Information on EC 3.4.22.28 - picornain 3C

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The expected taxonomic range for this enzyme is: Viruses

EC NUMBER
COMMENTARY
3.4.22.28
-
RECOMMENDED NAME
GeneOntology No.
picornain 3C
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Selective cleavage of Gln-/-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3C protease
-
-
-
-
3C protease
-
-
3C protease
bovine herpesvirus 1 Schoenboeken
-
-
-
3C protease
-
-
3C protease
-
-
3C protease
enterovirus CVB2
-
-
-
3C protease
Foot-and-mouth disease virus A Iran 97, Foot-and-mouth disease virus A1061, Foot-and-mouth disease virus A10_61, Foot-and-mouth disease virus O/NY00
-
-
-
3C protease
-
-
3C protease
-
-
3C protease
E9LTP4
-
3C protease
-
-
3C protease
-
-
3C protease
Human rhinovirus 14
-
-
3C protease
-
-
3C protease
-
-
3C protease
-
-
3C protease
Q04544
-
3C protein
-
-
3C protein
-
-
3C proteinase
-
-
-
-
3C proteinase
-
-
3C proteinase
coxsackievirus CVB3
-
-
-
3C proteinase
-
-
3C proteinase
-
-
3CP
bovine herpesvirus 1 Schoenboeken
-
-
-
3CP
Foot-and-mouth disease virus A Iran 97
-
-
-
3Cpro
coxsackievirus CVB3
-
-
-
3Cpro
-
-
3Cpro
-
3Cpro from foot-and-mouth disease is unusual among 3C proteases in being able to cleave sequences with P1-Gln or P1-Glu
3Cpro
-
a chymotrypsin-like cysteine protease
3Cpro
Foot-and-mouth disease virus A1061
-
a chymotrypsin-like cysteine protease
-
3Cpro
Foot-and-mouth disease virus A10_61
-
-
-
3Cpro
E9LTP4
-
3Cpro
Human rhinovirus 14
-
-
3Cpro
-
-
3Cpro protease
-
-
coxsackievirus 3C proteinase
-
-
-
-
cysteine proteinase 3C
-
-
-
-
foot-and-mouth protease 3C
-
-
-
-
HAC 3C
-
-
-
-
hepatitis A virus 3C proteinase
-
-
-
-
nonstructural 3 protease
-
-
NS3 protease
-
-
P3C
-
-
-
-
picornain 3C
-
-
picornain-3C
-
-
picornavirus endopeptidase 3C
-
-
-
-
poliovirus protease 3C
-
-
-
-
poliovirus proteinase 3C
-
-
-
-
protease 3C
-
-
-
-
protease 3C
-
-
protease 3C
-
-
proteinase, foot-and-mouth-disease virus, 3C
-
-
-
-
proteinase, picornavirus, 3C
-
-
-
-
proteinase, poliovirus, 3C
-
-
-
-
proteinase, rhinovirus, 3C
-
-
-
-
rhinovirus protease 3C
-
-
-
-
SV3CP
Q04544
-
tomato ringspot nepovirus 3C-related protease
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
97162-88-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bovine enterovirus
-
-
-
Manually annotated by BRENDA team
strain Schoenboeken
-
-
Manually annotated by BRENDA team
bovine herpesvirus 1 Schoenboeken
strain Schoenboeken
-
-
Manually annotated by BRENDA team
Coxsackie B virus (CVB)
-
-
Manually annotated by BRENDA team
recombinant enzyme; strain B3
-
-
Manually annotated by BRENDA team
recombinant enzyme; strain B3; wild-type and catalytic site-directed mutants
-
-
Manually annotated by BRENDA team
coxsackievirus B3
strain B3
-
-
Manually annotated by BRENDA team
coxsackievirus CVB3
CVB3
-
-
Manually annotated by BRENDA team
enterovirus 71, TW2231/98
-
-
Manually annotated by BRENDA team
human rhinovirus 14
-
-
Manually annotated by BRENDA team
human rhinovirus; recombinant enzyme; type 14; wild-type
-
-
Manually annotated by BRENDA team
human rhinovirus; type 14
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
strain CVB2, CVB5, EV6, and EV9
-
-
Manually annotated by BRENDA team
enterovirus CVB2
strain CVB2, CVB5, EV6, and EV9
-
-
Manually annotated by BRENDA team
strain A Iran 97
-
-
Manually annotated by BRENDA team
wild-type and mutant
-
-
Manually annotated by BRENDA team
Foot-and-mouth disease virus A Iran 97
strain A Iran 97
-
-
Manually annotated by BRENDA team
Foot-and-mouth disease virus A1061
strain A1061
-
-
Manually annotated by BRENDA team
Foot-and-mouth disease virus A10_61
strain A10_61
-
-
Manually annotated by BRENDA team
Foot-and-mouth disease virus O/NY00
strain O/NY00
-
-
Manually annotated by BRENDA team
C172A and C24S/C172A; recombinant enzyme
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
recombinant enzyme; wild-type and 3 mutants: C24S
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
recombinant enzyme; type 2, i.e. Sabin strain; wild-type and catalytic site-directed mutant D85N
-
-
Manually annotated by BRENDA team
type 1, human poliovirus; type 1, i.e. Mahoney strain
-
-
Manually annotated by BRENDA team
type 1, i.e. Mahoney strain
-
-
Manually annotated by BRENDA team
type 2, i.e. Sabin strain
-
-
Manually annotated by BRENDA team
Human enterovirus C Mahoney
type 1, i.e. Mahoney strain
-
-
Manually annotated by BRENDA team
Human enterovirus C Sabin
type 2, i.e. Sabin strain
-
-
Manually annotated by BRENDA team
Human rhinovirus 14
-
-
-
Manually annotated by BRENDA team
23 clinical isolates
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
expression of a functional 3C protease, in combination with the capsid protein precursor P1 or alone, is not compatible with productive replication of bovine herpesvirus 1
physiological function
-
human rhinovirus 3C protease contributes to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown
physiological function
-
the 3C protein is able to inhibit virus-induced activation of the interferon-beta promoter. When expressed in mammalian cells, the 3C protein suppresses retinoid acid-inducible gene-I signaling by disruption of the acid-inducible gene-I-interferon promoter-stimulating factor-1 complex and interferon regulatory factor 3 nuclear translocation. Enterovirus 71 infection does not stimulate the expression of interferon-beta, interferon-stimulated genes 54, 56, and tumor necrosis factor-alpha in rhabdomyosarcoma cells. The 3C protein of enterovirus 71 is able to inhibit virus-induced activation of the interferon-beta promoter and inhibits interferon-beta expression by targeting the adaptor retinoid acid-inducible gene I
physiological function
-
3Cpro cleavage inactivates CstF-64 and impairs the host cell polyadenylation in vitro, as well as in virus-infected cells
physiological function
-
infection of cells with coxsackievirus leads to the cleavage of the adaptor molecules MAVS and TRIF through 3Cpro, indicating that a single protease suppresses innate immune signaling through two pathways. 3Cpro cleaves specific residues within MAVS and TRIF that render these molecules deficient in type I IFN signaling and apoptotic signaling
physiological function
bovine herpesvirus 1 Schoenboeken
-
expression of a functional 3C protease, in combination with the capsid protein precursor P1 or alone, is not compatible with productive replication of bovine herpesvirus 1
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate + H2O
?
show the reaction diagram
-
slowly turned over
-
-
?
2-aminobenzoic acid-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoic acid-Phe-Thr-Gln-Ser-Glu-Gly-Glu-Phe(NO2)-Ala + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
2-aminobenzoyl-AALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-AALFQ + GPLQ-EDDnp
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EAAFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EAAFQ + GPLQ-EDDnp
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EALFQAPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + APLQ-EDDnp
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EALFQGALQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GALQ-EDDnp
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EALFQGPAQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPAQ-EDDnp
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EALFQGPLQ-EDDnp + H2O
2-aminobenzoyl-EALFQ + GPLQ-EDDnp
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
fluorogenic substrate
-
-
?
5-bromopyridin-3-yl furan-3-carboxylate + H2O
?
show the reaction diagram
-
slowly turned over
-
-
?
5-chloropyridin-3-yl furan-2-carboxylate + H2O
?
show the reaction diagram
-
slowly turned over
-
-
?
7-methoxycoumarin-4-yl-MEALFQGPLQY-2,4-dinitrophenyl amide + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-EALFQGPLQ-EDDnp + H2O
Abz-EALFQ + GPLQ-EDDnp
show the reaction diagram
-
-
-
-
?
abz-SVTLQSGY(NO2)R + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
-
?
Ac-DEFQLQ-4-nitroanilide + H2O
?
show the reaction diagram
Q04544
-
-
-
?
Ac-EFQLQ-4-nitroanilide + H2O
?
show the reaction diagram
Q04544
-
-
-
?
Ac-FQLQ-4-nitroanilide + H2O
?
show the reaction diagram
Q04544
-
-
-
?
Ac-RHSVGATLEALFQGPPVYREIKIS-NH2 + H2O
Ac-RHSVGATLEALFQ + GPPVYREIKIS-NH2
show the reaction diagram
-
-
-
-
?
acetyl-Arg-Pro-Val-Val-Val-Gln-Gly-Pro-Asn-NH2 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
corresponding to poliovirus type 2 polyprotein cleavage site 2C/3A
-
?
acetyl-ELRTQSFS-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Gly-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Gly
show the reaction diagram
-
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
show the reaction diagram
coxsackievirus, coxsackievirus B3
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro
show the reaction diagram
coxsackievirus, coxsackievirus B3
-
-
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
show the reaction diagram
coxsackievirus, coxsackievirus B3
-
sequence corresponding to 2C/3A cleavage site of polyprotein
-
?
acetyl-Glu-Ala-Leu-Phe-Gln-NH2 + H2O
acetyl-Glu-Ala-Leu-Phe-Gln + NH3
show the reaction diagram
coxsackievirus, coxsackievirus B3
-
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
show the reaction diagram
-
best substrate, corresponding to poliovirus type 2 polyprotein cleavage site 2B/2C
-
?
acetyl-Glu-Leu-Arg-Thr-Gln-Ser-Phe-Ser-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Glu-Leu-Arg-Thr-Gln-Ser-Phe-Ser-NH2 + H2O
?
show the reaction diagram
-
hepatitis A virus
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Human enterovirus C Sabin
-
corresponding to amino acid sequence flanking 2C/3A cleavage site, wild-type and mutant D85N enzyme
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
corresponding to poliovirus type 2 polyprotein cleavage site 3A/3B
-
?
activated transcription factor TFIIIC + H2O
?
show the reaction diagram
-
in HeLa-cells, poliovirus enzyme, in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription
-
-
?
APAKELLNFD + H2O
APAKE + LLNFD
show the reaction diagram
-
-
-
-
?
APAKQLLNFD + H2O
APAKQ + LLNFD
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
represents 2C/3A cleavage site, wild-type and E71D, D85N, K155E mutants, not other mutants
-
?
Bid protein + H2O
?
show the reaction diagram
-
-
-
-
?
cAMP-regulated response element binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
cAMP-responsible element binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
cardiovirus polyprotein + H2O
?
show the reaction diagram
-
cleavage specificity
-
-
?
cardiovirus polyprotein + H2O
?
show the reaction diagram
coxsackievirus B4
-
-
-
-
?
CstF-64 protein + H2O
?
show the reaction diagram
-
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-GLRTQSFS-Edans + H2O
?
show the reaction diagram
-
fluorogenic substrate, hydrolysis at the glutamine residue
-
-
?
dabcyl-GLRTQSND(edans)G + H2O
?
show the reaction diagram
-
fluorogenic substrate
-
-
?
Dabcyl-KIGNTIEALFQGPPKFRE-Edans + H2O
Dabcyl-KIGNTIEALFQ + GPPKFRE-Edans
show the reaction diagram
-
-
-
-
?
Dabcyl-KTSAVLQSGFRKME-Edans + H2O
Dabcyl-KTSAVL + QSGFRKME-Edans
show the reaction diagram
-
-
-
-
?
Dabcyl-RTATVQGPSLDFEEdans + H2O
Dabcyl-RTATVQ + GPSLDFEEdans
show the reaction diagram
E9LTP4
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
Human enterovirus C, Human enterovirus C Sabin
-
i.e. peptide corresponding to cleavage site between poliovirus polypeptides 2A and 2B
-
?
DEAMEQGVSDYI + H2O
DEAMEQ + GVSDYI
show the reaction diagram
-
-
-
-
?
DRRETLFQ-4-nitroanilide + H2O
DRRETLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
DSLETLFQ-4-nitroanilide + H2O
DSLETLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
DSLEVLFQ-4-nitroanilide + H2O
DSLEVLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
DSRETLFQ-4-nitroanilide + H2O
DSRETLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
EALFQ-4-nitroanilide + H2O
EALFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Edans-EDFHLQGPEDLAK-Dabcyl + H2O
?
show the reaction diagram
-
-
-
-
?
eIF4GI + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage sites: Gln-Gly, Glu-Ser and Glu-Ala
-
-
?
enterovirus polyprotein + H2O
?
show the reaction diagram
-
cleavage specificity
-
-
?
enterovirus polyprotein + H2O
?
show the reaction diagram
coxsackievirus B4
-
-
-
-
?
ETLFQ-4-nitroanilide + H2O
ETLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
show the reaction diagram
-
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-?
show the reaction diagram
-
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
-
-
?
eukaryotic translation initiation factor 4Gl + H2O
?
show the reaction diagram
-
-
-
-
?
EVLFQ-4-nitroanilide + H2O
EVLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.7
-
-
?
FAGLAQAVTQGFPTEL + H2O
FAGLAQAVTQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 2.93
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.11
-
-
?
FAGLRAAVTQGFPTEL + H2O
FAGLRAAVTQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 4.45
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.65
-
-
?
FAGLRQAVEQGFPTEL + H2O
FAGLRQAVEQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 3.79
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 14.22
-
-
?
FAGLRQAVFQGFPTEL + H2O
FAGLRQAVFQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 18.65
-
-
?
FAGLRQAVKQGFPTEL + H2O
FAGLRQAVKQ + GFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.902
-
-
?
FAGLRQAVKQGIPTEL + H2O
FAGLRQAVKQ + GIPTEL
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.3
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 5.77
-
-
?
FAGLRQAVTQGFPTEL + H2O
FAGLRQAVTQ + GFPTEL
show the reaction diagram
-
reference peptide, cleavage efficacy (micromol/l/min): 5.08
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.21
-
-
?
FAGLRQAVTQSFPTEL + H2O
FAGLRQAVTQ + SFPTEL
show the reaction diagram
-
mutated peptide, cleavage efficacy (micromol/l/min): 0.27
-
-
?
Foot-and-mouth disease virus polyprotein + H2O
?
show the reaction diagram
Foot-and-mouth disease virus, Foot-and-mouth disease virus A10_61
-
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 P1 precursor polyprotein + H2O
mature structural foot-and-mouth-disease virus proteins
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
Glu-Ala-Ile-Ala-Glu-Glu-Gln-Gly-Leu-Ser-Asp-Tyr-Ile-Thr + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
Glu-Ala-Leu-Phe-Gln-Gly-Pro-Pro-Val + H2O
Glu-Ala-Leu-Phe-Gln + Gly-Pro-Pro-Val
show the reaction diagram
coxsackievirus, coxsackievirus B3
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
deltaVP1-P2-P3*, C-terminally truncated protein
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
most effective cleavage at 2A/2B and 2C/3A sites
via respective intermediate products
?
hepatitis A virus P2-P3 precursor polyprotein + H2O
?
show the reaction diagram
-
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 protein P1-2A + hepatitis A virus protein P3 + hepatitis A virus protein 2BC + hepatitis A virus protein 3D + hepatitis A virus protein 3ABC
show the reaction diagram
-
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
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner
-
-
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme is responsible for the processing of the viral polyprotein
-
-
?
histone H3 protein + H2O
?
show the reaction diagram
-
-
-
-
?
histone protein H3 + H2O
?
show the reaction diagram
-
in BHK-cells, foot-and-mouth-disease virus enzyme
-
-
?
human rhinovirus 3CD polyprotein fragment + H2O
?
show the reaction diagram
-
recombinant enzyme HRV-14, structure/mechanism study
-
-
?
human rhinovirus polyprotein + H2O
1AB/1C/1D/2C/delta3CD
show the reaction diagram
-
-
-
-
?
IEALFQGPPKFR + H2O
IEALFQ + GPPKFR
show the reaction diagram
-
-
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 10.72
-
-
?
IGNTIEALFQGPPKFR + H2O
IGNTIEALFQ + GPPKFR
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 8.37
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.055
-
-
?
ILGIPIVQKQSASWLK + H2O
ILGIPIVQKQ + SASWLK
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.063
-
-
?
in vitro-translated (35S)methionine-labeled transcription factor cyclic AMP-responsive element binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 4.1
-
-
?
KPVLRTATVQGPSLDF + H2O
KPVLRTATVQ + GPSLDF
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 4.3
-
-
?
L-P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1-2A
show the reaction diagram
-
cardioviruses
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ + GEIQWM
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 5.09
-
-
?
LKRGYFASEQGEIQWM + H2O
LKRGYFASEQ GEIQWM
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 5.01
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 8.26
-
-
?
LKRSYFASEQGEIQWV + H2O
LKRSYFASEQ + GEIQWV
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 9.78
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.22
-
-
?
LWLDEEAMEQGVSDYI + H2O
LWLDEEAMEQ + GVSDYI
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.23
-
-
?
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
show the reaction diagram
-
-
-
?
nucleoporin + H2O
?
show the reaction diagram
-
-
-
-
?
P1-2A polyprotein + H2O
hydrolyzed P1-2A polyprotein
show the reaction diagram
Foot-and-mouth disease virus, bovine herpesvirus 1, Foot-and-mouth disease virus A Iran 97, bovine herpesvirus 1 Schoenboeken
-
-
-
-
?
P1-2A precursor polypeptide of encephalomyocarditis virus + H2O
peptide P1 + peptide 2A
show the reaction diagram
-
cardio- and aphthoviruses
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
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
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
bovine enterovirus, echovirus
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
essential for processing of virus polyprotein containing structural proteins and enzymes including the protease 3C itself
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
the enzyme is essential for viral replication and infectivity
-
-
-
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
most maturation cleavages within the precursor polyprotein are mediated by the enzyme
-
-
-
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
coxsackievirus B4
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
coxsackievirus B4
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
Human enterovirus C Mahoney
-
involved in proteolytic processing of virus polyprotein
-
-
?
poliovirus 3ABC precursor polyprotein + H2O
poliovirus protein 3A + poliovirus protein 3B + poliovirus protein 3C
show the reaction diagram
Human enterovirus C, Human enterovirus C Sabin
-
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
show the reaction diagram
-
-
-
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
show the reaction diagram
-
trans-cleavage
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
show the reaction diagram
Human enterovirus C, Human enterovirus C Sabin
-
trans-cleavage
-
-
?
poliovirus P1 precursor polyprotein + H2O
capsid proteins
show the reaction diagram
Human enterovirus C Mahoney
-
trans-cleavage
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
exclusive cleavage site: Gln-Gly
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
cleavage map
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
initial cleavage at 2C-3A and 2B-2C, followed by 3A-3B and/or 3C-3D
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
proteolytic autocatalysis
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
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
show the reaction diagram
-
essential for processing of virus polyprotein containing strucutral proteins and enzymes including the protease 3C itself
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
the polyprotein is cleaved into mature proteins predominantly by the viral 3C protease
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
Human enterovirus C Mahoney
-
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, involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein fragment corresponding to 2BC coding region + H2O
?
show the reaction diagram
Human enterovirus C, Human enterovirus C Sabin
-
in-trans cleavage, wild-type and mutant D85N enzyme
-
-
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
polypeptide translated from plasmid DNA T7-delta3A-3B-3Cmut-delta3D
delta3A-3B-3Cmut + 3Cmut-delta3D + 3B-3Cmut-delta3D
show the reaction diagram
-
-
-
-
?
pro-caspase 3 + H2O
caspase 3 + ?
show the reaction diagram
-
-
-
-
?
QTGTIQGDRVAD + H2O
QTGTIQ + GDRVAD
show the reaction diagram
-
-
-
-
?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
show the reaction diagram
-
-
-
-
?
rhinovirus polyprotein + H2O
?
show the reaction diagram
-
cleavage specificity
-
-
?
RNA polymerase I factor SL-1 + H2O
?
show the reaction diagram
-
-
-
-
?
RQAVTQGFPTEL + H2O
RQAVTQ + GFPTEL
show the reaction diagram
-
-
-
-
?
TATA binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
TATA-binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
Thr-Gly-Leu-Phe-Gln-Gly-Pro + H2O
Thr-Gly-Leu-Phe-Gln + Gly-Pro
show the reaction diagram
-
-
-
-
?
TLFQ-4-nitroanilide + H2O
TLFG + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
transcription factor OCT-1 + H2O
?
show the reaction diagram
-
cleaved by 3Cpro, precursor 3CD and mutant 3CD delta371
-
-
?
TSAVLQSGFRKM + H2O
TSAVLQ + SGFRKM
show the reaction diagram
-
-
-
-
?
TTLEALFQGPPVY + H2O
?
show the reaction diagram
-
-
-
-
?
viral 3CD protein + H2O
?
show the reaction diagram
-
-
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.56
-
-
?
VIYKLFAGFQGAYSGA + H2O
VIYKLFAGFQ + GAYSGA
show the reaction diagram
-
cleavage efficacy (micromol/l/min): 0.63
-
-
?
YFCSEQGEIQWN + H2O
YFCSEQ + GEIQWN
show the reaction diagram
-
-
-
-
?
mitochondrial antiviral signaling protein + H2O
?
show the reaction diagram
-
3Cpro-mediated MAVS cleavage occurrs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling
-
-
?
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 acetyl-Glu-Ala-Leu-Phe-Glu-Gly-Pro
-
-
-
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
?
-
-
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
?
-
-
catalytic sites: Cys172 (nucleophile) and His44 (general base), His191 defines Gln-residue specificity
-
-
-
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
?
-
-
the enzyme induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
-
-
-
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
?
-
-
cleavage of purified fusion proteins by immobilised protease
-
-
-
additional information
?
-
-
does not cleave death-associated protein 5
-
-
-
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
?
-
-
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
?
-
-
chymotrypsin-like protease is required for viral replication
-
-
-
additional information
?
-
-
picornavirus 3Cpro generally cleaves peptides at the Gln/Gly junction
-
-
-
additional information
?
-
-
the foot-and-mouth disease virus 3Cpro to cleaves sequences containing either P1-Gln or P1-Glu
-
-
-
additional information
?
-
coxsackievirus B3
-
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
?
-
coxsackievirus B3
-
no hydrolysis of acetyl-Glu-Ala-Leu-Phe-Glu-Gly-Pro
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
activated transcription factor TFIIIC + H2O
?
show the reaction diagram
-
in HeLa-cells, poliovirus enzyme, involved in shut-off of host-cell transcription
-
-
?
eukaryotic initiation factor + H2O
eukaryotic initiation factor 1-478 + eukaryotic initiation factor 479-?
show the reaction diagram
-
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-?
show the reaction diagram
-
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
-
-
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
processing relies on protease 3C as single proteinase controlled in a concentration-dependent manner
-
-
?
hepatitis A virus polyprotein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the enzyme is responsible for the processing of the viral polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
bovine enterovirus, echovirus
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
essential for processing of virus polyprotein containing structural proteins and enzymes including the protease 3C itself
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
the enzyme is essential for viral maturation and infectivity through the cleavage of polyprotein precursor
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
the enzyme is essential for viral replication and infectivity
-
-
-
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
-
most maturation cleavages within the precursor polyprotein are mediated by the enzyme
-
-
-
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
coxsackievirus B4
-
involved in proteolytic processing of virus polyprotein
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
show the reaction diagram
Human enterovirus C Mahoney
-
involved in proteolytic processing of virus polyprotein
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
essential for processing of virus polyprotein containing strucutral proteins and enzymes including the protease 3C itself
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
the polyprotein is cleaved into mature proteins predominantly by the viral 3C protease
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poliovirus polyprotein + H2O
hydrolyzed poliovirus polyprotein
show the reaction diagram
Human enterovirus C Mahoney
-
involved in proteolytic processing of poliovirus polyprotein
-
-
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
show the reaction diagram
-
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
fragments of poly(A)-binding protein
show the reaction diagram
-
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
-
-
?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
show the reaction diagram
-
-
-
-
?
Thr-Gly-Leu-Phe-Gln-Gly-Pro + H2O
Thr-Gly-Leu-Phe-Gln + Gly-Pro
show the reaction diagram
-
-
-
-
?
Toll/IL-1 receptor domain-containing adaptor inducing interferon-beta + H2O
?
show the reaction diagram
-
3Cpro cleaves both the N- and C-terminal domains of TRIF and localizes with TRIF to signalosome complexes within the cytoplasm
-
-
?
mitochondrial antiviral signaling protein + H2O
?
show the reaction diagram
-
3Cpro-mediated MAVS cleavage occurrs within its proline-rich region, leads to its relocalization from the mitochondrial membrane, and ablates its downstream signaling
-
-
?
additional information
?
-
-
the enzyme induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
-
-
-
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
?
-
-
chymotrypsin-like protease is required for viral replication
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
3C protease requires neither cofactors nor metals for activity
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cl-
-
activates
HPO42-
-
activates
SO42-
-
activates
SO42-
-
activates at high concentrations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
(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)-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-Dibromoacetone
-
-
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
-
13C-labeled beta-lactone
-
-
-
2,2'-dipyridyl disulfide
-
0.4 mM, complete inhibition
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
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-acetylbenzamide
-
-
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-bromoisoindolin-1-one
-
-
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
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
-
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 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
-
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 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
-
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 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
-
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
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-(2-phenylethyl)-2-(pyridin-3-yl)quinolin-4(1H)-one
-
100% effect at 0.1 mM
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-[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)
-
-
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
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
azidicarboxamide
-
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
-
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]
-
-
beta-lactones
-
-
-
bis-vinylic organotellurane
-
-
Calpastatin
-
0.8 mM, 30% inhibition
-
chloro-telluroxetane
-
-
chymostatin
-
-
chymostatin
-
0.1 mM, 54% inhibition
dimethyl 5-acetylbenzene-1,3-dicarboxylate
-
-
Elastinal
-
-
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 (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
-
-
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
iodoacetamide
bovine enterovirus
-
-
iodoacetamide
-
only wild-type enzyme, not C147S-mutant
iodoacetamide
-
-
iodoacetamide
-
-
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-3-(benzylamino)-5-carbamoylbenzoate
-
-
methyl-3-amino-5-carbamoylbenzoate
-
-
methyl-3-carbamoyl-5-(dibenzylamino)benzoate
-
-
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
Q04544
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-Cbz-L-serine beta-lactone
-
irreversible inhibitor, associated with His 102 of the enzyme
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-Methylmaleimide
-
-
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-[(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
-
-
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)-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
-
-
NEM
bovine enterovirus
-
-
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
-
-
-
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
rupintrivir
-
irreversible inhibitor of human enterovirus strains (4 of 4)
rupintrivir
-
potent in vitro activity against 23 clinical isolates tested in H1-HeLa cell protection assays
rupintrivir
-
AG7088
TLCK
-
0.2 mM, 51% inhibition
Tos-Phe-CH2-Cl
-
-
vinyl sulfones
-
-
-
Zn2+
-
2.0 mM ZnCl2, complete inhibition
methyl-3-{2,2-difluoro-1-[(2-methoxyethoxy)methoxy]ethenyl}-5-{[(trifluoromethyl)sulfonyl]oxy}benzoate
-
-
-
additional information
-
no inhibition by Triton X-100
-
additional information
-
no inhibition by Triton X-100, that inhibits picornain 3CD
-
additional information
-
-
-
additional information
-
no inhibition by acetyl-Leu-Ala-Ala-Gln'-thioester
-
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
-
not inhibited by the viral RNA polymerase 3Dpol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetate
-
activates
Sodium citrate
-
the peptidase activity of picornain-3C is 100fold higher in the presence of 1.5 M sodium citrate
additional information
-
no activation by Triton X-100
-
additional information
-
proteinase-active polypeptide precursor (3CD) and mature 3Cpro have equivalent cleavage activity on purified poly(A) binding protein, but only 3Cpro cleavage activity is stimulated by poly(A) binding protein-binding viral RNA
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00018
-
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate
-
-
0.0182
-
2-aminobenzoyl-AALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.02
-
2-aminobenzoyl-AALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0264
-
2-aminobenzoyl-EAAFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0349
-
2-aminobenzoyl-EAAFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.0413
-
2-aminobenzoyl-EALAQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.0435
-
2-aminobenzoyl-EALAQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0393
-
2-aminobenzoyl-EALFQAPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0533
-
2-aminobenzoyl-EALFQGALQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0185
-
2-aminobenzoyl-EALFQGPAQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.0213
-
2-aminobenzoyl-EALFQGPAQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.014
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.016
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.0179
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in D2O, in the absence of sodium citrate
0.0203
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in D2O, in the presence of 1 M sodium citrate
0.0058
-
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQSGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
-
0.00012
-
5-bromopyridin-3-yl furan-3-carboxylate
-
-
0.00024
-
5-chloropyridin-3-yl furan-2-carboxylate
-
-
0.8
-
Ac-DEFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
0.3
-
Ac-EFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
1.5
-
Ac-FQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
1.3
-
Asp-Ser-Leu-Glu-Thr-Leu-Phe-Gln-Gly-Pro-Val-Tyr-Lys-Asp-Leu-Glu
-
-
0.25
2.6
peptides derived from polyprotein cleavage sites
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00025
-
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate
-
-
0.01
-
2-aminobenzoyl-AALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.96
-
2-aminobenzoyl-AALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.08
-
2-aminobenzoyl-EAAFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
3.34
-
2-aminobenzoyl-EAAFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.01
-
2-aminobenzoyl-EALAQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.66
-
2-aminobenzoyl-EALAQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.34
-
2-aminobenzoyl-EALFQAPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.28
-
2-aminobenzoyl-EALFQGALQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.03
-
2-aminobenzoyl-EALFQGPAQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
2.72
-
2-aminobenzoyl-EALFQGPAQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
0.03
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate
0.06
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in D2O, in the absence of sodium citrate
0.87
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate
2.02
-
2-aminobenzoyl-EALFQGPLQ-EDDnp
-
in D2O, in the presence of 1 M sodium citrate
27
-
4-(4-dimethylaminophenylazo)benzoic acid-KTSAVLQSGFRKME-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
-
0.00119
-
5-bromopyridin-3-yl furan-3-carboxylate
-
-
0.0011
-
5-chloropyridin-3-yl furan-2-carboxylate
-
-
0.33
-
Ac-DEFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
0.14
-
Ac-EFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
0.08
-
Ac-FQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.41
-
Ac-DEFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
0
0.46
-
Ac-EFQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
0
0.05
-
Ac-FQLQ-4-nitroanilide
Q04544
pH 8.5, temperature not specified in the publication
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000042
-
acetyl-Leu-Ala-Ala-(N,N'-dimethylglutaminal)
-
25C, mutant enzyme C24S
0.00004
-
benzyloxycarbonyl-Leu-Phe-(glutaminol)
-
-
0.00019
-
benzyloxycarbonyl-Leu-Phe-L-(cyanomethyl-alaninal)
-
-
0.000005
-
benzyloxycarbonyl-Leu-Phe-L-(N,N-dimethyl-glutaminyl)
-
-
0.000006
-
benzyloxycarbonyl-Leu-Phe-L-(N-acetylamino-alaninal)
-
-
0.000012
-
benzyloxycarbonyl-Leu-Phe-L-(N-benzoylamino-alaninal)
-
-
0.000066
-
benzyloxycarbonyl-Leu-Phe-L-(N-butyloxycarbonylamino-alaninal)
-
-
0.000132
-
benzyloxycarbonyl-Leu-Phe-L-(N-carbomethoxyamino-alaninal)
-
-
0.000073
-
benzyloxycarbonyl-Leu-Phe-L-(N-formylamino-alaninal)
-
-
0.000018
-
benzyloxycarbonyl-Leu-Phe-L-(N-isobutyrylamino-alaninal)
-
-
0.000007
-
benzyloxycarbonyl-Leu-Phe-L-(N-propinylamino-alaninal)
-
-
0.0036
-
benzyloxycarbonyl-Leu-Phe-L-glutaminal-hemiaminal
-
-
0.000146
-
benzyloxycarbonyl-Leu-Phe-L-[(N-trifluoroacetyl)amino-alaninal]
-
-
0.000005
-
benzyloxycarbonyl-Leu-Phe-L-[methional sulfoxide]
-
-
0.000052
-
benzyloxycarbonyl-Leu-Phe-L-[N-(2-pyrrolidinone)-alaninal]
-
-
0.000005
-
benzyloxycarbonyl-Leu-Phe-L-[N-(isoxazole-5-carbonyl)aminoalaninal]
-
-
0.00001
-
benzyloxycarbonyl-Leu-Phe-L-[N-(N,N-dimethylcarbamoyl)amino-alaninal]
-
-
0.00064
-
benzyloxycarbonyl-Leu-Phe-[(N-methylsulfonyl)amino-alaninal]
-
-
0.000469
-
benzyloxycarbonyl-Leu-Phe-[N-(Me)Ac-amino-alaninal]
-
-
0.0015
-
N-(benzyloxycarbonyl)-D-serine-beta-lactone
-
pH 7.5, 25C
0.184
-
N-(benzyloxycarbonyl)-L-serine-beta-lactone
-
pH 7.5, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.075
-
(3S)-[N3-(benzyloxycarbonyl)-N1-[3'-(N,N-dimethylamino)-3'-oxopropyl]-N1-(p-methylphenylsulfonyl)]-1,3-diaminobutan-2-one
-
weak competitive, IC50: 0.075 mM
0.00014
-
(E)-5-chloropyridin-3-yl 3-(furan-2-yl)acrylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.018
-
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.024
-
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.125
-
3-phenyl-1-(3,4-dichlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.01
-
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.017
-
3-phenyl-1-(3-chlorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.0084
-
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.0096
-
3-phenyl-1-(3-nitrophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.013
-
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.025
-
3-phenyl-1-(4-chlorophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.005
-
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.02
-
3-phenyl-1-(4-cyanophenyl)-4-(4-carboxybenzylidene)-pyrazol-5(4H)-one
-
pH 7, 25C
0.0068
-
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.022
-
3-phenyl-1-(4-fluorophenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.012
-
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.0166
-
3-phenyl-1-(4-methoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.042
-
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.098
-
3-phenyl-1-(4-trifluoromethoxyphenyl)-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
0.1
-
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
-
0.00008
-
5-bromopyridin-3-yl furan-2-carboxylate
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30C
0.000053
-
5-bromopyridin-3-yl furan-3-carboxylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.00029
-
5-chloropyridin-3-yl 1H-pyrazole-3-carboxylate
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30C
0.00069
-
5-chloropyridin-3-yl 4-ethoxy-2-[(E)-2-phenylethenyl]-1,3-oxazole-5-carboxylate
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30C
0.0012
-
5-chloropyridin-3-yl 5-bromofuran-2-carboxylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.00025
-
5-chloropyridin-3-yl 5-nitro-1H-pyrazole-3-carboxylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.000338
-
5-chloropyridin-3-yl furan-2-carboxylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.00071
-
5-chloropyridin-3-yl naphthalene-2-carboxylate
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30C
-
0.00047
-
5-chloropyridin-3-yl thiophene-2-carboxylate
-
0.1 M potassium phosphate, 2 mM EDTA, pH 7.5, 100 nM proteinase, 37C
0.03
-
ammonium trichloro (dioxoethylene-O,O')tellurate
-
25C, pH not specified in the publication, value above
0.0001
-
bis-vinylic organotellurane
-
25C, pH not specified in the publication
0.0082
-
ethyl 4-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl-amino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
0.0106
-
ethyl 4[2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
0.0075
-
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-isoleucinamide
-
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
-
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
-
pH and temperature not specified in the publication
0.00165
-
rupintrivir
-
pH 6.5, 25C
0.002
-
rupintrivir
-
pH 6.5, 25C
0.0023
-
rupintrivir
E9LTP4
pH 7.0, 30C
0.051
-
1,3-diphenyl-4-(4-carboxybenzylidene)pyrazol-5(4H)-one
-
pH 7, 25C
additional information
-
2-(2-[3,4-(methylenedioxy)cinnamoyl]amino-1-oxo-3-phenyl)propyl amino-3-(2-oxo-3-pyrrolidyl)-propan-1-al
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.16 microM
0.0002
-
2-oxo-1,2-dihydroquinolin-4-yl furan-2-carboxylate
-
in 50 mM Tris (pH 7.6), 1 mM EDTA, at 30C
additional information
-
2-[2-[4-(dimethylamino)cinnamoyl]amino-1-oxo-3-phenyl]propyl amino-3-(2-oxo-3-pyrrolidyl)-propan-1-al
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.018 microM
0.00084
-
chloro-telluroxetane
-
25C, pH not specified in the publication
additional information
-
ethyl 4-[2-(4-cinnamoyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 1.3 microM
0.01
-
ethyl 4-[2-(4-cinnamoyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
-
additional information
-
ethyl 4-[2-(tert-butoxycarbonyl)amino-1-oxo-3-phenyl]propylamino-5-(2-oxo-3-pyrrolidyl)-2-pentenoate
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is above 20 microM; 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
-
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
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 2.9 microM
0.00087
-
N-[(benzyloxy)carbonyl]glycyl-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-norleucinamide
-
pH and temperature not specified in the publication
additional information
-
N-{(2S)-1-oxo-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.096 microM; IC50 value is below 0.5 microM
0.00182
-
N2-[(benzyloxy)carbonyl]-N-[(2S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl]-L-leucinamide
-
pH and temperature not specified in the publication
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
-
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
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.007 microM; 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
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.026 microM; 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
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.94 microM; 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
-
concentration required to reduce the virus-induced cell death by 50% relative to the virus control is 0.031 microM; 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
-
IC50 value is below 0.5 microM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
EV71 3C protease shows substantially better activity (60fold) against the substrate peptide TSAVLQSGFRKM compared to other tested substrates
additional information
-
-
uridylylation efficiency for soluble 3C mutants is determined. 3C mutants D5A, E45A, E71A and E96A/D99A exhibit at least a 2fold reduction in Vpg peptide uridylylation. Mutants E24A and D50A exhibit an increase in Vpg peptide uridylylation on the order of 2fold greater than wild type 3C. Other mutants do not exhibit a substantial difference (2fold or greater) in Vpg peptide uridylylation activity relative to wild type
additional information
-
-
3Cpro inhibits cap-independent translation mediated by the poliovirus internal ribosome entry site in a dose-dependent manner in HeLa translation extracts displaying cap-poly(A) synergy, 3Cpro-induced translation inhibition can be partially rescued by addition of recombinant poly(A)-binding protein in vitro; combined 2Apro and 3Cpro result in a net stimulation of poliovirus internal ribosome entry site-mediated translation, the resulting rate of translation is about 3fold greater than the control value but not as great as the 4fold stimulation of translation from preincubation with 2Apro alone
additional information
-
-
3Cpro cleavage of endogenous poly(A) binding protein in HeLa S10 lysates displays a rapid initial cleavage rate where 70% cleavage requires only 10 min incubation but very little additional substrate is cleaved upon extended incubation periods; addition of increasing concentrations of PABP-interacting protein 1 do not affect 3Cpro-mediated cleavage of poly(A) binding protein, at the highest concentration (3 microg) of PABP-interacting protein 1 tested, increasing concentrations of 3Cpro (1-3 microg) lead to a dose-dependent increase in cleavage of poly(A) binding protein; biphasic poly(A) binding protein cleavage kinetics by 3Cpro, about 30% of total protein is rapidly cleaved in 10 min, followed by a much slower cleavage rate that does not reach completion by 60 min or extended incubation periods; cleavage kinetics analysis indicates that poly(A) binding protein exists in multiple conformations, some of which are resistant to 3Cpro cleavage and can be modulated by reducing potential; poly(A) binding protein on cellular polysomes is cleaved only by 3Cpro; poly(A) binding protein sediments with non-ribosome fractions, 40S and 80S ribosomes and polysome fractions, addition of 3Cpro to each of these fractions leads to partial cleavage in every case, and only slightly higher percent cleavage of poly(A) binding protein in polysome fractions or 40S-80S fractions; the Ras-GTPase activating protein SH3 domain-binding protein 1 is rapidly cleaved by 3Cpro to completion when supplied as purified recombinant protein or as endogenous protein in HeLa S10 lysates; while only 40-75% of poly(A) binding protein in S10 lysates is cleaved in vitro by 3Cpro, a crude ribosome pellet fraction, which is deficient in endogenous PABP-interacting protein 2, is cleaved by 95%
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
assay at
7
-
E9LTP4
assay at
7.2
-
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at, 150 mM NaCl, 50 mM Tris-HCl
8.5
-
Q04544
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
E9LTP4
assay at
30
-
-
assay at
37
-
-
-
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.35
-
-
isoform D from wild-type and active mutant C24S
8.5
-
-
isoelectric focusing
8.65
-
-
isoform C from wild-type and active mutant C24S and isoforms C from mutants C24S/C172A and C172A
8.85
-
-
isoform B from wild-type and active mutant C24S
9.1
-
-
isoform A from wild-type and active mutant C24S and isoforms A from mutants C24S/C172A and C172A
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
recombinant HRV14 3Cpro
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mature 3Cpro and precursor 3CD detected 2-4 hours post-infection of HeLa cells
Manually annotated by BRENDA team
-
recombinant enzyme, expressed in Escherichia coli
Manually annotated by BRENDA team
-
recombinant enzyme, expressed in Escherichia coli
Manually annotated by BRENDA team
-
recombinant enzyme; rhinovirus, expressed in Escherichia coli
Manually annotated by BRENDA team
-
mature 3Cpro and precursor 3CD detected 2-4 hours post-infection of HeLa cells
Manually annotated by BRENDA team
-
native enzyme: partial; recombinant enzyme
-
Manually annotated by BRENDA team
-
recombinant enzyme
-
Manually annotated by BRENDA team
-
recombinant enzyme
-
Manually annotated by BRENDA team
-
recombinant enzyme
-
Manually annotated by BRENDA team
coxsackievirus B3, coxsackievirus B4
-
recombinant enzyme
-
-
Manually annotated by BRENDA team
Human enterovirus C Sabin
-
native enzyme: partial; recombinant enzyme
-
-
Manually annotated by BRENDA team
coxsackievirus B4
-
recombinant enzyme
-
Manually annotated by BRENDA team
additional information
-
in the perinuclear membrane
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Coxsackievirus A16
Coxsackievirus A16
Coxsackievirus A16
Human hepatitis A virus genotype IB (isolate HM175)
Human hepatitis A virus genotype IB (isolate HM175)
Human hepatitis A virus genotype IB (isolate HM175)
Human hepatitis A virus genotype IB (isolate HM175)
Human hepatitis A virus genotype IB (isolate HM175)
Human hepatitis A virus genotype IB (isolate MBB)
Human hepatitis A virus genotype IB (isolate MBB)
Human rhinovirus 2
Human rhinovirus 2
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
in the presence of sodium citrate, gel filtration
20000
-
-
SDS-PAGE
22400
-
-
in the absence of sodium citrate, gel filtration
23880
-
-
wild type 3C proteinase, determined by MALDI-TOF mass spectrometry
23970
-
-
wild type 3C proteinase in complex with inhibitor compound 24, determined by MALDI-TOF mass spectrometry
25000
-
-
poliovirus, recombinant enzyme, gel filtration
additional information
-
-
amino acid sequence compared to that of some other cysteine and some serine proteases
additional information
-
-
amino acid sequences
additional information
-
-
amino acid composition
additional information
-
-
enzyme structure
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 26000, SDS-PAGE
?
-
x * 24000, SDS-PAGE
dimer
-
3C dimer interacts with 3Dpol
monomer
-
1 * 25000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE, under reducing conditions, wild-type and C172A mutant enzyme each behave as dimers under nonreducing conditions
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of AG7088 bound to serotype 2 rhinovirus 3C protease, hanging-drop vapor diffusion method
-
crystal structure of inhibitors covalently bound to the enzyme, hanging drop vapor diffusion method
-
high-resolution cocrystal structures for the inhibitors bound to the enzyme benzyloxycarbonyl-Leu-Phe-(N,N-dimethyl-glutaminyl), benzyloxycarbonyl-Leu-Phe-[methional sulfoxide] or benzyloxycarbonyl-Leu-Phe-(N-acetyl-aminoalaninal)
-
in complex with substrate APAKQLLNFD, sitting drop vapor diffusion method, using 40-42.5% (w/v)polyethylene glycol 400, 0.2 M LiSO4 and 0.1 M Tris (pH 8.0), and in complex with substrate APAKELLNFD, sitting drop vapor diffusion method, using 41-43% (w/v) polyethylene glycol 400, 0.2 M LiSO4 and 0.1 M Tris (pH 8.0)
-
sitting drop vapour diffusion method with 16 to 22% polyethylene glycol 4000, 100 mM Tris HCl (pH 8.5), and 2 mM sodium acetate
-
sitting drop vapour diffusion, at 1.9 A resolution
-
sitting drop vapour diffusion, iterative crystal-screening strategy, at 1.9 A resolution
-
double mutant C24S/C172A
-
hanging drop vapor diffusion method at room temperature, to 1.5 A resolution
-
in complex with inhibitors N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-fluoromethyl ketone, N-acetyl-L-leucyl-phenylalanyl-phenylalanyl-glutamate-fluoromethyl ketone, and N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-(1,4-dioxo-3,4-dihydro-1H-phthalazin-2-yl)methyl ketone
-
high-resolution crystal structures of the EV71 3Cpro/rupintrivir complex is determined, showing that although rupintrivir interacts with EV71 3Cpro similarly to HRV 3Cpro, the C terminus of the inhibitor cannot accommodate the leaving-group pockets of EV71 3Cpro. EV71 3Cpro possesses a surface-recessive S2' pocket that is not present in HRV 3Cpro that contributes to the additional substrate binding affinity
E9LTP4
crystal structure of 3Cpro alone and in complex with the anti-HRV molecules compound (AG7404) and rupintrivir (AG7088) at resolutions of 1.9, 1.3, and 1.5 A is reported. This 20.2-kDa cysteine protease adopts a chymotrypsin-like fold with a catalytic triad, Cys147-His40-Glu71, located in the cleft between the two six-stranded barrels. The residues that form the inhibitor binding pockets are highly conserved among EV 3Cpros, which explains the broad activity of compounds developed initially against a specific virus
-
X-ray structure of the Southampton norovirus 3C protease (SV3CP) bound to an active site-directed peptide inhibitor which has been refined at 1.7 A resolution is described
Q04544
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
47
-
-
pH 8.0, melting point of mutant enzyme M27G/C147S is 46.5, for mutant enzyme M37G it is 46.7C
48
-
-
pH 8.5, melting point of mutant enzyme M27G/C147S is 47.7C, for mutant enzyme M27G it is 48.1C
50
-
-
pH 9.5, melting point of mutant enzyme M27G/C147S and M27G is 50.4, for mutant enzyme M27G it is 50.0C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol stabilizes during gel filtration
-
enzyme is less stable in eukaryotic cells than in bacteria
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
3C protease activity is insensitive against up to 10% organic solvents
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 2 months
-
-80C, in 0.05 M phosphate buffer, pH 6.8, 10 mM cysteine, 5 mM EDTA, 10% glycerol, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
as expressed in Escherichia coli; as fusion protein; recombinant enzyme
-
as expressed in Escherichia coli; from Escherichia coli membrane fraction
-
as expressed in Escherichia coli; mutant enzyme; recombinant enzyme; to near homogeneity
-
from Escherichia coli inclusion bodies
-
recombinant enzymes are purified by using a Ni-NTA column
-
on TALON resin and by gel filtration on a Hi Load 16/60 Superdex 75 column
-
Talon beads chromatography
-
TALON resin chromatography and by gel filtration
-
2 isoforms, as expressed in Escherichia coli; recombinant enzymes
-
recombinant enzyme is purified by ion exchange chromatography
-
recombinant enzymes; wild-type and 3 mutant enzymes
-
nickel-chelating column chromatography
-
using Ni-NTA chromatography
-
His-3Cpro is purified using Ni-nitrilotriacetic acid chelating resin under non-denaturing conditions
-
recombinant enzyme
-
recombinant enzyme; recombinant enzyme from Escherichia coli in soluble form; recombinant enzyme from infected HeLa cells, to near homogeneity
-
Resource-Q column chromatography and a Superdex-75 gel filtration
-
to near homogeneity
-
using a DEAE column
Human rhinovirus 14
-
Q-Sepharose column chromatography and BioGel hydroxyapatite column chromatography
-
recombinant protein purified to 90% homogeneity
-
using the IMPACT-CN system
-
soluble mutant proteins are purified to greater than 80% purity in a single step by using a nickel nitrilotriacetic acid agarose spin column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in COS-7 cells
-
expressed in HEK-293T cells; recombinant 3Cpro is expressed in Escherichia coli
-
expressed in HeLa cells
-
expression as a fusion protein in Escherichia coli
-
expression in Escherichia coli 21 (DE3)
-
overexpressed
-
expressed in HeLa cells
-
expressed in HeLa cells
-
expressed with pET16b vector contained a N- or C-terminal hexa-His tag in Escherichia coli, protease with a C-terminus His-tag has specific activity equal to that of the tag-free enzyme, but the enzyme with N-terminal His-tag displays 10fold lower activity, indicating that additional N-terminal amino acids interfered with the protease activity
-
expression as a fusion protein in Escherichia coli
-
into pET-23a and expressed in Escherichia coli BL21 (DE3 pLysS)
-
cloned into a plasmid under the control of the bacteriophage T7 promoter, expressed both in an in vito transcription-translation system and in vivo in an Escherichia coli system containig an inducible T7 RNA polymerase
-
expressed in CEF cells infected with the recombinant fowlpox virus vUTAL3CP1 containing the 3C protease coding regions of foot-and-mouth-disease virus
-
expressed in COS-7 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in HeLa cells
-
expression in baby hamster kidney cells and human A293 cells
-
expression in Escherichia coli BL21 (DE3) pLysS
-
expression in Escherichia coli BL21 (DE3) pLysS from a pET-28 vector modified to add a thrombin-cleavable N-terminal polyhistidine tag
-
expressed in HeLa cells
-
expression in bacteria, cell-free transcription-translation systems and eukaryotic cells
-
expression in Escherichia coli
-
the 3Cpro mutant is produced heterologously using Escherichia coli BL21(DE3) pLysS containing pHAV-3CEX
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in HeLa cells
-
expressed in Escherichia coli
-
cloned and expressed in Escherichia coli as a His-tagged fusion protein
-
; expressed in HeLa cells
-
a cDNA fragment containing the 3C protease coding region is inserted into pET22b vector and expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli or BL21(D3)
-
expressed in Escherichia coli or BL21(D3); expressed in HeLa cells
-
expressed in Escherichia coli strain JM 109
-
expressed in HEK-293T cells; recombinant 3Cpro is expressed in Escherichia coli
-
expressed in HeLa cells; expression in BLR pLys DE3
-
into pQE30 and expressed in Escherichia coli M15 pREP4 strain
-
poliovirus His-3Cpro is expressed in Escherichia coli from pET-3C
-
segment of poliovirus genome: nucleotides 5438-6061
-
expressed in Escherichia coli
Human rhinovirus 14
-
cloned into cDNA and expressed in Escherichia coli BL21 (DE3) pLysS, transfection of HeLa cells; expressed in HeLa cells
-
expressed in Escherichia coli BL2 1 (DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
-
green fluorescent protein-tagged enzyme is expressed in COS-7 cells
-
expressed in HeLa cells
-
2 recombinant adenoviruses are constructed expressing foot-and-mouth disease virus capsid and 3C/3CD proteins in replicative deficient human adenovirus type 5 vector, production of adeno-FMD hybrid virus, about 50% of vaccinated pigs can be protected after virus challenge when the LPB-ELISA antibody titers are between 4 and 45
-
expressed in HeLa cells
-
expression of 3C mutants in Escherichia coli
-
expressed in HeLa cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C146S
-
mutant protease does not cleave Glu-Ala-Ile-Ala-Glu-Glu-Gln-Gly-Leu-Ser-Asp-Tyr-Ile-Thr
C147S
-
no proteolytic activity in vivo and in vitro
D85N
-
possesses proteolytic activity equal to that of wild type
G155A
-
markedly reduced RNA binding activity
H40D
-
no proteolytic activity in vivo and in vitro
I86A
-
no proteolytic activity
K156Q
-
markedly reduced RNA binding activity
K82Q
-
possesses proteolytic activity equal to that of wild type
R84K
-
possesses proteolytic activity equal to that of wild type
R84Q
-
possesses proteolytic activity equal to that of wild type
V154S
-
markedly reduced RNA binding activity, possesses proteolytic activity equal to that of wild type
V154T
-
still binds to viral RNA though with lower efficiency than the wild type, possesses proteolytic activity equal to that of wild type
A133S
-
processed enzyme, polydispersity of 35%
A133S/C142S
-
processed enzyme, polydispersity of 29%
C142A
-
mutant shows reduced activity
C142L
-
mutant shows increased activity
C142L
-
introduction of the C142L mutation into a type O1K FMDV has no significant effect on the infectivity of the virus in tissue culture
C142S
-
processed enzyme, polydispersity of 25%
C142S
-
enhanced solubility
C142S
-
mutation has no effect onsubstrate specificity but drastically reduces the proteolytic activity of the enzyme to less than 1% of the wild type activity
C142T
-
mutant shows reduced activity
C142V
-
mutant shows reduced activity
C163A
-
elimination of the activity of the active site nucleophile
C31A
-
the single mutation reduces the rate of cleavage of the APAKQLLNFD peptide by about 3fold
C31A/L47A
-
the double mutation causes only a very slight further reduction in cleavage activity of the APAKQLLNFD peptide compared to the single mutation C31A
C95K
-
processed enzyme, polydispersity of 37%
C95K
-
enhanced solubility
C95K/C142S
-
processed enzyme, polydispersity of 11%
C95K/C142S
-
both mutations are required to make the recombinant enzyme soluble
D84E
-
cleavage by the D84E mutant is about 200times slower than cleavage by wild type enzyme
F70S
-
incorrect processed enzyme
I55D
-
insoluble enzyme
I55N/M56T
-
incorrect processed enzyme
L82D
-
processed enzyme, polydispersity of 55%
L82D/C142S
-
partially processed enzyme, polydispersity of 33%
M81N
-
processed enzyme, polydispersity of 33%
M81N/C142S
-
processed enzyme, polydispersity of 19%
P114S/V115D
-
unprocessed enzyme
P713T
-
the human eIF4GI mutant is cleaved efficiently by 3Cpro
V124S
-
processed enzyme, polydispersity of 47%
V124S/C142S
-
processed enzyme, polydispersity of 29%
V140S
-
processed enzyme
C142A
Foot-and-mouth disease virus A1061
-
mutant shows reduced activity
-
C142L
Foot-and-mouth disease virus A1061
-
mutant shows increased activity
-
C142S
Foot-and-mouth disease virus A1061
-
mutation has no effect onsubstrate specificity but drastically reduces the proteolytic activity of the enzyme to less than 1% of the wild type activity
-
C142T
Foot-and-mouth disease virus A1061
-
mutant shows reduced activity
-
C95K/C142S
Foot-and-mouth disease virus A1061
-
both mutations are required to make the recombinant enzyme soluble
-
C142S
Foot-and-mouth disease virus A10_61
-
enhanced solubility
-
C163A
Foot-and-mouth disease virus A10_61
-
elimination of the activity of the active site nucleophile
-
C95K
Foot-and-mouth disease virus A10_61
-
enhanced solubility
-
C172G
-
mutation results in complete loss of virus-specific proteolytic cascade
C172S
-
mutation results in complete loss of virus-specific proteolytic cascade
C24S
-
mutant enzyme in which the nonessential surface cysteine is replaced with serine and which exhibits catalytic parameters identical to those of wild-type enzyme
C24S
-
intact active site Cys172, displays the same catalytic properties as the wild-type enzyme
C24S
-
substitution of the non-essential surface cysteine residue in the C24S variant prevents intermolecular disulfide bond formation
D98N
-
mutation results in only slightly delayed processing
D98N/V47G
-
mutation results in a pronounced loss of processing
H44Y
-
mutation results in complete loss of virus-specific proteolytic cascade
C147A
-
catalytically inactive mutant is successfully crystallized in the presence of peptide KPVLRTATVQGPSLDF. Mutant also folds into two domains and exhibits extremely high structural similarity to its coxsackievirus counterpart
C147A
-
inactive mutant does not induce the appearance of a MAVS cleavage product
C147A
-
catalytically inactive mutant is successfully crystallized in the presence of peptide KPVLRTATVQGPSLDF. Mutant also folds into two domains and exhibits extremely high structural similarity to its coxsackievirus counterpart
E71D
E9LTP4
enzyme is void of catalytic activity. Structure of mutant E71D is determined: The structure shows that when Glu71 is replaced by Asp, the side chain is simply too short to reach the catalytic histidine and thus cannot provide enough electrostatic stabilization to the residue
H133G
E9LTP4
mutant H133G has close-to-wild-type enzyme activity and substrate specificity. Due to the practical difficulty in obtaining the measurable crystals from the wild-type, H133G mutant is used
H40G
-
inactive enzyme
N69D
E9LTP4
kcat/Km values are significantly reduced in mutant compared to wild-type
N69S
E9LTP4
kcat/Km values are significantly reduced in mutant compared to wild-type
R39E
E9LTP4
kcat/Km values are significantly reduced in mutant compared to wild-type
R39K
E9LTP4
kcat/Km values are significantly reduced in mutant compared to wild-type
R39T
E9LTP4
kcat/Km values are significantly reduced in mutant compared to wild-type
C147A
-
inactive mutant
C147A
-
catalytically inactive 3C proteinase has only a modest effect on translation when high doses are added to lysates, and proteinase that is heat inactivated at 70C for 15 min has no significant effect on translation
C147S
-
inactive mutant enzyme
E71Q
-
inactive mutant enzyme
H40Y
-
inactive mutant enzyme
M27G
-
indistinguishable from wild type enzyme
Q537E
-
cleavage-resistant mutant of poly(A)-binding protein
C147S
Human enterovirus C Sabin
-
inactive mutant enzyme
-
E71Q
Human enterovirus C Sabin
-
inactive mutant enzyme
-
D32A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
D50A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
D58A/E63A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
D5A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
D64A
-
infectious virus can not be recovered from three of the mutated RNA in transfected HeLa cells
D85A
-
infectious virus can not be recovered from three of the mutated RNA in transfected HeLa cells
E121A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
E24A
-
the specific infectivity is reduced by 100fold relative to wild type RNA in transfected HeLa cells
E45A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
E53A/E55A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
E71A
-
infectious virus can not be recovered from three of the mutated RNA in transfected HeLa cells
E81A
-
the specific infectivity is equivalent to wild type RNA in transfected HeLa cells
E96A/D99A
-
the specific infectivity is reduced by 100fold relative to wild type RNA in transfected HeLa cells
M27G/C147S
-
430fold reduction in specificity rate constant, the bell-shaped curve for the modified enzyme is shifted towards the alkaline pH values by 0.45 units on the acidic side and by 0.9 units on the alkaline side. The reduced activity of the enzyme is primarily due to the less ordered ground state of ist reaction
additional information
-
2C deletion mutants affect its ability to inhibit 3Cpro
H40Y
Human enterovirus C Sabin
-
inactive mutant enzyme
-
additional information
-
3CD delta371 with deletion of 371 aa at the carboxyl terminus of 3D
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
3Cpro as the molecular target to develop anti enterovirus 71 agents
drug development
-
3C protease inhibitors as anti-enterovirus anti-EV71 agents
medicine
-
conservation of critical amino acid residues in 3C protease and the potent, broad-spectrum activity of rupintrivir highlight the advantage of 3C protease as an antiviral target
medicine
enterovirus CVB2
-
conservation of critical amino acid residues in 3C protease and the potent, broad-spectrum activity of rupintrivir highlight the advantage of 3C protease as an antiviral target
-
medicine
-
foot-and mouth disease virus 3Cpro plays a vital role in virus replication, the enzyme is an attractive target for antiviral drugs
medicine
-
3Cpro as an attractive target for antiviral drugs
medicine
Foot-and-mouth disease virus A10_61
-
3Cpro as an attractive target for antiviral drugs
-
medicine
-
the enzyme is essential for viral replication and infectivity and represents a target for the development of antiviral drugs
medicine
-
attractive target for antiviral drugs
medicine
-
poliovirus-encoded nonstructural polypeptide 2C can negatively regulate the viral protease 3Cpro-mediated cleavage of transcription factor cyclic AMP-responsive element binding protein in vitro
medicine
-
enteroviruses use a dual strategy for host translation shutoff, requiring cleavage of poly(A)-binding protein by 3Cpro and of translation iniation factor 4GI by 2Apro, inhibition of endogenous mRNA translation by 3Cpro in HeLa cells is independent of translation iniation factor 4GI or translation iniation factor 4GI cleavage
molecular biology
Human rhinovirus 14
-
a protein-tagging system for purification of EGFP from Escherichia coli using a single-step glutathione column purification and release of EGFP from the column using a variant of Human Rhinovirus 14 3C is described. A biotinylated variant of Human Rhinovirus 14 3C protease (bHR3Cp) is constructed, which includes a factor Xa or thrombin cleavage site between the protease gene and the biotinylation signal. This system readily allows attachment of the protease to a variety of surfaces and subsequent release using either thrombin or factor Xa proteases
drug development
-
three-dimensional pharmacophore models for peptidic and small organic nonpeptidic inhibitors of the human rhinovirus 3C protease, structure-based and ligand-based approach, using the software package Catalyst
drug development
-
3CP is an optimal target for the development of anti-viral agents
medicine
-
conservation of critical amino acid residues in 3C protease and the potent, broad-spectrum activity of rupintrivir highlight the advantage of 3C protease as an antiviral target
additional information
-
stemloop D of the 5' cloverleaf RNA is the cognate ligand of the coxsackievirus B3 3C proteinase, both are indispensable components of the viral replication initiation complex, NMR spectroscopy of the stemloop D structure, 3Cpro recognizes a structural motif instead of a specific sequence
additional information
coxsackievirus CVB3
-
stemloop D of the 5' cloverleaf RNA is the cognate ligand of the coxsackievirus B3 3C proteinase, both are indispensable components of the viral replication initiation complex, NMR spectroscopy of the stemloop D structure, 3Cpro recognizes a structural motif instead of a specific sequence
-