAYPIQTVNGPQYR + H2O
RKEEGPPQAY + PIQTVNGPQYR
-
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
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
Gag-Pol polyprotein + H2O
?
-
-
-
-
?
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
?
-
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
?
-
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
-
-
?
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
-
-
?
additional information
?
-
-
substrate specificity, cleavage sites of synthetic peptides corresponding to the natural cleavage sites of the Gag-Pol polyprotein, overview
-
-
?
additional information
?
-
-
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
-
-
?
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Ac-Gly-Ser-Gly-Val-Phe-Psi[CH2NH2]-Val-Val-Asn-Gly-Leu
-
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-[benzyloxycarbonyl]-L-Ala-N-[(1S)-1-benzyl-2-hydroxyethyl]-L-valinamide
ie. TL-3
(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-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
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
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
saquinovir
-
weak inhibition of wild-type protease
[(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
[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
LP-149
-
LP-149
i.e. Ac-NA-Val-Sta-Glu-NA-NH2
protease inhibitor TL-3
-
IC50: 90 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
[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
-
-
[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
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
-
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
-
FIV PR exchange mutants are much more susceptible to HIV-1 protease inhibitors than the wild-type FIV protease
-
additional information
-
structural features of compounds with high inhibitory potency, overview, e.g. small P3 residues results in highly inhibitory compounds
-
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
-
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0.0204
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
pH 5.25, wild-type enzyme
0.013
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln-Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2
-
0.0056 - 0.271
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
0.462 - 1.845
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
0.033
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR
-
pH 5.3, 0.2 M NaCl, 0.1 mM EDTA, 1 mM DTT
10
RKEEGPPQAYPIQTVNGPQYR
-
pH 5.3, 37°C, 1 M NaCl
additional information
additional information
-
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
0.0205
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.01
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
pH 5.25, wild-type enzyme
0.11
Arg-Ala-Leu-Thr-Lys-(4-aminobenzoic acid)-Val-Gln-Phe-(NO2)-Val-Gln-Ser-Lys-Gly-Arg-NH2
-
0.0015 - 0.0223
Ala-Leu-Thr-Lys-Val-Gln-Val-Val-Gln-Ser-Lys-Gly
0.945 - 4
Ile-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly
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
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
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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
0.000128
(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
0.00031
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
0.00009
protease inhibitor TL-3
feline immunodeficiency virus
-
IC50: 90 nM
0.0001
TL3
feline immunodeficiency virus
-
IC50: 100 nM
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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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/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
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/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/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
L101I
-
mutant enzyme with dramatically reduced activity
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
N55D
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
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
P100N
-
the mutant shows low-level infectivity
Q64K
-
mutant enzyme with dramatically reduced activity
D30N
-
D30N
inactive mutant enzyme
D30N
-
inactive mutant
D30N
-
mutant enzyme can bind substrate but is inactive
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
I37V
-
mutation near the active core
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
I98P
-
mutant enzyme with dramatically reduced activity
I98P
-
the mutant shows low-level infectivity
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
M56I
-
the mutant cleaves the FIV nucleocapsid-p2 site poorly
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
Q99V
-
the mutant shows low-level infectivity
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
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
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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.
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