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(2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR + H2O
(2-(N-methylamino)benzoyl)-IEALFQ + GPPK(2,4-dinitrophenyl)-FR
most efficient substrate
-
-
?
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate + H2O
?
-
slowly turned over
-
-
?
2-(N-methylamino)benzoyl-DEAMEQGVSDYIK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-DEAMEQ + GVSDYIK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-IAALFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IAALFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
2-(N-methylamino)benzoyl-IEALAQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALAQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEALFQSPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALFQ + SPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEALKQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEALKQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IEFLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEFLFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
2-(N-methylamino)benzoyl-LFAGFQGAYSGAK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-LFAGFQ + GAYSGAK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-QTGTIQGDRVADK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-QTGTIQ + GDRVADK-2,4-dinitrophenyl
poor substrate
-
-
?
2-(N-methylamino)benzoyl-RQAVTQGFPTELK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-RQAVTQ + GFPTELK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-RTATVQGPSLDFK-2,4-dinitrophenyl + H2O
2-(N-methylamino)benzoyl-RTATVQ + GPSLDFK-2,4-dinitrophenyl
-
-
-
?
2-(N-methylamino)benzoyl-TSAVLQSGFRK-(2,4-dinitrophenyl)-Met + H2O
2-(N-methylamino)benzoyl-TSAVLQ + SGFRK-(2,4-dinitrophenyl)-Met
-
-
-
?
2-aminobenzoic acid-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
?
-
-
-
-
?
2-aminobenzoic acid-Phe-Thr-Gln-Ser-Glu-Gly-Glu-Phe(NO2)-Ala + H2O
?
-
poor substrate
-
-
?
2-aminobenzoyl-AALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-AALFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EAAFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EAAFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALAQGPLQ-EDDnp + H2O
2-aminobenzoyl-EALAQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQAPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + APLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGALQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GALQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGPAQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPAQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-EALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPLQ-EDDnp
-
-
-
-
?
2-aminobenzoyl-Nle-Nle-Nle-Glu-Ala-Leu-Phe-Gln-Gly-Pro-(4-nitro)Phe + H2O
2-aminobenzoyl-Nle-Nle-Nle-Glu-Ala-Leu-Phe-Gln + Gly-Pro-(4-nitro)Phe
-
synthetic peptide spanning the 2C/3A cleavage region of poliovirus polyprotein
-
?
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQSGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQ + SGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
fluorogenic substrate
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-ASFMNQSKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-ASFMNQ + SKVRRFE-5'-[(2-aminoethyl)amino] naphthalene-1-sulfonic acid
YP_007969882
the fluorometric substrate is cleaved by the 3C protease at the 2C-3A junction, which is derived from the native protease cleavage site within the DHAV polyprotein
-
-
?
5-bromopyridin-3-yl furan-3-carboxylate + H2O
?
-
slowly turned over
-
-
?
5-chloropyridin-3-yl furan-2-carboxylate + H2O
?
-
slowly turned over
-
-
?
7-methoxycoumarin-4-yl-MEALFQGPLQY-2,4-dinitrophenyl amide + H2O
?
-
-
-
-
?
Abz-EALFQGPLQ-EDDnp + H2O
Abz-EALFQ + GPLQ-EDDnp
-
-
-
-
?
abz-SVTLQSGY(NO2)R + H2O
?
-
fluorogenic substrate
-
-
?
Ac-DEFQLQ-4-nitroanilide + H2O
?
-
-
-
?
Ac-EFQLQ-4-nitroanilide + H2O
?
-
-
-
?
Ac-FQLQ-4-nitroanilide + H2O
?
-
-
-
?
Ac-RHSVGATLEALFQGPPVYREIKIS-NH2 + H2O
Ac-RHSVGATLEALFQ + GPPVYREIKIS-NH2
-
-
-
-
?
acetyl-Arg-Pro-Val-Val-Val-Gln-Gly-Pro-Asn-NH2 + H2O
?
-
human rhinovirus
-
-
?
acetyl-Arg-Ser-Tyr-Phe-Ala-Gln-Ile-Gln-Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2 + H2O
acetyl-Arg-Ser-Tyr-Phe-Ala-Gln-Ile-Gln + Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3C/3D
-
?
acetyl-Asn-Cys-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Asn-Cys-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2C/3A
-
?
acetyl-ELRTQSFS-NH2 + H2O
?
-
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Gly-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Gly-NH2
-
as good as acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-NH2
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-NH2
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
-
sequence corresponding to 2C/3A cleavage site of polyprotein
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + NH3
-
cleavage with reduced but significant efficiency, better substrate than acetyl-Glu-Ala-Leu-Phe-Gln-Gly-NH2
-
?
acetyl-Glu-Ile-Pro-Tyr-Ala-Ile-Glu-Gln-Gly-Asp-Ser-Trp-Leu-Lys-Lys-Phe-NH2 + H2O
acetyl-Glu-Ile-Pro-Tyr-Ala-Ile-Glu-Gln + Gly-Asp-Ser-Trp-Leu-Lys-Lys-Phe-NH2
-
best substrate, corresponding to poliovirus type 2 polyprotein cleavage site 2B/2C
-
?
acetyl-Glu-Leu-Arg-Thr-Gln-Ser-Phe-Ser-NH2 + H2O
?
acetyl-Ile-Arg-Thr-Ala-Lys-Val-Gln-Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2 + H2O
acetyl-Ile-Arg-Thr-Ala-Lys-Val-Gln + Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3B/3C
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
acetyl-Thr-Ile-Arg-Thr-Ala-Lys-Val-Gln-Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2 + H2O
acetyl-Thr-Ile-Arg-Thr-Ala-Lys-Val-Gln + Gly-Pro-Gly-Phe-Asp-Tyr-Ala-Val-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3B/2C
-
?
acetyl-Tyr-Glu-Glu-Glu-Ala-Met-Glu-Gln-Gly-Ile-Ser-Asn-Tyr-Ile-Glu-Ser-NH2 + H2O
acetyl-Tyr-Glu-Glu-Glu-Ala-Met-Glu-Gln + Gly-Ile-Ser-Asn-Tyr-Ile-Glu-Ser-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2A/2B
-
?
acetyl-Tyr-Lys-Leu-Phe-Ala-Gly-His-Gln-Gly-Ala-Tyr-Thr-Gly-Leu-Phe-Asn-NH2 + H2O
acetyl-Tyr-Lys-Leu-Phe-Ala-Gly-His-Gln + Gly-Ala-Tyr-Thr-Gly-Leu-Phe-Asn-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 3A/3B
-
?
activated transcription factor TFIIIC + H2O
?
APAKELLNFD + H2O
APAKE + LLNFD
-
-
-
-
?
APAKQLLNFD + H2O
APAKQ + LLNFD
-
-
-
-
?
Asp-Ser-Leu-Glu-Thr-Leu-Phe-Gln-Gly-Pro-Val-Tyr-Lys-Asp-Leu-Glu + H2O
Asp-Ser-Leu-Glu-Thr-Leu-Phe-Gln + Gly-Pro-Val-Tyr-Lys-Asp-Leu-Glu
-
represents 2C/3A cleavage site, wild-type and E71D, D85N, K155E mutants, not other mutants
-
?
Bid protein + H2O
?
-
-
-
-
?
cAMP-regulated response element binding protein + H2O
?
-
-
-
-
?
cAMP-responsible element binding protein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
CstF-64 protein + H2O
?
-
CstF-64 protein is short for cleavage stimulation factor, 39 pre-RNA, subunit 2, 64 kD. The 3Cpro cleavage sites are located at position 251 in the N-terminal P/G-rich domain and at multiple positions close to the C-terminus of CstF-64 (around position 500)
-
-
?
Dabcyl-APAKQLLD(Edans)FDLLK + H2O
Dabcyl-APAKQ + LLD(Edans)FDLLK
-
-
-
-
?
Dabcyl-GLRTQSFS-EDANS + H2O
?
-
fluorogenic substrate, hydrolysis at the glutamine residue
-
-
?
dabcyl-GLRTQSND + H2O
?
-
fluorogenic peptide substrate
-
-
?
dabcyl-GLRTQSND(EDANS)G + H2O
?
-
fluorogenic substrate
-
-
?
Dabcyl-IEALFQGPPKFRE-Edans + H2O
Dabcyl-IEALFQ + GPPKFRE-Edans
-
-
-
?
Dabcyl-KEALFQGPPQFE-Edans + H2O
Dabcyl-KEALFQ + GPPQFE-Edans
Dabcyl-KIGNTIEALFQGPPKFRE-EDANS + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-EDANS
Dabcyl-KRTATVQGPSLDFE-Edans + H2O
Dabcyl-KRTATVQ + GPSLDFE-Edans
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVL + QSGFRKME-EDANS
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
Dabcyl-RTATVQGPSLDFE-EDANS + H2O
Dabcyl-RTATVQ + GPSLDFE-EDANS
-
-
-
?
Dabcyl-RTATVQGPSLDFKE-Edans + H2O
Dabcyl-RTATVQ + GPSLDFKE-Edans
-
-
-
?
Dabcyl-TAKVQGPGFD-Edans + H2O
Dabcyl-TAKVQ + GPGFD-Edans
Dabcyl-TSAVLQSGFRKM-Edans + H2O
Dabcyl-TSAVLQ + SGFRKM-Edans
poor substrate
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
DEAMEQGVSDYI + H2O
DEAMEQ + GVSDYI
-
-
-
-
?
DRRETLFQ-4-nitroanilide + H2O
DRRETLFG + 4-nitroaniline
-
-
-
-
?
DSLETLFQ-4-nitroanilide + H2O
DSLETLFG + 4-nitroaniline
-
-
-
-
?
DSLEVLFQ-4-nitroanilide + H2O
DSLEVLFG + 4-nitroaniline
-
-
-
-
?
DSRETLFQ-4-nitroanilide + H2O
DSRETLFG + 4-nitroaniline
-
-
-
-
?
EALFQ-4-nitroanilide + H2O
EALFG + 4-nitroaniline
-
-
-
-
?
Edans-DFHLQGP-Dabcyl + H2O
Edans-DFHLQ + GP-Dabcyl
-
-
-
-
?
EDANS-EDFHLQGPEDLAK-Dabcyl + H2O
EDANS-EDFHLQ + GPEDLAK-Dabcyl
-
-
-
-
?
eIF4GI + H2O
?
-
cleavage in baby hamster kidney cells and 3T3 cells, cleavage can occur either on the full-length protein or on the primary cleavage product that is generated by Lpro, human and green monkey eIF4GI is resistant to the action of 3Cpro, a single amino acid substitution renders human eIF4GI sensitive to 3Cpro
-
-
?
encephalomyocarditis virus polyprotein + H2O
?
-
cleavage sites: Gln-Gly, Glu-Ser and Glu-Ala
-
-
?
enterovirus polyprotein + H2O
?
ERGIC53 protein + H2O
?
-
-
-
-
?
ETLFQ-4-nitroanilide + H2O
ETLFG + 4-nitroaniline
-
-
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
eukaryotic translation initiation factor 4Gl + H2O
?
-
-
-
-
?
EVLFQ-4-nitroanilide + H2O
EVLFG + 4-nitroaniline
-
-
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
foot-and-mouth disease virus capsid precursor (P1-2A) + H2O
foot-and-mouth disease virus protein VP0 + foot-and-mouth disease virus protein VP3 + foot-and-mouth disease virus protein VP1 + foot-and-mouth disease virus protein 2A
-
cleavages at the three junctions (VP0/VP3, VP3/VP1, and VP1/2A) within the foot-and-mouth disease virus capsid precursor (P1-2A) by the 3C protease are mutually independent
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
foot-and-mouth-disease virus P1 precursor polyprotein + H2O
mature structural foot-and-mouth-disease virus proteins
-
recombinant foot-and-mouth-disease virus enzyme, cleaves VP3-VP1 site, followed by VP0-VP3 and VP1-2A site (least efficiently), kinetic of P1 processing
VPO-VP3 + VP1-2A (enzyme from supernatant), VPO + VP3 + VP1 (pellet enzyme)
?
foot-and-mouth-disease virus P1-2A polyprotein + H2O
mature structural foot-and-mouth-disease virus proteins
-
recombinant foot-and-mouth-disease virus enzyme, cleaves VP3-VP1 site initially, followed by VP0-VP3 and VP1-2A site (least efficiently), kinetic of P1-processing
VPO-VP3 + VP1-2A (enzyme from supernatant), VPO + VP3 + VP1 (pellet enzyme)
?
foot-and-mouth-disease virus P2 precursor protein + H2O
foot-and-mouth-disease virus protein 2B + foot-and-mouth-disease virus protein 2C + foot-and-mouth-disease virus protein 2A-2B
-
-
-
?
Glu-Ala-Ile-Ala-Glu-Glu-Gln-Gly-Leu-Ser-Asp-Tyr-Ile-Thr + H2O
?
-
synthetic peptide spanning the 2A/2B cleavage region of human rhinovirus polyprotein
-
-
?
Glu-Ala-Leu-Phe-Gln-4-nitroanilide + H2O
Glu-Ala-Leu-Phe-Gln + 4-nitroaniline
-
-
-
-
?
Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
-
represents 2C/3A cleavage site, wild-type and C147S mutant, the latter with very reduced activity
-
?
hepatitis A virus deltaP1-2AB polyprotein fragment + H2O
hepatitis A virus protein 2A + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2BC + hepatitis A virus protein 2 + hepatitis A virus protein 2B
-
C-terminally truncated protein
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
hepatitis A virus deltaVP1-P2-P3*my polyprotein fragment + H2O
hepatitis A virus protein 2BC + hepatitis A virus proteins P3*my + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
C-terminally truncated protein, proteolytically inactive substrate, kinetics, yields the same products as active polyprotein precursor deltaVP1-P2-P3*
P3my and deltaVP1-2A are intermediates
?
hepatitis A virus P1-2AB* polyprotein fragment + H2O
hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A
-
C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC
-
?
hepatitis A virus P1-2ABC* polyprotein fragment + H2O
hepatitis A virus protein VP3 + hepatitis A virus proteins VP0 + hepatitis A virus proteins VP1-2A + hepatitis A virus proteins VP0-VP3 + hepatitis A virus proteins P1-2A + hepatitis A virus proteins 2A + hepatitis A virus proteins 2BC
-
C-terminally truncated protein, cleavage sites: VPO/VP3, VP3/VP1, 2A/2B, less efficient are VP1/2A and 2B/2C, via 2BC
-
?
hepatitis A virus P1-P2 precursor polyprotein + H2O
hepatitis A virus protein 2A + hepatitis A virus protein 2B + hepatitis A virus protein 2C + hepatitis A virus protein 3ABC + hepatitis A virus protein 3D
-
most effective cleavage at 2A/2B and 2C/3A sites
via respective intermediate products
?
hepatitis A virus P2-P3 precursor polyprotein + H2O
?
-
trans-cleavage, rapid cleavage at P2/P3 junction, the 3A/3B, 3B/3C and 3C/3D sites are less efficiently cleaved, the hepatitis A virus enzyme has a broader activity profile than enzymes of other picornaviruses, recombinant enzyme cleaves all putative cleavage sites of the polyprotein
-
-
?
hepatitis A virus polyprotein + H2O
?
hepatitis A virus polyprotein + H2O
hepatitis A virus protein P1-2A + hepatitis A virus protein P3 + hepatitis A virus protein 2BC + hepatitis A virus protein 3D + hepatitis A virus protein 3ABC
-
cleavage of P2-P3 domain, cleaves primary cleavage site and all secondary sites within P2 as well as the 3C/3D junction
followed by hepatitis A virus protein 2B and hepatitis A virus protein 2C and later by hepatitis A virus protein VP0 and hepatitis A virus protein VP3, enzyme-concentration dependent product formation
?
histone H3 protein + H2O
?
-
-
-
-
?
histone protein H3 + H2O
?
-
in BHK-cells, foot-and-mouth-disease virus enzyme
-
-
?
host zinc-finger antiviral protein + H2O
?
-
cleavage specifically at Gln369, ZAP cleavage is dependent on its amino acid pair Q369 and G370
-
-
?
human rhinovirus 3CD polyprotein fragment + H2O
?
-
recombinant enzyme HRV-14, structure/mechanism study
-
-
?
human rhinovirus polyprotein + H2O
1AB/1C/1D/2C/delta3CD
-
-
-
-
?
IEALFQGPPKFR + H2O
IEALFQ + GPPKFR
-
-
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
in vitro-translated (35S)methionine-labeled transcription factor cyclic AMP-responsive element binding protein + H2O
?
-
-
-
-
?
interferon regulatory factor 7 + H2O
?
-
cleavage occurs at the Q189-S190 junction within the constitutive activation domain
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
L-P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1-2A
-
cardioviruses
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
Lys-Gly-Leu-Phe-Ser-Gln-Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr + H2O
Lys-Gly-Leu-Phe-Ser-Gln + Ala-Lys-Ile-Ser-Leu-Phe-Tyr-Thr
-
-
-
?
membrin + H2O
?
-
-
-
-
?
mitochondrial antiviral signaling protein + H2O
?
-
3Cpro-mediated MAVS cleavage occurs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling
-
-
?
N-acetyl-DEFQLQ-4-nitroanilide + H2O
N-acetyl-DEFQLQ + 4-nitroaniline
-
-
-
-
?
nuclear factor-kappaB essential modulator + H2O
?
-
the enzyme cleaves the substrate at the Q304 residue, negating its signaling adaptor function
-
-
?
nucleoporin + H2O
?
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1 + peptide 2A
-
cardio- and aphthoviruses
-
?
peptides derived from polyprotein cleavage sites + H2O
?
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
poliovirus P1 precursor polyprotein + H2O
capsid proteins
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
poly(A) binding protein + H2O
?
-
the enzyme cleaves poly(A) binding protein within the C-terminal domain at Q437/G438
-
-
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
-
contains 2 main cleavage sites for 3C proteinase within the proline-rich linker domain, cleavage of recombinant protein with 3C proteinase heavily favors the 3Cpro primary cleavage site Q537/G538 over the 3CAlt cleavage site Q413/T414
-
-
?
Poly(A)-binding protein + H2O
?
-
3Cpro removes the C-terminal domain that interacts with several translation factors, in HeLa cells 3Cpro inhibits translation of endogenous mRNAs and reporter RNA, 3Cpro-mediated translation inhibition can be restored by the addition of exogenous poly(A)-binding protein
-
-
r
poly(A)-binding protein + H2O
fragments of poly(A)-binding protein
-
inhibition of viral internal ribosome entry site-mediated translation, cleavage of poly(A)-binding protein by 3Cpro is a necessary component for host translation shutoff
-
-
?
poly-(ADP-ribose) polymerase + H2O
?
-
-
-
-
?
polypeptide translated from plasmid DNA T7-delta3A-3B-3Cmut-delta3D
delta3A-3B-3Cmut + 3Cmut-delta3D + 3B-3Cmut-delta3D
-
-
-
-
?
pro-caspase 3 + H2O
caspase 3 + ?
-
-
-
-
?
QTGTIQGDRVAD + H2O
QTGTIQ + GDRVAD
-
-
-
-
?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
-
-
-
-
?
receptor-interacting protein kinase 1 + H2O
?
receptor-interacting protein kinase-1 + H2O
?
rhinovirus polyprotein + H2O
?
-
cleavage specificity
-
-
?
RNA polymerase I factor SL-1 + H2O
?
-
-
-
-
?
RQAVTQGFPTEL + H2O
RQAVTQ + GFPTEL
-
-
-
-
?
SLEVLFQGPVRR + H2O
SLEVLFQ + GPVRR
-
-
-
-
?
TATA binding protein + H2O
?
-
-
-
-
?
TATA-binding protein + H2O
?
-
-
-
-
?
TENLYFQSGTRR + H2O
TENLYFQ + SGTRR
-
-
-
-
?
Thr-Gly-Leu-Phe-Gln-Gly-Pro + H2O
Thr-Gly-Leu-Phe-Gln + Gly-Pro
-
-
-
-
?
TLFQ-4-nitroanilide + H2O
TLFG + 4-nitroaniline
-
-
-
-
?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O
?
-
3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm
-
-
?
transcription factor OCT-1 + H2O
?
TRIF protein + H2O
?
-
-
-
-
?
TSAVLQSGFRKM + H2O
TSAVLQ + SGFRKM
-
-
-
-
?
TTLEALFQGPPVY + H2O
?
-
-
-
-
?
viral 3CD protein + H2O
?
-
-
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
YFCSEQGEIQWN + H2O
YFCSEQ + GEIQWN
-
-
-
-
?
additional information
?
-
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IEAAFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IEAAFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
-
-
-
?
2-(N-methylamino)benzoyl-IELLFQGPPK(2,4-dinitrophenyl)FR + H2O
2-(N-methylamino)benzoyl-IELLFQ + GPPK(2,4-dinitrophenyl)FR
poor substrate
-
-
?
acetyl-Glu-Leu-Arg-Thr-Gln-Ser-Phe-Ser-NH2 + H2O
?
-
-
-
-
?
acetyl-Glu-Leu-Arg-Thr-Gln-Ser-Phe-Ser-NH2 + H2O
?
-
hepatitis A virus
-
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to amino acid sequence flanking 2C/3A cleavage site, wild-type and mutant D85N enzyme
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to poliovirus type 2 polyprotein cleavage site 2C/3A
-
?
acetyl-Met-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2 + H2O
acetyl-Met-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Leu-Gln-Tyr-Lys-Asp-Leu-NH2
-
corresponding to amino acid sequence flanking 2C/3A cleavage site, wild-type and mutant D85N enzyme
-
?
activated transcription factor TFIIIC + H2O
?
-
in HeLa-cells, poliovirus enzyme
-
-
?
activated transcription factor TFIIIC + H2O
?
-
in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
cleavage specificity
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
cardiovirus polyprotein + H2O
?
-
-
-
-
?
Dabcyl-KEALFQGPPQFE-Edans + H2O
Dabcyl-KEALFQ + GPPQFE-Edans
-
best substrate
-
-
?
Dabcyl-KEALFQGPPQFE-Edans + H2O
Dabcyl-KEALFQ + GPPQFE-Edans
-
best substrate
-
-
?
Dabcyl-KIGNTIEALFQGPPKFRE-EDANS + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-EDANS
-
-
-
-
?
Dabcyl-KIGNTIEALFQGPPKFRE-EDANS + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-EDANS
-
-
-
-
?
Dabcyl-KRTATVQGPSLDFE-Edans + H2O
Dabcyl-KRTATVQ + GPSLDFE-Edans
-
-
-
?
Dabcyl-KRTATVQGPSLDFE-Edans + H2O
Dabcyl-KRTATVQ + GPSLDFE-Edans
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVL + QSGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVL + QSGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-EDANS + H2O
Dabcyl-KTSAVLQ + SGFRKME-EDANS
-
-
-
-
?
Dabcyl-TAKVQGPGFD-Edans + H2O
Dabcyl-TAKVQ + GPGFD-Edans
-
-
-
-
?
Dabcyl-TAKVQGPGFD-Edans + H2O
Dabcyl-TAKVQ + GPGFD-Edans
-
-
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
?
dansyl-Glu-Glu-Glu-Ala-Met-Glu-Gly-Ile-Thr-Asn-Lys-NH2 + H2O
dansyl-Glu-Glu-Glu-Ala-Met-Glu + Gly-Ile-Thr-Asn-Lys-NH2
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
cleavage specificity
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
enterovirus polyprotein + H2O
?
-
-
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
-
cleaveage at a single site, rabbit eIF5B is proteolytically cleaves during coxsackievirus infection of cultured cells, beginning at 3 h post-infection and increasing thereafter
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
-
cleaveage at a single site, rabbit eIF5B is proteolytically cleaves during poliovirus infection of cultured cells, beginning at 3 hours post-infection and increasing thereafter
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.93
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.7
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.45
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.11
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.79
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.65
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 18.65
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 14.22
-
-
?
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.902
-
-
?
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.902
-
-
?
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
-
cleavage efficacy (micromol/l/min): 0.3
-
-
?
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
-
cleavage efficacy (micromol/l/min): 0.3
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
-
cleavage efficacy (micromol/l/min): 5.77
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
-
reference peptide, cleavage efficacy (micromol/l/min): 5.08
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.27
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.21
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
-
3Cpro is only weakly selective for Gln over Glu, most susceptible peptides correspond to the VP1/2A and 2B/2C junctions, which were completely cleaved within 6 hours, whereas peptides corresponding to the VP2/VP3, 2C/3A, 3A/3B1, 3B1/3B2 and 3B2/3B3 junctions were uncleaved after 24 hours incubation
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
-
3Cpro is only weakly selective for Gln over Glu, most susceptible peptides correspond to the VP1/2A and 2B/2C junctions, which were completely cleaved within 6 hours, whereas peptides corresponding to the VP2/VP3, 2C/3A, 3A/3B1, 3B1/3B2 and 3B2/3B3 junctions were uncleaved after 24 hours incubation
-
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
putative primary cleavage sites within P2 region are VP1-2A, 2A/2B, i.e. Gln745-Ser and Gln836-Ala
-
-
?
hepatitis A virus deltaVP1-P2-P3 polyprotein fragment + H2O
hepatitis A virus proteins2BC + hepatitis A virus proteins P3* + hepatitis A virus proteins 2B + hepatitis A virus proteins deltaVP1-2A + hepatitis A virus proteins 2A
-
deltaVP1-P2-P3*, C-terminally truncated protein
-
?
hepatitis A virus polyprotein + H2O
?
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
hepatitis A virus polyprotein + H2O
?
-
involved in primary cleavages yielding precursors of structural proteins, it mediates all secondary cleavages yielding mature structural and functional proteins
-
-
?
hepatitis A virus polyprotein + H2O
?
-
processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner
-
-
?
hepatitis A virus polyprotein + H2O
?
-
the enzyme is essential for cleavage of the initially synthesized viral polyprotein precursor to mature fragents and is therefore required for viral replication in vivo
-
-
?
hepatitis A virus polyprotein + H2O
?
-
the enzyme is responsible for the processing of the viral polyprotein
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
-
cleavage efficacy (micromol/l/min): 10.72
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
-
cleavage efficacy (micromol/l/min): 8.37
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
-
cleavage efficacy (micromol/l/min): 0.063
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
-
cleavage efficacy (micromol/l/min): 0.055
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
-
cleavage efficacy (micromol/l/min): 4.3
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
-
cleavage efficacy (micromol/l/min): 4.1
-
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
-
cleavage efficacy (micromol/l/min): 5.09
-
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
-
cleavage efficacy (micromol/l/min): 5.01
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
-
cleavage efficacy (micromol/l/min): 9.78
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
-
cleavage efficacy (micromol/l/min): 8.26
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
-
cleavage efficacy (micromol/l/min): 0.23
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
-
cleavage efficacy (micromol/l/min): 0.22
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
most maturation cleavages within the precursor polyprotein are mediated by the enzyme
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
essential for processing of virus polyprotein containing structural proteins and enzymes including the protease 3C itself
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
the enzyme is essential for viral replication and infectivity
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage specificity, cleavage at Glx-Gly, where Gly can be replaced by Ser, Thr, Ala, Val or Met, other picornaviruses than poliovirus
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
involved in proteolytic processing of virus polyprotein
-
-
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
-
in-cis cleavage, autocatalytical processing, cleavage sites: 3A/3B and 3B/3C, in-cis cleavage ability of D85N mutant severely impaired
poliovirus protein 3B is only 22 amino acids long and not detected in the assay
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
-
in-cis cleavage, autocatalytical processing, cleavage sites: 3A/3B and 3B/3C, in-cis cleavage ability of D85N mutant severely impaired
poliovirus protein 3B is only 22 amino acids long and not detected in the assay
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
-
-
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
-
trans-cleavage
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
exclusive cleavage site: Gln-Gly
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
cleavage map
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
initial cleavage at 2C-3A and 2B-2C, followed by 3A-3B and/or 3C-3D
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
proteolytic autocatalysis
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
protease 2A cleavage at COOH-terminal Tyr-Gly bond of P1, i.e. P1/P2 junction, may be necessary before this region of the polyprotein serves as substrate for protease 3C
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
essential for processing of virus polyprotein containing strucutral proteins and enzymes including the protease 3C itself
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
the polyprotein is cleaved into mature proteins predominantly by the viral 3C protease
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
protease 2A cleavage at COOH-terminal Tyr-Gly bond of P1, i.e. P1/P2 junction, may be necessary before this region of the polyprotein serves as substrate for protease 3C
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
-
in-trans cleavage, wild-type and mutant D85N enzyme
-
-
?
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
-
in-trans cleavage, wild-type and mutant D85N enzyme
-
-
?
receptor-interacting protein kinase 1 + H2O
?
-
cleavage of the RIPK1 death-domain, and generation of N-terminal RIPK1 fragments
-
-
?
receptor-interacting protein kinase 1 + H2O
?
-
in vitro cleavage of RIPK1 by 3Cpro in HeLa cell extracts, cleavage of the RIPK1 death-domain, and generation of N-terminal RIPK1 fragments. The middle p62/SQSTM1 binding domain of RIPK1 contains three strictly defined HRV 3Cpro consensus motifs [AVNTPISQ]-x-x-Q-[GNSA]-[PLDIQEVAN] at Q401, Q464, and Q573. 3Cpro cleaves parts of the middle domain and the C-terminus of RIPK1. Enzyme 3Cpro generates a 60 kDa N-terminal RIPK1 fragment
-
-
?
receptor-interacting protein kinase-1 + H2O
?
i.e. RIPK1
-
-
?
receptor-interacting protein kinase-1 + H2O
?
i.e. RIPK1, HRV 3C protease cleaves RIPK1 to produce a 23 kDa cleavage product
-
-
?
transcription factor OCT-1 + H2O
?
-
-
-
-
?
transcription factor OCT-1 + H2O
?
-
cleaved by 3Cpro, precursor 3CD and mutant 3CD delta371
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
-
cleavage efficacy (micromol/l/min): 0.63
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
-
cleavage efficacy (micromol/l/min): 0.56
-
-
?
additional information
?
-
YP_007969882
optimization of in vitro cleavage assay method with a fluorogenic peptide substrate derived from the cleavage site of the DHAV polyprotein, overview
-
-
?
additional information
?
-
-
optimization of in vitro cleavage assay method with a fluorogenic peptide substrate derived from the cleavage site of the DHAV polyprotein, overview
-
-
?
additional information
?
-
-
no hydrolysis of acetyl-Glu-Ala-Leu-Phe-Glu-Gly-Pro
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
all catalytic-site mutations result in reduction or inactivation of autocatalytic cleavage of recombinant 3C precursor protein, Cys147 to Ala mutant is inactive, Cys147 to Ser has reduced in-cis and in-trans activity
-
-
?
additional information
?
-
-
cleavage of purified fusion proteins by immobilised protease
-
-
?
additional information
?
-
-
no activity with cellular protein MAVS
-
-
?
additional information
?
-
-
does not cleave death-associated protein 5
-
-
?
additional information
?
-
-
no activity with cellular protein MAVS
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
non-proteolytic function: wild-type and H40D, E71A, C16S mutant enzymes bind specifically to 5'-noncoding region of viral RNA, not D85E or D85N mutant enzymes
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
3Cpro possess RNA-binding activity, the regions responsible for RNA binding are KFRDI (positions 82-86) and VGK (positions 154-156)
-
-
?
additional information
?
-
-
chymotrypsin-like protease is required for viral replication
-
-
?
additional information
?
-
-
picornavirus 3Cpro generally cleaves peptides at the Gln/Gly junction
-
-
?
additional information
?
-
-
no activity with cellular protein MAVS
-
-
?
additional information
?
-
-
no activity with Q369A ZAP mutant
-
-
?
additional information
?
-
-
usage of a fluorescence resonance energy transfer (FRET)-based enzyme assay for activity determination
-
-
?
additional information
?
-
-
no hydrolysis of acetyl-Arg-Ser-Tyr-Phe-Thr-Gln-Ile-Gln-Gly-Glu-Ile-Gln-Trp-Met-Arg-Pro-NH2
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
does not hydrolyze 4-aminobenzyl-EALFAGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFEGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFRGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFHGPLQED-2,4-dinitrophenol, 4-aminobenzyl-EALFNGPLQED-2,4-dinitrophenol, and 4-aminobenzyl-EALFYGPLQED-2,4-dinitrophenol
-
-
?
additional information
?
-
-
no activity with cellular protein MAVS
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
the enzyme induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
-
-
?
additional information
?
-
-
the foot-and-mouth disease virus 3Cpro to cleaves sequences containing either P1-Gln or P1-Glu
-
-
?
additional information
?
-
-
the VP2 K217R and VP3 I2P substitutions (near the VP0/VP3 junction of the substrate) strongly reduce the processing at this junction by 3Cpro while the substitution VP2 K217E blocks cleavage. At the VP3/VP1 junction, the substitutions VP3 Q2221P and VP1 T1P each severely inhibit processing at this site. Blocking cleavage at either junction does not prevent processing elsewhere in P1-2A. Processing of the P1-2A precursor in the transient expression assay using BHK cells
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
the pattern of proteolytic products of polyprotein processing in recombinant systems and in infected cells differs, mature protease 3C is produced in bacteria, but cleavage is arrested at 3ABC intermediate in eukaryotic system
-
-
?
additional information
?
-
-
catalytic sites: Cys172 (nucleophile) and His44 (general base), His191 defines Gln-residue specificity
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
no hydrolysis of cellular proteins during viral infection
-
-
?
additional information
?
-
-
no maturation cleavage in picornavirus replication
-
-
?
additional information
?
-
-
3C protein and 3C-containing precursor proteins play roles in the virus lifecycle before, during and after RNA synthesis, enzyme has uridylylation activity on Vpg peptide
-
-
?
additional information
?
-
the accessibility of the HRV 3C cleavage site within RIPK1 in-vitro is probably increased by concurrent cleavage of RIPK1 through caspase-8. Prior to cleavage of RIPK1 by caspase 8 does not abrogate 3C protease-mediated cleavage in vitro
-
-
?
additional information
?
-
-
HRV 3C protease shows high and unique specificity. It recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro and cleaves between glutamine and glycine
-
-
?
additional information
?
-
-
NF-kappaB-p65 activation by SVA 3Cpro. NF-kappaB-p65 cleavage occurs at the caspase cleavage site (444LQFDTDED), suggesting that cleavage of NF-kappaB-p65 is mediated by caspases and not by the direct action of SVA 3Cpro. While expression of wild-type SVA 3Cpro results in activation of Casp-3 and cleavage of NF-kappaB-p65, expression of the 3Cpro catalytic-dead mutants H47D or C159R does not lead to Casp-3 activation nor to NF-kappaB-p65 cleavage
-
-
?
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(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
(2Z)-3-[4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinolin-6-yl]prop-2-enoic acid
-
70% effect at 0.1 mM
(3S)-[N3-(acetyl-L-leucyl-L-alanyl)-N1-[3'-(N,N-dimethylamino)-3'-oxopropyl]-N1-(methylsulfonyl)]-1,3-diaminobutan-2-one
-
weak competitive
(3S)-[N3-(acetyl-L-leucyl-L-alanyl)-N1-[3'-(N,N-dimethylamino)-3'-oxopropyl]-N1-(p-methylphenylsulfonyl)]-1,3-diaminobutan-2-one
-
weak competitive
(3S)-[N3-(benzyloxycarbonyl)-N1-[3'-(N,N-dimethylamino)-3'-oxoprolyl]-N1-(methylsulfonyl)]-1,3-diaminobutan-2-one
-
weak competitive
(3S)-[N3-(benzyloxycarbonyl)-N1-[3'-(N,N-dimethylamino)-3'-oxopropyl]-N1-(p-methylphenylsulfonyl)]-1,3-diaminobutan-2-one
-
weak competitive, IC50: 0.075 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[(4-phenylpiperazin-1-yl)carbonyl]-1,3-dioxolane-4-carboxamide
-
82.47% inhibition at 0.1 mM; complete inhibition at 0.1 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(3-methylbenzyl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
-
78.74% inhibition at 0.1 mM; 84.20% inhibition at 0.1 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(pyridin-2-yl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
-
85.35% inhibition at 0.1 mM; 97.80% inhibition at 0.1 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[(4-benzylpiperazin-1-yl)carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
-
67.80% inhibition at 0.1 mM; 85.51% inhibition at 0.1 mM, molecular docking study using the HRV 3C protease structure, PDB ID 1CQQ
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[[4-(2-cyanophenyl)piperazin-1-yl]carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
-
56.36% inhibition at 0.1 mM; complete inhibition at 0.1 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-N'-[2-[(3-methoxyphenyl)amino]ethyl]-2,2-dimethyl-1,3-dioxolane-4,5-dicarboxamide
-
99.91% inhibition at 0.1 mM
(4R,5R)-N-(1,3-benzothiazol-2-yl)-N'-[2-[(4-methoxyphenyl)amino]ethyl]-2,2-dimethyl-1,3-dioxolane-4,5-dicarboxamide
-
85.22% inhibition at 0.1 mM
(4R,5R)-N4-(2-((3-methoxyphenyl)amino)ethyl)-2,2-dimethyl-N5-(naphthalen-2-yl)-1,3-dioxolane-4,5-dicarboxamide
-
80.56% inhibition at 0.1 mM
(4S)-4-(acetylamino)-N,N-dimethyl-5-oxopentanamide
-
hepatitis A virus
(5-bromopyridin-3-yl)methyl furan-2-carboxylate
-
67% inhibition at 10 microM inhibitor concentration
(E)-2-({2-acetyl-1-[3-(dimethylamino)-3-oxopropyl]hydrazinyl}carbonyl)-N-(2-phenylethyl)diazenecarboxamide
-
potent, irreversible inhibitors with IC50 values in the low micromolar range, probably act by adding the active site thiol to the azo moiety in a Michael fashion to give a covalent complex
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate
-
83% inhibition at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, 43% inhibition at 0.25 microM inhibitor concentration
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-methylthiosemicarbazide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-(benzyloxy)-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-3-(1H-imidazol-3-ium-2-yl)-L-alaninamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-5-ammonio-L-norvalinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-N5-[amino(iminio)methyl]-L-ornithinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-N6-[amino(iminio)methyl]-L-lysinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]glycinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-[methoxy(methyl)amino]-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
1-acetyl-L-prolyl-L-alanyl-N1-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-L-glutamamide
-
-
1-acetyl-L-prolyl-L-alanyl-N6-acetyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-L-lysinamide
-
-
1-acetyl-L-prolyl-N-[(2S)-1-[[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]amino]-4-ammonio-1-oxobutan-2-yl]-L-alaninamide
-
-
1-acetyl-L-prolyl-N-[(2S)-1-[[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]amino]-4-[[amino(iminio)methyl]amino]-1-oxobutan-2-yl]-L-alaninamide
-
-
1-benzoylprolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
1-benzylprolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
1-[(4-methylphenyl)sulfonyl]prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
13C-labeled beta-lactone
-
-
-
2,2'-dipyridyl disulfide
-
0.4 mM, complete inhibition
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-bromophenyl)ethylidene)acetohydrazide
-
enzyme binding and protein interactions analysis
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-phenylethylidene)acetohydrazide
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(2-oxoindolin-3-ylidene)acetohydrazide
-
-
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(5-bromo-2-oxoindolin-3-ylidene)acetohydrazide
-
-
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(5-chloro-2-oxoindolin-3-ylidene)acetohydrazide
-
-
2-(pyridin-3-yl)quinolin-4(1H)-one
-
35% effect at 0.1 mM
2-aminopyridin-3-yl furan-2-carboxylate
-
24% inhibition at 0.001 mM
2-carbamoylpyridin-3-yl furan-2-carboxylate
-
14% inhibition at 0.001 mM
2-chloropyridin-3-yl thiophene-2-carboxylate
-
11% inhibition at 10 microM inhibitor concentration
2-methylpyridin-3-yl thiophene-2-carboxylate
-
below 10% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 1 microM inhibitor concentration
2-oxo-1,2-dihydroquinolin-4-yl furan-2-carboxylate
-
98% inhibition at 0.001 mM
2-pyridin-3-yl-1-thiophen-2-ylethanone
-
10% inhibition at 10 microM inhibitor concentration
2-[(2-oxo-4-phenyl-2H-chromen-7-yl)oxy]acetohydrazide
-
-
3-(benzylamino)-5-[1-N-hydroxyethanimidoyl]benzamide
-
-
3-(bromoacetyl)-5-(naphth-2-ylmethyl)benzamide
-
12% inhibition at inhibitor concentration of 100 nM, 39% inhibition at inhibitor concentration of 1 microM, 83% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-(bromoacetyl)benzamide
-
4% inhibition at inhibitor concentration of 100 nM, 23% inhibition at inhibitor concentration of 1 microM, 85% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-(chloroacetyl)-5-(naphth-2-ylmethyl)benzamide
-
25% inhibition at inhibitor concentration of 100 nM, 61% inhibition at inhibitor concentration of 1 microM, 81% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-(chloroacetyl)benzamide
-
-
3-(dibromoacetyl)-5-(naphth-2-ylmethyl)benzamide
-
-
3-(dibromoacetyl)benzamide
-
-
3-(dichloroacetyl)benzamide
-
-
3-(difluoroacetyl)-5-[(phenylcarbonyl)amino]benzamide
-
-
3-(difluoroacetyl)benzamide
-
-
3-(trifluoroacetyl)benzamide
-
no inhibition of 3CP
3-(trifluoroacetyl)benzonitrile
-
-
3-acetyl-5-(5,8-dihydronaphthalen-2-ylmethyl)benzamide
-
-
3-acetyl-5-(naphth-1-ylcarbamoyl)benzoic acid
-
-
3-acetyl-5-(phenylcarbamoyl)benzoic acid
-
-
3-acetyl-5-benzylbenzamide
-
-
3-amino-6-([[(2S)-1-([(2S,3E)-5-ethoxy-5-oxo-1-[(3S)-2-oxopyrrolidin-3-yl]pent-3-en-2-yl]amino)-1-oxo-3-phenylpropan-2-yl]amino]oxy)-6-methyl-4-oxoheptanoic acid
-
-
3-benzyl-5-(bromoacetyl)benzamide
-
0% inhibition at inhibitor concentration of 100 nM, 30% inhibition at inhibitor concentration of 1 microM, 68% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-benzyl-5-(chloroacetyl)benzamide
-
14% inhibition at inhibitor concentration of 100 nM, 79% inhibition at inhibitor concentration of 1 microM, 91% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-benzyl-5-(dibromoacetyl)benzamide
-
14% inhibition at inhibitor concentration of 100 nM, 27% inhibition at inhibitor concentration of 1 microM, 75% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
3-benzyl-5-(difluoroacetyl)benzamide
-
-
3-carbamoylphenyl furan-2-carboxylate
-
5% inhibition at 0.001 mM
3-chloro-5-(furan-2-ylmethoxy)pyridine
-
below 10% inhibition at 10 microM inhibitor concentration
3-chlorophenyl furan-2-carboxylate
-
11% inhibition at 10 microM inhibitor concentration
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
3-[N1-(acetyl-L-leucyl-L-alanyl-L-alanyl)-N2-(o-nitrophenyl-sulfenyl)hydrazino]-N,N-(dimethyl)propanamide
-
IC50: 0.1 mM, time-dependent inactivation of the enzyme due to disulfide bond formation with the active site cysteine thiol
3-[N1-(bromoacetyl)-N2-(acetyl-L-leucyl-L-alanyl-L-alanyl)hydrazino]-N,N-(dimethyl)propanamide
-
time-dependent irreversible inactivator
3-[N1-(chloroacetyl)-N2-(acetyl-L-leucyl-L-alanyl-L-alanyl)hydrazino]1-N,N-(dimethyl)propanamide
-
time-dependent irreversible inactivator
4-(bromoacetyl)isoindolin-1-one
-
-
4-acetylisoindolin-1-one
-
-
4-amino-7-([[(2S)-1-([(2S,3E)-5-ethoxy-5-oxo-1-[(3S)-2-oxopyrrolidin-3-yl]pent-3-en-2-yl]amino)-1-oxo-3-phenylpropan-2-yl]amino]oxy)-7-methyl-5-oxooctanoic acid
-
-
4-bromoisoindolin-1-one
-
-
4-chloromercuribenzenesulfonate
-
strong inhibition at 0.05 mM
4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinoline-6-carbaldehyde
-
95% effect at 0.1 mM
4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinoline-6-carbonitrile
-
50% effect at 0.1 mM
4-phenyl-7-[(5-thioxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)methoxy]-2H-chromen-2-one
-
-
4S-(3-benzo[1,3]dioxol-5-yl-acryloylamino)-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(2H-chromene-3-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(2methyl-5-phenylfuran-3-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(6-bromo-2H-chromene-3-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(6-chloro-2H-chromene-3-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(6-methyl-naphthalene-2-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[(7-bromonaphthalene-2-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)-pent-2-enoic acid ethyl ester
-
-
4S-[(naphthalene-2-carbonyl)amino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid
-
-
4S-[3-(2,5-dibromophenyl)acryloylamino]-5-(2-oxopyrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[3-(3-bromo-4-fluorophenyl)acryloylamino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[3-(3-bromo-4-methyl-phenyl)-acryloylamino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[3-(3-bromophenyl)acryloylamino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid ethyl ester
-
-
4S-[3-(6'-bromo-benzo[1,3]dioxol-5-yl)acryloylamino]-5-(2-oxopyrrolidin-3S-yl)pent-2-enoic acid
-
-
5-(bromoacetyl)-N-2-naphthylisophthalamide
-
5% inhibition at inhibitor concentration of 100 nM, 19% inhibition at inhibitor concentration of 1 microM, 80% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
5-(bromoacetyl)-N-phenylisophthalamide
-
8% inhibition at inhibitor concentration of 100 nM, 27% inhibition at inhibitor concentration of 1 microM, 86% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
5-(dibromoacetyl)-N-2-naphthylisophthalamide
-
-
5-(dibromoacetyl)-N-phenylisophthalamide
-
-
5-acetyl-N-(naphthalen-1-yl)benzene-1,3-dicarboxamide
-
-
5-acetyl-N-phenylbenzene-1,3-dicarboxamide
-
-
5-bromopyridin-3-yl (2E)-3-phenylprop-2-enoate
-
63% inhibition at 0.001 mM
5-bromopyridin-3-yl 3-phenylpropanoate
-
34% inhibition at 0.001 mM
5-bromopyridin-3-yl furan-2-carboxylate
-
most potent inhibitor, 90% inhibition at 0.001 mM
5-bromopyridin-3-yl furan-3-carboxylate
-
inhibition not detected at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, 87% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1,3-thiazole-4-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 85% inhibition at 1 microM inhibitor concentration, 37% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1-benzofuran-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1-benzothiophene-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 47% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 1-naphthoate
-
above 90% inhibition at 10 microM inhibitor concentration, 30% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 1H-benzo[d]imidazole-5-carboxylate
-
82% inhibition at 10 microM inhibitor concentration, 75% inhibition at 1 microM inhibitor concentration, 32% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1H-benzo[d][1,2,3]triazole-5-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 1H-imidazole-4-carboxylate
-
33% inhibition at 10 microM inhibitor concentration, 47% inhibition at 1 microM inhibitor concentration, 34% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1H-indole-2-carboxylate
-
80% inhibition at 10 microM inhibitor concentration, 58% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 1H-indole-3-carboxylate
-
13% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 1H-indole-5-carboxylate
-
87% inhibition at 10 microM inhibitor concentration, 60% inhibition at 1 microM inhibitor concentration, 22% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 1H-pyrazole-3-carboxylate
-
82% inhibition at 0.001 mM
5-chloropyridin-3-yl 1H-pyrazole-4-carboxylate
-
56% inhibition at 10 microM inhibitor concentration, 21% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 2,6-dichloro-5-fluoronicotinate
-
44% inhibition at 10 microM inhibitor concentration, 19% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 2-(diphenylmethyl)-4-ethoxy-1,3-oxazole-5-carboxylate
-
5% inhibition at 0.001 mM
5-chloropyridin-3-yl 2-benzyl-4-ethoxy-1,3-oxazole-5-carboxylate
-
5% inhibition at 0.001 mM
5-chloropyridin-3-yl 2-chlorobenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 67% inhibition at 1 microM inhibitor concentration, 23% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 2-methoxybenzoate
-
85% inhibition at 10 microM inhibitor concentration, 57% inhibition at 1 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 2-methylbenzoate
-
82% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 2-naphthoate
-
23% inhibition at 10 microM inhibitor concentration, 35% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 2-nitrobenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 24% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 2-oxo-2H-chromene-3-carboxylate
-
75% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 3,4-dimethoxybenzoate
-
59% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 3-acetoxybenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 27% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 3-chlorobenzoate
-
29% inhibition at 10 microM inhibitor concentration, 50% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 3-methylbenzoate
-
63% inhibition at 10 microM inhibitor concentration, 32% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 3-methylthiophene-2-carboxylate
-
below 10% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 3-[4-(trifluoromethyl)phenyl]-3H-pyrrole-5-carboxylate
-
40% inhibition at 0.001 mM
5-chloropyridin-3-yl 4-(diethylamino)benzoate
-
64% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 4-(dimethylamino)benzoate
-
above 90% inhibition at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, 20% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 4-(methylamino)benzoate
-
82% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 4-aminobenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 26% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 4-chloro-2-hydroxybenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 59% inhibition at 1 microM inhibitor concentration, 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 4-ethoxy-2-(naphthalen-2-yl)-1,3-oxazole-5-carboxylate
-
34% inhibition at 0.001 mM
5-chloropyridin-3-yl 4-ethoxy-2-[(E)-2-phenylethenyl]-1,3-oxazole-5-carboxylate
-
87% inhibition at 0.001 mM
5-chloropyridin-3-yl 4-fluorobenzoate
-
above 90% inhibition at 10 microM inhibitor concentration, 45% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 4-hydroxy-7-(trifluoromethyl)quinoline-3-carboxylate
-
below 10% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 4-methoxybenzoate
-
85% inhibition at 10 microM inhibitor concentration; above 90% inhibition at 10 microM inhibitor concentration, 50% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 4-methylbenzoate
-
77% inhibition at 10 microM inhibitor concentration, 70% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 4-sulfamoylbenzoate
-
64% inhibition at 10 microM inhibitor concentration, 57% inhibition at 1 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-(2-(trifluoromethyl)phenyl)furan-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-(2-chloro-5-(trifluoromethyl)phenyl)furan-2-carboxylate
-
76% inhibition at 10 microM inhibitor concentration, 36% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl 5-(2-nitrophenyl)furan-2-carboxylate
-
37% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 5-(3-nitrophenyl)furan-2-carboxylate
-
Inhibition not detected at 10 microM, 1 microM and 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-(4-chloro-2-nitrophenyl)furan-2-carboxylate
-
40% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl 5-(4-chlorophenyl)furan-2-carboxylate
5-chloropyridin-3-yl 5-(4-methylphenyl)furan-2-carboxylate
-
79% inhibition at 0.001 mM
5-chloropyridin-3-yl 5-(4-nitrophenyl)furan-2-carboxylate
-
60% inhibition at 0.001 mM
5-chloropyridin-3-yl 5-bromofuran-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 54% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-methyl-3-phenylisoxazole-4-carboxylate
-
below 10% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-methylthiophene-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 24% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-nitro-1H-pyrazole-3-carboxylate
-
54% inhibition at 10 microM inhibitor concentration, 69% inhibition at 1 microM inhibitor concentration, 53% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-phenylfuran-2-carboxylate
-
80% inhibition at 0.001 mM
5-chloropyridin-3-yl benzoate
5-chloropyridin-3-yl benzo[d]thiazole-6-carboxylate
-
74% inhibition at 10 microM inhibitor concentration, 54% inhibition at 1 microM inhibitor concentration, 27% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl benzo[d][1,3]dioxole-5-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 11% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl biphenyl-4-carboxylate
-
39% inhibition at 10 microM inhibitor concentration, 23% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl cinnamate
-
above 90% inhibition at 10 microM inhibitor concentration, 53% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl cyclohexanecarboxylate
-
81% inhibition at 10 microM inhibitor concentration, 32% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl furan-2-carboxylate
5-chloropyridin-3-yl furan-3-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl isonicotinate
-
37% inhibition at 10 microM inhibitor concentration, 34% inhibition at 1 microM inhibitor concentration
5-chloropyridin-3-yl naphthalene-1-carboxylate
-
75% inhibition at 0.001 mM
5-chloropyridin-3-yl naphthalene-2-carboxylate
-
80% inhibition at 0.001 mM
5-chloropyridin-3-yl pyrazine-2-carboxylate
-
22% inhibition at 10 microM inhibitor concentration
5-chloropyridin-3-yl thiophene-2-carboxylate
5-methylpyridin-2-yl thiophene-2-carboxylate
-
12% inhibition at 10 microM inhibitor concentration
6-(bromoacetyl)isoindolyn-1-one
-
0% inhibition at inhibitor concentration of 100 nM, 25% inhibition at inhibitor concentration of 1 microM, 70% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
6-acetyl-2-(pyridin-3-yl)quinolin-4(1H)-one
-
25% effect at 0.1 mM
6-acetylisoindolin1-one
-
-
6-bromoisoindolin-1-one
-
-
6-chloropyridin-2-yl thiophene-2-carboxylate
-
16% inhibition at 10 microM inhibitor concentration
6-chloropyridin-3-yl 1H-pyrrole-2-carboxylate
-
92% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 1 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
6-chloropyridin-3-yl thiophene-2-carboxylate
-
25% inhibition at 10 microM inhibitor concentration
6-methyl-2-nitropyridin-3-yl thiophene-2-carboxylate
-
14% inhibition at 10 microM inhibitor concentration
6-methylpyridin-2-yl thiophene-2-carboxylate
-
91% inhibition at 10 microM inhibitor concentration, below 10% inhibition at 1 microM inhibitor concentration
6-methylpyridin-3-yl thiophene-2-carboxylate
-
23% inhibition at 10 microM inhibitor concentration
7-((4-ethyl-5-thioxo-1,2,4-triazol-3-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((4-methyl-5-thioxo-1,2,4-triazol-3-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(2-(diethylamino)ethylthio)-1,3,4-oxadiazol-2-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(2-(dimethylamino)ethylthio)-1,3,4-oxadiazol-2-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(2-morpholinoethylthio)-1,3,4-oxadiazol-2-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(2-morpholinoethylthio)-4-ethyl-4H-1,2,4-triazol-3-yl) methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(ethylamino)-1,3,4-thiadiazol-2-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-((5-(methylamino)-1,3,4-thiadiazol-2-yl)methoxy)-4-phenyl-2H-chromen-2-one
-
-
7-(2-(3,5-dimethyl-1H-pyrazol-1-yl)-2-oxoethoxy)-4-phenyl-2H-chromen-2-one
-
-
7-(2-phenylethyl)-2-(pyridin-3-yl)quinolin-4(1H)-one
-
100% effect at 0.1 mM
7-hydroxy-4-phenyl-2H-chromen-2-one
-
-
7-methoxy-2-(pyridin-3-yl)quinolin-4(1H)-one
-
below 10% effect at 0.1 mM
7-methyl-2-(pyridin-3-yl)quinolin-4(1H)-one
-
40% effect at 0.1 mM
7-[(4-amino-5-sulfanyl-4H-1,2,4-triazol-3-yl)methoxy]-4-phenyl-2H-chromen-2-one
-
-
7-[hydroxy(phenyl)methyl]-2-(pyridin-3-yl)quinolin-4(1H)-one
-
80% effect at 0.1 mM
acetyl-Ala-Ala-Ala-(N,N'-dimethylglutaminal)
-
-
acetyl-LEALFQ-ethylpropionate
-
-
acetyl-Leu-Ala-Ala N,N-dimethylglutamine fluoroketone
-
irreversible inactivator
acetyl-Leu-Ala-Ala-(N,N'-dimethylglutaminal)
-
-
AL21-01
-
Agouron aldehydic compound, 8% inhibition at inhibitor concentration of 100 nM, 75% inhibition at inhibitor concentration of 1 microM, 92% inhibition at inhibitor concentration of 0.01 mM, 700 nM enzyme
-
ammonium trichloro (dioxoethylene-O,O')tellurate
-
-
Aprotinin
-
0.1 mM, 64% inhibition
benzyloxycarbonyl-Leu-Phe-(glutaminol)
-
-
benzyloxycarbonyl-Leu-Phe-L-(cyanomethyl-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N,N-dimethyl-glutaminyl)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-acetylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-benzoylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-butyloxycarbonylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-carbomethoxyamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-formylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-isobutyrylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-(N-propinylamino-alaninal)
-
-
benzyloxycarbonyl-Leu-Phe-L-glutaminal-hemiaminal
-
-
benzyloxycarbonyl-Leu-Phe-L-[(N-trifluoroacetyl)amino-alaninal]
-
-
benzyloxycarbonyl-Leu-Phe-L-[methional sulfoxide]
-
-
benzyloxycarbonyl-Leu-Phe-L-[N-(2-pyrrolidinone)-alaninal]
-
-
benzyloxycarbonyl-Leu-Phe-L-[N-(isoxazole-5-carbonyl)aminoalaninal]
-
-
benzyloxycarbonyl-Leu-Phe-L-[N-(N,N-dimethylcarbamoyl)amino-alaninal]
-
-
benzyloxycarbonyl-Leu-Phe-[(N-methylsulfonyl)amino-alaninal]
-
-
benzyloxycarbonyl-Leu-Phe-[N-(Me)Ac-amino-alaninal]
-
-
bis-vinylic organotellurane
-
-
calpastatin
-
0.8 mM, 30% inhibition
-
Cu2+
-
5 mM decreases protease activity remarkably relative to the level of activity before the extra cations were added
dimethyl 5-acetylbenzene-1,3-dicarboxylate
-
-
ethyl (2E)-3-[(2S,5S,14S)-2-(4-fluorobenzyl)-9-methyl-14-[[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino]-3,8,15-trioxo-1,4,9-triazacyclopentadecan-5-yl]prop-2-enoate
-
-
ethyl (2E,4S)-4-([(2S)-2-[3-[[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino]-2-oxopyridin-1(2H)-yl]pent-4-ynoyl]amino)-5-[(3R)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
compound AG7404
ethyl (2E,4S)-4-([(2S)-2-[3-[[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino]-2-oxopyridin-1(2H)-yl]pent-4-ynoyl]amino)-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2E,4S)-4-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2E,4S)-4-[(N-[5-[(tert-butoxycarbonyl)amino]-6-hydroxy-2-methyl-4-oxoheptan-2-yl]-L-phenylalanyl)amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2E,4S)-4-[(N6-acetyllysyl)amino]-7-amino-7-oxohept-2-enoate
-
-
ethyl (2E,4S)-4-[(tert-butoxycarbonyl)amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2E,4S)-4-[[N-(5-amino-6-hydroxy-2-methyl-4-oxohexan-2-yl)-L-phenylalanyl]amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
most potent inhibitor
ethyl (2E,4S)-4-[[N-(5-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-6-hydroxy-2-methyl-4-oxoheptan-2-yl)-L-phenylalanyl]amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2E,4S)-4-[[N-(tert-butoxycarbonyl)-L-phenylalanyl]amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
-
-
ethyl (2Z)-3-[4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinolin-6-yl]prop-2-enoate
-
90% effect at 0.1 mM
ethyl 3-amino-5-[1-(hydroxyamino)ethyl]benzoate
-
-
ethyl 3-[4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinolin-6-yl]propanoate
-
0% effect at 0.1 mM
ethyl 4-[2-(4-cinnamoyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
ethyl 4-[2-(tert-butoxycarbonyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
ethyl 4-[2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
ethyl 4-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl-amino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
ethyl [(2-oxo-4-phenyl-2H-chromen-7-yl)oxy]acetate
-
-
eukaryotic release factor 3
-
increasing concentrations of recombinant His-tagged eRF3 lead to partial inhibition of 3Cpro-proteolytic cleavage of poly(A) binding protein that increases modestly
-
furan-2-yl pyridine-3-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration
iodoacetic acid
-
0.4 mM, complete inhibition
LY338387
-
0.00022 mM, 19% inhibition
LY355455
-
0.00031 mM, 72% inhibition
LY362270
-
0.01 mM, 43% inhibition
methyl 3-benzamido-5-{2,2-difluoro-1-[(2-methoxyethoxy)methoxy]ethenyl}benzoate
-
-
methyl 3-benzyl-5-bromobenzoate
-
-
methyl 3-bromo-5-(5,8-dihydronaphthalen-2-ylmethyl)benzoate
-
-
methyl 3-bromo-5-{2,2-difluoro-1-[(2-methoxyethoxy)methoxy]ethenyl}benzoate
-
-
methyl methanethiosulfonate
-
almost complete inhibition at 0.05 mM
methyl-3-(benzylamino)-5-carbamoylbenzoate
-
-
methyl-3-amino-5-carbamoylbenzoate
-
-
methyl-3-carbamoyl-5-(dibenzylamino)benzoate
-
-
methyl-3-{2,2-difluoro-1-[(2-methoxyethoxy)methoxy]ethenyl}-5-{[(trifluoromethyl)sulfonyl]oxy}benzoate
-
-
N-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-[(2-oxo-4-phenyl-2H-chromen-7-yl)oxy]acetamide
-
-
N-(2-chloropyridin-3-yl)thiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-(5-chloropyridin-2-yl)thiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-(5-fluoropyridin-2-yl)thiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-(6-chloropyridin-3-yl)thiophene-2-carboxamide
-
19% inhibition at 10 microM inhibitor concentration
N-(benzyloxycarbonyl)-D-serine-beta-lactone
-
competitive reversible inhibitor
N-(benzyloxycarbonyl)-L-serine-beta-lactone
-
irreversible, inactivation of the enzyme occurs by nucleophilic attack of the cysteine thiol Cys172 at the beta-position of the oxetanione ring
N-(methylsulfonyl)-L-serine-beta-lactone
-
weak time-dependent inhibition
N-(phenethylsulfonyl)-D-serine-beta-lactone
-
irreversible
N-(phenethylsulfonyl)-L-serine-beta-lactone
-
reversible
N-(trans-beta-styrenesulfonyl)-D-serine-beta-lactone
-
reversible
N-(trans-beta-styrenesulfonyl)-L-serine-beta-lactone
-
reversible
N-acetyl-L-alpha-glutamyl-L-phenylalanyl-L-glutaminyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-L-leucinamide
i.e. Michael acceptor peptidyl inhibitor (MAPI). Irreversible inhibitor in which the natural polyprotein substrate recognition sequence is linked to a propenyl ethyl ester moiety (X). The catalytic cysteine at position 139 of the enzyme is rapidly modified by the inhibitor
N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-(1,4-dioxo-3,4-dihydro-1H-phthalazin-2-yl)methyl ketone
-
-
N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-fluoromethyl ketone
-
-
N-acetyl-L-leucyl-phenylalanyl-phenylalanyl-glutamate-fluoromethyl ketone
-
-
N-benzoyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
-
-
N-Cbz-L-serine beta-lactone
-
irreversible inhibitor, associated with His 102 of the enzyme
N-ethylmaleimide
-
almost complete inhibition at 0.05 mM
N-iodoacetyl-Val-Phe-amide
-
irreversible inhibitor, alkylates the active site cysteine 172
N-methyl-3-[4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinolin-7-yl]propanamide
-
45% effect at 0.1 mM
N-methyl-4-oxo-2-(pyridin-3-yl)-1,4-dihydroquinoline-7-carboxamide
-
40% effect at 0.1 mM
N-pyridin-2-ylthiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-pyridin-3-ylthiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-pyridin-3-ylthiophene-2-sulfonamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-pyridin-4-ylthiophene-2-carboxamide
-
below 10% inhibition at 10 microM inhibitor concentration
N-[(2S)-1-oxo-3-[(3S)-2-oxopiperidin-3-yl]propan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(pentylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(phenylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
docking modeling
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propylamino)butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]-4-(phenylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(benzylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(benzylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(butylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(butylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(dodecylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(hexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(methylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-(tert-butylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-[(2-methylpropyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-[(4-methylphenyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-[(4-nitrophenyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S)-4-[(furan-2-ylmethyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N-[(2S,5S,14S)-2-(4-fluorobenzyl)-5-formyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(2S,5S,14S)-2-(4-fluorobenzyl)-5-formyl-9-methyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
crystal structure of 4 in complex with HRV2 3C protease (PDB ID 6FFS)
N-[(2S,5S,14S)-5-[azetidin-1-yl(oxo)acetyl]-2-(4-fluorobenzyl)-9-methyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(3S,12S,16S,17aS)-3-formyl-7-methyl-1,6,13-trioxo-16-phenylhexadecahydro-1H-pyrrolo[1,2-a][1,4,9]triazacyclopentadecin-12-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(4S,7S,10S,17aR)-7-(4-fluorobenzyl)-10-formyl-1,5,8,13-tetraoxohexadecahydro-1H-pyrrolo[1,2-a][1,4,8,11]tetraazacyclopentadecin-4-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-leucyl-N-[(2S)-1-(acetylamino)-3-oxopropan-2-yl]-4-fluoro-L-phenylalaninamide
-
-
N-[(5S,8S,11S)-8-(4-fluorobenzyl)-11-formyl-2,6,9,14-tetraoxooctadecahydropyrrolo[2,1-k][1,4,8,12]tetraazacyclohexadecin-5-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(5S,8S,11S,13E,17S)-8-(4-fluorobenzyl)-5-formyl-2,7,10-trioxo-16-oxa-1,6,9-triazabicyclo[15.2.1]icos-13-en-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(5S,8S,11S,13Z,19S)-8-(4-fluorobenzyl)-5-formyl-2,7,10-trioxo-18-oxa-1,6,9-triazabicyclo[17.2.1]docos-13-en-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(5S,8S,11S,17S)-8-(4-fluorobenzyl)-5-formyl-2,7,10,16-tetraoxo-1,6,9,15-tetraazabicyclo[15.2.1]icos-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(6S,9S,12S)-9-(4-fluorobenzyl)-12-formyl-1-methyl-3,7,10,15-tetraoxo-1,4,8,11-tetraazacyclopentadecan-6-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(7S,10S,13S)-10-(4-fluorobenzyl)-7-formyl-3-methyl-4,9,12-trioxo-3,8,11-triazabicyclo[12.3.1]octadeca-1(18),14,16-trien-13-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(7S,10S,13S)-10-(4-fluorobenzyl)-7-formyl-4,9,12-trioxo-3,8,11-triazabicyclo[12.3.1]octadeca-1(18),14,16-trien-13-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
-
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-isoleucinamide
-
-
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
-
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-norleucinamide
-
-
N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
-
N2-(morpholin-4-ylcarbonyl)-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
N6-(1-acetylprolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
-
-
N6-(N-acetylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
-
-
N6-(N-acetylalanylprolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
-
-
N6-(prolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
-
-
Na+
-
the enzyme is strongly inhibited by 200 mM Na+
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-(1,3-benzodioxol-5-yl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-(4-chloro-2-fluorophenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
Nalpha-[(2E)-3-(4-methylphenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
Nalpha-[(2E)-4-(5-methyl-1,2-oxazol-3-yl)but-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-4-fluoro-L-phenylalaninamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
Nalpha-{(2E)-3-[4-(dimethylamino)phenyl]prop-2-enoyl}-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
-
-
PABP-interacting protein 2
-
increasing concentrations of 1-3 microg inhibit cleavage of poly(A) binding protein by 3Cpro in a dose-dependent manner
-
peptide-mimetic monofluoromethyl ketones
-
-
-
phenylmethylsulfonyl fluoride
-
-
PMSF
-
1.7 mM, 32% inhibition
poliovirus-encoded nonstructural polypeptide 2B
-
low but detectable activity
-
poliovirus-encoded nonstructural polypeptide 2BC
-
efficiently blocks 3Cpro activity
-
poliovirus-encoded nonstructural polypeptide 2C
-
efficiently blocks 3Cpro activity, inhibits 3Cpro-catalyzed cleavage of cellular transcription factors at Q-G sites in vitro
-
pyridin-2-yl thiophene-2-carboxylate
-
89% inhibition at 10 microM inhibitor concentration, 8% inhibition at 1 microM inhibitor concentration
pyridin-3-yl furan-2-carboxylate
-
8% inhibition at 0.001 mM
pyridin-3-yl thiophene-2-carboxylate
-
83% inhibition at 10 microM inhibitor concentration, 21% inhibition at 1 microM inhibitor concentration
pyridin-4-yl thiophene-2-carboxylate
-
below 10% inhibition at 10 microM inhibitor concentration, 10% inhibition at 1 microM inhibitor concentration
TLCK
-
0.2 mM, 51% inhibition
(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
-
-
(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
-
-
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
-
enzyme binding and protein interactions analysis
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
-
enzyme binding and protein interactions analysis
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
-
enzyme binding and protein interactions analysis
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
-
enzyme binding and protein interactions analysis
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-phenylethylidene)acetohydrazide
-
-
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-phenylethylidene)acetohydrazide
-
enzyme binding and protein interactions analysis
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
5-chloropyridin-3-yl 5-(4-chlorophenyl)furan-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, 36% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl 5-(4-chlorophenyl)furan-2-carboxylate
-
89% inhibition at 0.001 mM
5-chloropyridin-3-yl benzoate
-
above 90% inhibition at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, below 10% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl benzoate
-
59% inhibition at 0.001 mM
5-chloropyridin-3-yl furan-2-carboxylate
-
above 90% inhibition at 10 microM inhibitor concentration, above 90%% inhibition at 1 microM inhibitor concentration, 49% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl furan-2-carboxylate
-
87% inhibition at 0.001 mM
5-chloropyridin-3-yl thiophene-2-carboxylate
-
93% inhibition at 10 microM inhibitor concentration; above 90% inhibition at 10 microM inhibitor concentration, above 90% inhibition at 1 microM inhibitor concentration, 50% inhibition at 0.25 microM inhibitor concentration
5-chloropyridin-3-yl thiophene-2-carboxylate
-
64% inhibition at 0.001 mM
acyclovir
-
-
AG7088
-
inhibitor with potent antiviral activity against multiple human rhinovirus serotypes, highly specific for picornavirus 3C proteases having negligible inhibitory activity against a panel of mammalian cysteine proteases, including cathepsin B, elastase, chymotrypsin, trypsin and calpain
AG7088
-
irreversible inhibitor, inhibits virus replication as well as cytokine production in a human bronchial epithelial cell line, BEAS-2B
AG7088
-
potent irreversible inhibitor, in vitro activity against a variety of different HRV serotypes as well as related picornaviruses in different cell-based systems
AG7088
-
inhibits all 48 serotypes of rhinoviruses
AG7088
-
3Cpro specific inhibitor, late addition of AG7088 to HeLa cells inhibits production of HRV-A16. Inhibition of 3Cpro by AG7088 early in infection (prior to onset of virion production) has stronger effects than late addition, due to inhibition of poly-protein processing
chymostatin
-
-
chymostatin
-
0.1 mM, 54% inhibition
Hg2+
-
-
Hg2+
-
5 mM decreases protease activity remarkably relative to the level of activity before the extra cations were added
iodoacetamide
-
-
iodoacetamide
-
only wild-type enzyme, not C147S-mutant
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
-
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
-
-
NEM
-
-
rupintrivir
YP_007969882
i.e. AG7088
rupintrivir
-
irreversible inhibitor of human enterovirus strains (4 of 4)
rupintrivir
potent inhibitor
rupintrivir
-
potent in vitro activity against 23 clinical isolates tested in H1-HeLa cell protection assays
rupintrivir
the activity of HRV16 3C protease is clearly inhibited by Rupintrivir treatment as viral polyprotein (P1) processing is downregulated
Zn2+
-
5 mM decreases protease activity remarkably relative to the level of activity before the extra cations were added
Zn2+
-
2.0 mM ZnCl2, complete inhibition
additional information
-
no inhibition by Triton X-100, that inhibits picornain 3CD
-
additional information
-
no inhibition by acetyl-Leu-Ala-Ala-Gln'-thioester
-
additional information
-
inhibitor synthesis and assay for their biochemical and antiviral activities, structure-activity relationship (SAR) study, ligand docking, overview. The small moieties are primarily tolerated at P1' and the introduction of para-fluoro benzyl at P2 notably improves the inhibitor's potency
-
additional information
-
no inhibition by benzyloxycarbonyl-VAD-(O-methyl)-fluoromethylketone
-
additional information
-
no inhibition by Triton X-100
-
additional information
-
-
-
additional information
-
not inhibited by the viral RNA polymerase 3Dpol
-
additional information
-
no inhibition by acetyl-Leu-Ala-Ala-Gln'-thioester
-
additional information
-
a series of 4-phenylcoumarin derivatives is designed and synthesized starting from (2-oxo-4-phenyl-2H-chromen-7-yloxy) acetic acid hydrazide. Evaluation of the target compounds for their antiviral activity against hepatitis A virus reveals that 4-phenylcoumarin derivatives are potent 3C protease inhibitors, anti-HAV effect and molecular modeling, 3D-pharmacophore and quantitative structure activity relationship (QSAR) models, overview. The ethylthiosemicarbazide derivative is the most potent virucidal agent and the Schiff's bases cause the highest virustatic effects against viral adsorption and replication, respectively. Docking within the pocket site of HAV 3C protease (using the structure with PDB ID 2HAL) illustrates a strong H-profile with the key amino acids Gly170 and Cys172 similar to the co-crystallized ligand. Generation of pharmacophore and quantitative structure activity relationship (QSAR) models. Cytotoxicity and antiviral effect of the synthesized compounds on HAV 3C protease, detailed overview
-
additional information
-
efficiency of inhibitors in inhibition of virus replication, quantitative realtime PCR expression analysis, overview
-
additional information
-
inhibitors possess an electophilic moiety, often a Michael acceptor function, which covalently binds to a cysteine in the active site of the enzyme, key step for virus inactivation
-
additional information
-
efficiency of inhibitors in inhibition of virus replication, quantitative realtime PCR expression analysis, overview
-
additional information
-
design, synthesis, and evaluation of 2,2-dimethyl-1,3-dioxolane derivatives as human rhinovirus 3C protease inhibitors. Virtual screening. Structure-function analysis, docking studies
-
additional information
-
a series of 4-phenylcoumarin derivatives is designed and synthesized starting from (2-oxo-4-phenyl-2Hchromen-7-yloxy) acetic acid 2-[(2-oxo-4-phenyl-2H-chromen-7-yl)oxy]acetohydrazide. Evaluation of the target compounds for their antiviral activity against hepatitis A virus reveals that 4-phenylcoumarin derivatives are potent 3C protease inhibitors, anti-HRV effect and molecular modeling, 3D-pharmacophore and quantitative structure activity relationship (QSAR) models, overview. The ethylthiosemicarbazide derivative is the most potent virucidal agent and the Schiff's bases cause the highest virustatic effects against viral adsorption and replication, respectively. Generation of pharmacophore and quantitative structure activity relationship (QSAR) models
-
additional information
-
HRV 3C protease activity is completely abolished in the presence of eight detergents (C-HEGA1-10, C-HEGA1-9, HEGA1-8, CYMAL1-2, n-decyl-N,N-dimethylglycine, MEGA-8, FOS-choline1-8 and ANAPOE1-20)
-
additional information
-
no inhibition by benzyloxycarbonyl-VAD-(O-methyl)-fluoromethylketone or QVD
-
additional information
-
design and synthesis of macrocyclic inhibitors of human rhinovirus 3C protease, overview. Macrocyclization is a good way to improve the potency and ADME properties of peptidomimetics. Cyclization of peptidomimetic molecules can lead to increased potency by picking up additional interactions on the protein surface and reducing the entropic penalty inherent in binding a peptide-like structure to a protein
-
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0.0002 - 0.00177
(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
0.075
(3S)-[N3-(benzyloxycarbonyl)-N1-[3'-(N,N-dimethylamino)-3'-oxopropyl]-N1-(p-methylphenylsulfonyl)]-1,3-diaminobutan-2-one
Hepatovirus A
-
weak competitive, IC50: 0.075 mM
0.01 - 8.57
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[(4-phenylpiperazin-1-yl)carbonyl]-1,3-dioxolane-4-carboxamide
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(3-methylbenzyl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
0.01 - 10.62
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(pyridin-2-yl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[(4-benzylpiperazin-1-yl)carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
0.01 - 2.5
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[[4-(2-cyanophenyl)piperazin-1-yl]carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
8.28
(4R,5R)-N-(1,3-benzothiazol-2-yl)-N'-[2-[(3-methoxyphenyl)amino]ethyl]-2,2-dimethyl-1,3-dioxolane-4,5-dicarboxamide
Human rhinovirus sp.
-
pH and temperature not specified in the publication
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-N'-[2-[(4-methoxyphenyl)amino]ethyl]-2,2-dimethyl-1,3-dioxolane-4,5-dicarboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
0.01
(4R,5R)-N4-(2-((3-methoxyphenyl)amino)ethyl)-2,2-dimethyl-N5-(naphthalen-2-yl)-1,3-dioxolane-4,5-dicarboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
0.00014
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.018 - 0.051
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.0161 - 0.01778
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
0.0077
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-(benzyloxy)-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0098
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-3-(1H-imidazol-3-ium-2-yl)-L-alaninamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0027
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-5-ammonio-L-norvalinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00084
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-N5-[amino(iminio)methyl]-L-ornithinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0012
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-N6-[amino(iminio)methyl]-L-lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
2.8
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]glycinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.066
1-acetyl-L-prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-[methoxy(methyl)amino]-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.053
1-acetyl-L-prolyl-L-alanyl-N1-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-L-glutamamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.13
1-acetyl-L-prolyl-L-alanyl-N6-acetyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-L-lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.021
1-acetyl-L-prolyl-N-[(2S)-1-[[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]amino]-4-ammonio-1-oxobutan-2-yl]-L-alaninamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0038
1-acetyl-L-prolyl-N-[(2S)-1-[[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]amino]-4-[[amino(iminio)methyl]amino]-1-oxobutan-2-yl]-L-alaninamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00043
1-benzoylprolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0015
1-benzylprolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0016
1-[(4-methylphenyl)sulfonyl]prolyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00719
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-bromophenyl)ethylidene)acetohydrazide
Hepatovirus A
-
pH 7.5, 37°C
0.00594 - 0.0063
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
0.00413
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-phenylethylidene)acetohydrazide
Human rhinovirus sp.
-
pH 7.5, 37°C
0.0002
2-oxo-1,2-dihydroquinolin-4-yl furan-2-carboxylate
Human rhinovirus sp.
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30°C
0.024 - 0.125
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.01 - 0.017
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.0084 - 0.0096
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
0.013 - 0.025
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
0.005 - 0.02
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
0.0068 - 0.022
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.012 - 0.0166
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.042 - 0.098
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
0.1
3-[N1-(acetyl-L-leucyl-L-alanyl-L-alanyl)-N2-(o-nitrophenyl-sulfenyl)hydrazino]-N,N-(dimethyl)propanamide
Hepatovirus A
-
IC50: 0.1 mM, time-dependent inactivation of the enzyme due to disulfide bond formation with the active site cysteine thiol
0.00008
5-bromopyridin-3-yl furan-2-carboxylate
Human rhinovirus sp.
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30°C
0.000053
5-bromopyridin-3-yl furan-3-carboxylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.00029
5-chloropyridin-3-yl 1H-pyrazole-3-carboxylate
Human rhinovirus sp.
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30°C
0.00069
5-chloropyridin-3-yl 4-ethoxy-2-[(E)-2-phenylethenyl]-1,3-oxazole-5-carboxylate
Human rhinovirus sp.
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30°C
0.0012
5-chloropyridin-3-yl 5-bromofuran-2-carboxylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.00025
5-chloropyridin-3-yl 5-nitro-1H-pyrazole-3-carboxylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.000338
5-chloropyridin-3-yl furan-2-carboxylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.00071
5-chloropyridin-3-yl naphthalene-2-carboxylate
Human rhinovirus sp.
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30°C
0.00047
5-chloropyridin-3-yl thiophene-2-carboxylate
Hepatovirus A
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37°C
0.03
ammonium trichloro (dioxoethylene-O,O')tellurate
Human poliovirus 3
-
25°C, pH not specified in the publication, value above
0.0001
bis-vinylic organotellurane
Human poliovirus 3
-
25°C, pH not specified in the publication
0.00084
chloro-telluroxetane
Human poliovirus 3
-
25°C, pH not specified in the publication
0.00737
ethyl (2E)-3-[(2S,5S,14S)-2-(4-fluorobenzyl)-9-methyl-14-[[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino]-3,8,15-trioxo-1,4,9-triazacyclopentadecan-5-yl]prop-2-enoate
Rhinovirus B14
-
pH 7.4, temperature not specified
0.0032
ethyl (2E,4S)-4-([(2S)-2-[3-[[(5-methyl-1,2-oxazol-3-yl)carbonyl]amino]-2-oxopyridin-1(2H)-yl]pent-4-ynoyl]amino)-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate
Rhinovirus B14
-
pH 7.4, temperature not specified
0.6
ethyl (2E,4S)-4-[(N6-acetyllysyl)amino]-7-amino-7-oxohept-2-enoate
Foot-and-mouth disease virus
-
IC50 above 0.6 mM, at pH 7.4 and 37°C
0.01
ethyl 4-[2-(4-cinnamoyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
-
0.0082
ethyl 4-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl-amino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
-
0.0106
ethyl 4[2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
-
0.0023
N-benzoyl-L-alanyl-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]-6-ammonio-L-norleucinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00054
N-[(2S)-1-oxo-3-[(3S)-2-oxopiperidin-3-yl]propan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
51 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00381
N-[(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
50 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(pentylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
67 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(phenylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
60 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00132
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
73 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00134
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
57 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00188
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propylamino)butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
74 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00622
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
63 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]-4-(phenylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
55 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00875
N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
52 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00783
N-[(2S)-4-(benzylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
61 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-(benzylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
56 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00821
N-[(2S)-4-(butylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
58 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.0176
N-[(2S)-4-(butylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
53 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00371
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
76 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00486
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
59 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.0127
N-[(2S)-4-(cyclohexylamino)-3,4-dioxo-1-[(3S)-2-oxopyrrolidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
54 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00152
N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
75 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00332
N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
64 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-(dodecylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
69 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-(hexylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
68 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00408
N-[(2S)-4-(methylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
62 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-(tert-butylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
66 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00507
N-[(2S)-4-[(2-methylpropyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
65 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-[(4-methylphenyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
70 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.02
N-[(2S)-4-[(4-nitrophenyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
71 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.0063
N-[(2S)-4-[(furan-2-ylmethyl)amino]-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
Enterovirus A71
-
72 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.000007
N-[(2S,5S,14S)-2-(4-fluorobenzyl)-5-formyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000018
N-[(2S,5S,14S)-2-(4-fluorobenzyl)-5-formyl-9-methyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.00384
N-[(2S,5S,14S)-5-[azetidin-1-yl(oxo)acetyl]-2-(4-fluorobenzyl)-9-methyl-3,8,15-trioxo-1,4,9-triazacyclopentadecan-14-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000008
N-[(3S,12S,16S,17aS)-3-formyl-7-methyl-1,6,13-trioxo-16-phenylhexadecahydro-1H-pyrrolo[1,2-a][1,4,9]triazacyclopentadecin-12-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000035
N-[(4S,7S,10S,17aR)-7-(4-fluorobenzyl)-10-formyl-1,5,8,13-tetraoxohexadecahydro-1H-pyrrolo[1,2-a][1,4,8,11]tetraazacyclopentadecin-4-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
50 pH 7.4, temperature not specified
0.000063
N-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-leucyl-N-[(2S)-1-(acetylamino)-3-oxopropan-2-yl]-4-fluoro-L-phenylalaninamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000002
N-[(5S,8S,11S)-8-(4-fluorobenzyl)-11-formyl-2,6,9,14-tetraoxooctadecahydropyrrolo[2,1-k][1,4,8,12]tetraazacyclohexadecin-5-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000002
N-[(5S,8S,11S,13E,17S)-8-(4-fluorobenzyl)-5-formyl-2,7,10-trioxo-16-oxa-1,6,9-triazabicyclo[15.2.1]icos-13-en-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000003
N-[(5S,8S,11S,17S)-8-(4-fluorobenzyl)-5-formyl-2,7,10,16-tetraoxo-1,6,9,15-tetraazabicyclo[15.2.1]icos-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000006
N-[(6S,9S,12S)-9-(4-fluorobenzyl)-12-formyl-1-methyl-3,7,10,15-tetraoxo-1,4,8,11-tetraazacyclopentadecan-6-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000753
N-[(7S,10S,13S)-10-(4-fluorobenzyl)-7-formyl-3-methyl-4,9,12-trioxo-3,8,11-triazabicyclo[12.3.1]octadeca-1(18),14,16-trien-13-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.000002
N-[(7S,10S,13S)-10-(4-fluorobenzyl)-7-formyl-4,9,12-trioxo-3,8,11-triazabicyclo[12.3.1]octadeca-1(18),14,16-trien-13-yl]-5-methyl-1,2-oxazole-3-carboxamide
Rhinovirus B14
-
pH 7.4, temperature not specified
0.0075
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-isoleucinamide
Norwalk virus
-
pH and temperature not specified in the publication
0.00145
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
Norwalk virus
-
pH and temperature not specified in the publication
0.00087
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-norleucinamide
Norwalk virus
-
pH and temperature not specified in the publication
0.0072
N2-(morpholin-4-ylcarbonyl)-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
Norwalk virus
-
pH and temperature not specified in the publication
0.00065 - 0.00202
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
0.00055 - 0.00284
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
0.00068
N6-(1-acetylprolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.017
N6-(N-acetylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00064
N6-(N-acetylalanylprolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.0046
N6-(prolylalanyl)-N-[(2E,4S)-7-amino-1-ethoxy-1,7-dioxohept-2-en-4-yl]lysinamide
Foot-and-mouth disease virus
-
at pH 7.4 and 37°C
0.00178
Nalpha-(tert-butoxycarbonyl)-N-[(2S)-4-(cyclopropylamino)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]butan-2-yl]-4-fluoro-L-phenylalaninamide
Enterovirus A71
-
78 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00142
Nalpha-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-[(3S)-2-oxopiperidin-3-yl]-4-(propan-2-ylamino)butan-2-yl]-4-fluoro-L-phenylalaninamide
Enterovirus A71
-
77 mM Tris, pH 7.0, 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 10% glycerol, 30°C, substrate (2-(N-methylamino)benzoyl)-IEALFQGPPK(2,4-dinitrophenyl)-FR
0.00034 - 0.0073
rupintrivir
additional information
2-(2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl)propyl amino-3-(2-oxo-3-pyrrolidyl)-propan-1-al
0.0002
(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
Human rhinovirus sp.
-
pH 8.0, 37°C, recombinant enzyme
0.00177
(2S)-2-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonic acid
Human poliovirus 1
-
pH 8.0, 37°C, recombinant enzyme
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[(4-phenylpiperazin-1-yl)carbonyl]-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
8.57
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[(4-phenylpiperazin-1-yl)carbonyl]-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
pH and temperature not specified in the publication
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(pyridin-2-yl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
10.62
(4R,5R)-N-(1,3-benzothiazol-2-yl)-2,2-dimethyl-5-[[4-(pyridin-2-yl)piperazin-1-yl]carbonyl]-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
pH and temperature not specified in the publication
0.01
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[[4-(2-cyanophenyl)piperazin-1-yl]carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
above, pH and temperature not specified in the publication
2.5
(4R,5R)-N-(1,3-benzothiazol-2-yl)-5-[[4-(2-cyanophenyl)piperazin-1-yl]carbonyl]-2,2-dimethyl-1,3-dioxolane-4-carboxamide
Human rhinovirus sp.
-
pH and temperature not specified in the publication
0.018
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.051
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.0161
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
Human rhinovirus sp.
-
pH 7.5, 37°C
0.01778
1-(2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)acetyl)-4-ethylthiosemicarbazide
Hepatovirus A
-
pH 7.5, 37°C
0.00594
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
Hepatovirus A
-
pH 7.5, 37°C
0.0063
2-(2-oxo-4-phenyl-2H-chromen-7-yloxy)-N'-(1-(4-chlorophenyl)ethylidene)acetohydrazide
Human rhinovirus sp.
-
pH 7.5, 37°C
0.024
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.125
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.01
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.017
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.0084
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.0096
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.013
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.025
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.005
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.02
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.0068
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.022
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.012
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.0166
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.042
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Severe acute respiratory syndrome-related coronavirus
-
pH 7, 25°C
0.098
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
Coxsackievirus B3
-
pH 7, 25°C
0.00065
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
Human rhinovirus sp.
-
pH 8.0, 37°C, recombinant enzyme
0.00182
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
Norwalk virus
-
pH and temperature not specified in the publication
0.00202
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
Human poliovirus 1
-
pH 8.0, 37°C, recombinant enzyme
0.00055
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
Human rhinovirus sp.
-
pH 8.0, 37°C, recombinant enzyme
0.00284
N2-[(benzyloxy)carbonyl]-N-[(2S)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)-4-(propan-2-ylamino)butan-2-yl]-L-leucinamide
Human poliovirus 1
-
pH 8.0, 37°C, recombinant enzyme
0.00034
rupintrivir
Human rhinovirus sp.
-
pH 8.0, 37°C, recombinant enzyme
0.00165
rupintrivir
Enterovirus A71
-
pH 6.5, 25°C
0.00183
rupintrivir
Human poliovirus 1
-
pH 8.0, 37°C, recombinant enzyme
0.002
rupintrivir
Coxsackievirus A16
-
pH 6.5, 25°C
0.0023
rupintrivir
Enterovirus A71
pH 7.0, 30°C
0.0023
rupintrivir
Enterovirus A71
-
pH and temperature not specified in the publication
0.0073
rupintrivir
Enterovirus A71
-
pH and temperature not specified in the publication
additional information
2-(2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl)propyl amino-3-(2-oxo-3-pyrrolidyl)-propan-1-al
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.16 microM
additional information
2-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl amino-3-(2-oxo-3-pyrrolidyl)-propan-1-al
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.018 microM
additional information
ethyl 4-[2-(4-cinnamoyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 1.3 microM
additional information
ethyl 4-[2-(tert-butoxycarbonyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is above 20 microM
additional information
ethyl 4-[2-(tert-butoxycarbonyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
IC50 value is above 0.02 mM
additional information
ethyl 4-[2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 1.8 microM
additional information
ethyl 4-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl-amino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 2.9 microM
additional information
N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.096 microM
additional information
N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-[(2E)-3-(1,3-benzodioxol-5-yl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-[(2E)-3-(4-chloro-2-fluorophenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.007 microM
additional information
Nalpha-[(2E)-3-(4-chloro-2-fluorophenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-[(2E)-3-(4-methylphenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.026 microM
additional information
Nalpha-[(2E)-3-(4-methylphenyl)prop-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-[(2E)-4-(5-methyl-1,2-oxazol-3-yl)but-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.94 microM
additional information
Nalpha-[(2E)-4-(5-methyl-1,2-oxazol-3-yl)but-2-enoyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-[(benzyloxy)carbonyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.031 microM
additional information
Nalpha-[(benzyloxy)carbonyl]-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
additional information
Nalpha-{(2E)-3-[4-(dimethylamino)phenyl]prop-2-enoyl}-N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-phenylalaninamide
enterovirus
-
IC50 value is below 0.5 microM
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.