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Information on EC 3.4.21.91 - Flavivirin
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3.4.21.91 FlavivirinSpecify your search results
Word Map
- 3.4.21.91
- polyprotein
- viruses
- ns4a
-
replicons
-
west
- ribavirin
-
anti-hcv
-
direct-acting
-
virologic
-
cirrhosis
-
flaviviral
- boceprevir
- flaviviruses
- encephalitis
-
pegylated
- flaviviridae
- telaprevir
-
subgenomic
-
rna-dependent
-
unwind
-
mosquito-borne
- asunaprevir
-
resistance-associated
-
daclatasvir
- simeprevir
-
hcv-infected
- coronaviruses
-
anti-dengue
- ntpase
-
peptidomimetic
-
nonnucleoside
-
hcv-specific
-
macrodomains
- drug development
-
treatment-naive
-
peginterferon
-
replicase
-
quasispecies
-
interferon-free
-
trans-cleavage
- alphavirus
-
positive-stranded
- sofosbuvir
- analysis
- molecular biology
-
rna-stimulated
- medicine
-
hcv-1b
- synthesis
- gt1
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Selective hydrolysis of -Xaa-Xaa-/-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala
Synonyms
ns3 protease, nonstructural protein 3, ns2b-ns3 protease, ns3 serine protease, ns2b-ns3pro, ns2b/ns3 protease, ns3 proteinase, ns3pro, ns2b/ns3, zikv protease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dengue NS2b-NS3 protease
dengue virus protease
dengue virus serotype 2 protease
DENV2 NS2BNS3pro
DV2 NS2B/NS3pro
flavivirus NS2B-NS3 protease
NS2B-3 proteinase
NS2B-NS3 protease
NS2B-NS3 protease-helicase
NS2B-NS3 proteinase
NS2B-NS3 serine proteinase
NS2B-NS3(pro)teinase
NS2b-NS3-protease
NS2B-NS3pro
NS2B/NS3
NS2B/NS3 protease
NS2B/NS3 protease complex
NS2B/NS3pro serine protease
NS2B18NS3
NS3 protease
NS3 proteinase
Yellow fever virus (flavivirus) protease
-
-
-
-
ZIKV NS2B/NS3 protease
NS2B-3 proteinase
-
-
-
-
NS2B-NS3 protease
Dengue virus type 2 16681
-
-
-
NS2B-NS3 serine proteinase
Dengue virus type 2 16681
-
-
-
NS2B18NS3
-
NS3 protein covalently attached to 18 residues of the N22B cofactor region
NS2B18NS3
NS3 protein covalently attached to 18 residues of the N22B cofactor region
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Selective hydrolysis of -Xaa-Xaa-/-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
serine endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
154215-26-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-AAGRKSLTL-3-nitrotyrosine-amide + H2O
Abz-AAGRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-AGRKGTGN-3-nitrotyrosine-amide + H2O
Abz-AGRKGTGN + 3-nitrotyrosine-amide
-
the poorest substrate
-
-
?
Abz-AGRKS-3-nitrotyrosine-amide + H2O
Abz-AGRKS + 3-nitrotyrosine-amide
-
-
-
-
?
Abz-AGRKSLT-3-nitrotyrosine-amide + H2O
Abz-AGRK + SLT-3-nitrotyrosine-amide
-
-
-
-
?
Abz-ARRKSLTL-3-nitrotyrosine-amide + H2O
Abz-ARRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-FAAGRKSLTL-3-nitrotyrosine-amide + H2O
Abz-FAAGRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-GRKS-3-nitrotyrosine-amide + H2O
Abz-GRK + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-GRKSLTL-3-nitrotyrosine-amide + H2O
Abz-GRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-KKQR-AGVLnY-amide + H2O
Abz-KKQR + AGVLnY-amide
-
high degree of cleavage efficiency, based on the NS2B/NS3 polyprotein cleavage site
-
-
?
Abz-KKQRAGVL-3-nitrotyrosine-amide + H2O
Abz-KKQR + AGVL-3-nitrotyrosine-amide
-
is based on the NS2B/NS3 polyprotein cleavage site, shows high degree of cleavage efficiency
-
-
?
Abz-KKQRSAGM-3-nitrotyrosine-amide + H2O
Abz-KKQR + SAGM-3-nitrotyrosine-amide
-
substrates containing the capsid protein prime side sequence SAGM are efficiently hydrolysed
-
-
?
Abz-NRRRRSAGM-3-nitrotyrosine-amide + H2O
Abz-NRRRR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RKS-3-nitrotyrosine-amide + H2O
Abz-RK + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RKSLTL-3-nitrotyrosine-amide + H2O
Abz-RK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRR-3-nitrotyrosine-amide + H2O
Abz-RRRR + 3-nitrotyrosine-amide
-
marginal activity
-
-
?
Abz-RRRR-SAGnY-amide + H2O
Abz-RRRR + SAGnY-amide
-
efficient substrate of the NS3 protease, based on the Dengue virus capsid protein processing site
-
-
?
Abz-RRRRS-3-nitrotyrosine-amide + H2O
Abz-RRRR + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRRSAG-3-nitrotyrosine-amide + H2O
Abz-RRRR + SAG-3-nitrotyrosine-amide
-
most efficiently hydrolysed substrate, which contains the tetrabasic non-prime side sequence RRRR of the dengue virus capsid protein
-
-
?
Abz-RRRRSAGM-3-nitrotyrosine-amide + H2O
Abz-RRRR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRRSLTL-3-nitrotyrosineamide + H2O
Abz-RRRR + SLTL-3-nitrotyrosineamide
-
-
-
-
?
Abz-SKKRAGVL-3-nitrotyrosine-amide + H2O
Abz-SKKR + AGVL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-SKKRSAGM-3-nitrotyrosine-amide + H2O
Abz-SKKR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
substrate profiling of the P1 position using Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is natural or unnatural amino acid)
-
-
?
Ac-Thr-Arg-Arg-7-amido-4-methylcoumarin + H2O
Ac-Thr-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
acetyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
ADP ATOO-647N + H2O
?
-
affinity of complete NS3 molecule fused to 18 residues of the NS2B cofactor is 10fold higher than that of NS3 helicase
-
-
?
AQRRGRIG + H2O
?
-
three individual batches of the peptide results in 45%, 37%, and 36% cleavages
-
-
?
AQRRGRIG + H2O
AQRR + GRIG
-
three individual batches of the peptide results in AQRR2GRIG 3%, 2%, and 0% cleavages
-
-
?
ATP ATOO-647N + H2O
?
-
affinity of complete NS3 molecule fused to 18 residues of the NS2B cofactor is 10fold higher than that of NS3 helicase
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester + H2O
benzoyl-Nle-Lys-Arg-Arg + thiobenzoic acid
-
-
-
-
?
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Thr-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Thr-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Thr-Lys-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Thr-Thr-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
substrate of isoform DENV-2
-
-
?
Boc-Gly-Arg-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
Bz-Arg-Arg-4-methylcoumaryl-7-amide + H2O
Bz-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bz-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
10fold higher affinity for the tetrapeptide than for the tripeptide Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin, and processes it with 34fold greater efficiency
-
-
?
Dengue virus DEN4 polyprotein + H2O
?
-
involved in processing of downstream nonstructural proteins of the Dengue virus DEN4 polyprotein precursor
-
-
?
DSSTKRGGSW + H2O
DSSTKR + GGSW
-
each substrate plasmid contains the ER membrane-anchoring domain, a specific cleavage sequence that includes the P6-P1 P19-P49 residues and a fluorescent reporter group (DsRed)
-
-
?
Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
human neural transcription factor Sox2 + H2O
?
the substrate protein exhibits likely cleavage sites for NS2B-NS3pro: K95RLR-A99 and R110PRRK-T115
-
-
?
KPGLKRGGAK + H2O
KPGLKR + GGAK
-
each substrate plasmid contains the ER membrane-anchoring domain, a specific cleavage sequence that includes the P6-P1 P19-P49 residues and a fluorescent reporter group (DsRed)
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide + H2O
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-L-arginine + 5-amino-2-nitrobenzamide
substrate binding structure in the enzyme's active site (PDB ID 5LC0), modeling. The peptidic substrate with the sequence ABZ-Val-Lys-Lys-Arg-ANB-NH2 is selected as the most efficient peptidic substrate with the nonprimed binding sites of ZIKV NS3 protease
-
-
ir
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-pyridyl-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-pyridyl-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(guanidino)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(guanidino)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
NRKR + GGPA + H2O
NRKRGGPA
-
two individual batches of the peptide results in 78 and 77% cleavages
-
-
?
NS2B-3181-polyproteins + H2O
?
-
effect of mutations within Gly-Ala-Arg-Arg-+-Ser sequence on cis-cleavage (mutations at P1', P1, P2, P3 and P4), the term-+- depicts the point of cleavage
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-EVKKQR + AGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-FAAGRK + SLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-FAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-HRREKR + SVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
is poorly hydrolyzed
-
-
?
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KKR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KRR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-LNRRRR + TAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-RTSKKR + SWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-SAAGRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRKGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGLIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGNNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGRLQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRILRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRTGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRSRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-TTSTRR + GTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
PhAc-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
PhAc-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
substrate of isoform DENV-3
-
-
?
protein C of tick-borne encephalitis virus + H2O
?
-
the protein contains two amino acid sequence motifs within the carboxy-terminal region that match the canonical NS2B/3 recognition site. The downstream site is necessary and sufficient for efficient cleavage and virion assembly. In contrast, the upstream site is dispensable and placed in a structural context that renders it largely inaccessible to the viral protease. The NS2B/3 protease predominantly uses the downstream cleavage motif R95-R96-S97 for cleavage
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pyroglutamic acid-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pyroglutamic acid-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
QRRRGGTA + H2O
QRRR + GGTA
-
two individual batches of the peptide results in 58% cleavage
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
YF17D virus protein + H2O
?
-
cleavage site: Gln-Gln-Arg-+-Ser, i.e. 4A/2K site, this cleavage is prerequisite for processing at the downstream signalase site, determinants of cleavage site specificity for 2B/3 cleavage (site: Gly-Ala-Arg-Arg-+-Ser), the term-+- depicts the point of cleavage
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
Zika virus Brazilian isolate BeH823339
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
CFP-LQYTKRGGVLWD-YFP + H2O
CFP-LQYTKR + GGVLWD-YFP
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
CFP-LQYTKRGGVLWD-YFP + H2O
CFP-LQYTKR + GGVLWD-YFP
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
CFP-SAAQRRGRIGRN-YFP + H2O
CFP-SAAQRR + GRIGRN-YFP
-
cleavage is barely detectable
-
-
?
CFP-SAAQRRGRIGRN-YFP + H2O
CFP-SAAQRR + GRIGRN-YFP
-
cleavage is barely detectable
-
-
?
Dengue virus polyprotein + H2O
Dengue virus proteins NS3 and NS5
-
cleaves NS3/NS4A and NS4B/NS5 junctions, not NS4A/4B junction, cleavage site consists of 2 basic amino acids followed by Gly, Ala or Ser, e.g. Arg-Arg-/-Gly
-
?
eIF4G1 protein + H2O
?
-
human eukaryotic translation initiation factor 4 gamma 1, high activity
-
-
?
eIF4G1 protein + H2O
?
-
human eukaryotic translation initiation factor 4 gamma 1
-
-
?
Flavivirus sp. polyproteins + H2O
?
-
cleavage sites consist of Lys-Arg, Arg-Lys or Arg-Arg (Dengue virus: Gln-Arg) usually followed by Gln, Ala or Ser, cleavage sites: NS2A/2B, NS2B/3, NS3/4A (not SLE virus), NS4B/5 (not SLE virus)
-
-
?
Flavivirus sp. polyproteins + H2O
?
-
involved in processing of downstream nonstructural proteins of the virus polyprotein
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
LQYTKRGGVLWD + H2O
LQYTKR + GGVLWD
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
LQYTKRGGVLWD + H2O
LQYTKR + GGVLWD
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
Dengue virus type 2 Thailand/16681/1984
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
no substrate-dependent precipitation for either Alkhurma virus mutants or chimeric proteins
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
is most efficiently cleaved. Substrates containing two or three basic amino acids (Arg or Lys) in tandem are best
-
-
?
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
phenylacetyl-Lys-Lys-Arg-4-nitroanilide + H2O
phenylacetyl-Lys-Lys-Arg + 4-nitroaniline
-
-
-
-
?
phenylacetyl-Lys-Lys-Arg-4-nitroanilide + H2O
phenylacetyl-Lys-Lys-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
Dengue virus type 2 16681
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
efficiently cleaved
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Yellow fever virus protein + H2O
?
-
cleavage sites: 2A/2B, 2B/3, 3/4A and 4B/5, 4 dibasic sites in nonstructural region of viral polyprotein
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
strong preference for basic amino acid residues (Arg/Lys) at the P1 position, preference for the P2-4 sites are in the order of Arg > Thr > Gln/Asn/Lys for P2, Lys > Arg > Asn for P3, and Nle > Leu > Lys > Xaa for P4. The prime site substrate specificity is for small and polar amino acids in P1' and P3'
-
-
?
additional information
?
-
-
o-aminobenzoyl-EPEKQRTPQDNQQ-N-(2,4-dinitrophenyl)-ethylenediamine, o-aminobenzoyl-AGRRPAQ-N-(2,4-dinitrophenyl)-ethylenediamine and o-aminobenzoyl-AKRRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine are not hydrolyzed
-
-
?
additional information
?
-
-
peptides with a similar sequence, including GIKRGETD, LQKRGIVE, LSKRQHPG, LVTAGHGQ, and MLKKGMTT, are completely resistant to proteolysis
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
preferred substrate size for the dengue virus NS3 protease encompasses the residues from P4 to P3'. The presence of basic residues at the P3 and P4 positions significantly promotes reactivity. Serine is the preferred P1' residue
-
-
?
additional information
?
-
-
preferred substrate size for the Dengue virus NS3 protease encompasses the residues from P4 to P3'. Serine is the preferred P1' residue
-
-
?
additional information
?
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition
-
-
?
additional information
?
-
-
NS2B-NS3 protease is a trypsin-like protease with a serine protease catalytic triad (His51, Asp75, Ser135) that has a polybasic substrate recognition profile
-
-
?
additional information
?
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
NS2/3 auto-cleavage and NS3 protease activity
-
-
?
additional information
?
-
-
interaction of human brain proteins with the Japanese encephalitis virus NS2B-NS3 protease could be involved in the Japanese encephalitis virus induced pathogenesis
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
enzyme is highly specific toward lysines at the P2 and P3 positions
-
-
?
additional information
?
-
-
NS3 alone triggers the apoptotic pathways involving caspases-8 and -3. Activation of caspase-8 is essential to initiate apoptotic signaling in NS3-expressing cells
-
-
?
additional information
?
-
-
during purification, incomplete autolytic conversion of the 36 kDa NS2B-NS3pro construct into the individual 30 kDa NS3pro and the NS2B sequence (5-6 kDa). Undergoes self-cleavage during expression and purification at the K48G-G site of the glycine linker
-
-
?
additional information
?
-
-
peptides with a similar sequence, including GIKRGETD, LQKRGIVE, LSKRQHPG, LVTAGHGQ, and MLKKGMTT, are completely resistant to proteolysis. Peptides GLKRFGAK, KKQRAGVL, LYKRYGGF, MLKRGMPR, and NQKRYGGF are also not cleaved
-
-
?
additional information
?
-
-
strict substrate specificity, the (K/R)(K/R)R-GG amino acid motif is optimal. Efficiently cleaves peptides derived from the West Nile virus and Dengue virus capsid protein C, from the NS2A/NS2B junction region and NS4B/NS5 junction region and from NS2B/NS3
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage. It catalyzes two autolytic cleavages. The NS2B/NS3 junction is cleaved before protein purification. A second site at Arg4592Gly460 within the C-terminal helicase region of NS3 is cleaved more slowly. Intramolecular cleavage of both the N-terminal site and the internal helicase site of recombinant NS2B-NS3. The artificial substrates CFP-LQYTHMGGVLWD-YFP and CFP-GGGGHMGGVLWD-YFP are not cleaved
-
-
?
additional information
?
-
-
the substrate that corresponds to the NS4B/NS5 junction site is cleaved in trans, whereas the remaining substrates that correspond to the NS2A/NS2B,NS2B/NS3, and NS3/NS4A proprotein junction sites are poorly processed in trans under experimental conditions
-
-
?
additional information
?
-
-
enzyme is highly specific toward lysines at the P2 and P3 positions
-
-
?
additional information
?
-
-
strict substrate specificity, the (K/R)(K/R)R-GG amino acid motif is optimal. Efficiently cleaves peptides derived from the West Nile virus and Dengue virus capsid protein C, from the NS2A/NS2B junction region and NS4B/NS5 junction region and from NS2B/NS3
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage. It catalyzes two autolytic cleavages. The NS2B/NS3 junction is cleaved before protein purification. A second site at Arg4592Gly460 within the C-terminal helicase region of NS3 is cleaved more slowly. Intramolecular cleavage of both the N-terminal site and the internal helicase site of recombinant NS2B-NS3. The artificial substrates CFP-LQYTHMGGVLWD-YFP and CFP-GGGGHMGGVLWD-YFP are not cleaved
-
-
?
additional information
?
-
-
viral serine protease consisting of viral protein NS2B and NS3
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
cleavage preference for substrates containing basic amino acids
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
docking studies of the bioactive compounds at the active site of NS2B-NS3 complex also indicate 4-hydroxypanduratin A as potential lead compound for drug development
-
-
?
additional information
?
-
analysis of substrate specificity at substrate positions P1, P2, P3, and P4, and cleavage site parameters, detailed overview. Enzyme cleavage sequence is Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is a natural or nonnatural amino acid). The P4-P1 optimal sequence is D-Arg-Lys-Orn-Arg. Most preferred amino acid residues at P1 are L-Arg(Me) and L-Arg. At P2, the NS2B-NS3 protease displays also a very high level of specificity. The most preferred amino acids are the non-proteinogenic L-Orn (100%) and L-Arg(Z)2 (40%). Natural amino acids interact significantly weaker with the S2 pocket, and only L-Lys and L-Arg are recognized (38% and 17%, respectively). Similarly to the S2 and S1 pockets, the S3 site exhibits very narrow specificity. L-Lys is the most preferentially recognized residue at P3 among all tested amino acids. Other amino acids such as L-Orn, L-Arg, L-Arg(Z)2, L-hArg, L-Agp or L-Phe(guan) are recognized with significantly lower affinity. However, all these amino acids have basic side chains. The S4 site exhibits very broad substrate specificity. Almost all amino acids, including unnatural ones, are recognized at the same level at P4 position
-
-
?
additional information
?
-
-
analysis of substrate specificity at substrate positions P1, P2, P3, and P4, and cleavage site parameters, detailed overview. Enzyme cleavage sequence is Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is a natural or nonnatural amino acid). The P4-P1 optimal sequence is D-Arg-Lys-Orn-Arg. Most preferred amino acid residues at P1 are L-Arg(Me) and L-Arg. At P2, the NS2B-NS3 protease displays also a very high level of specificity. The most preferred amino acids are the non-proteinogenic L-Orn (100%) and L-Arg(Z)2 (40%). Natural amino acids interact significantly weaker with the S2 pocket, and only L-Lys and L-Arg are recognized (38% and 17%, respectively). Similarly to the S2 and S1 pockets, the S3 site exhibits very narrow specificity. L-Lys is the most preferentially recognized residue at P3 among all tested amino acids. Other amino acids such as L-Orn, L-Arg, L-Arg(Z)2, L-hArg, L-Agp or L-Phe(guan) are recognized with significantly lower affinity. However, all these amino acids have basic side chains. The S4 site exhibits very broad substrate specificity. Almost all amino acids, including unnatural ones, are recognized at the same level at P4 position
-
-
?
additional information
?
-
-
identification of 31 human proteins that are cleaved by the NS2B-NS3 protease. The cofactor NS2B is the principal determinant in ZVP substrate selection
-
-
?
additional information
?
-
no activity with human maltose binding protein
-
-
?
additional information
?
-
screening for potential intracellular substrates of NS3, substrate specificity analysis of recombinant enzyme NS2BLNNS3pr using synthesized FRET-type substrate libraries, peptide library preparation. Profiling of the P1-P4 substrate specificity of the NS2B-NS3 protease using a combinatorial chemistry approach and the split-and-mix method. Arg is the only preferred P1 residue of the enzyme, preference for Val at P4, and Lys at P3 and P2, no activity for Trp, Tyr, Asp, and Pro at P3 position, structure-function analysis, overview
-
-
?
additional information
?
-
-
screening for potential intracellular substrates of NS3, substrate specificity analysis of recombinant enzyme NS2BLNNS3pr using synthesized FRET-type substrate libraries, peptide library preparation. Profiling of the P1-P4 substrate specificity of the NS2B-NS3 protease using a combinatorial chemistry approach and the split-and-mix method. Arg is the only preferred P1 residue of the enzyme, preference for Val at P4, and Lys at P3 and P2, no activity for Trp, Tyr, Asp, and Pro at P3 position, structure-function analysis, overview
-
-
?
additional information
?
-
the enzyme performs self-cleavage processes viral polyproteins. Protease activity analysis of gZiPro, eZiPro and bZiPro
-
-
?
additional information
?
-
-
the enzyme performs self-cleavage processes viral polyproteins. Protease activity analysis of gZiPro, eZiPro and bZiPro
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Dengue virus DEN4 polyprotein + H2O
?
-
involved in processing of downstream nonstructural proteins of the Dengue virus DEN4 polyprotein precursor
-
-
?
eIF4G1 protein + H2O
?
-
human eukaryotic translation initiation factor 4 gamma 1, high activity
-
-
?
Flavivirus sp. polyproteins + H2O
?
-
involved in processing of downstream nonstructural proteins of the virus polyprotein
-
-
?
additional information
?
-
-
interaction of human brain proteins with the Japanese encephalitis virus NS2B-NS3 protease could be involved in the Japanese encephalitis virus induced pathogenesis
-
-
?
additional information
?
-
-
NS3 alone triggers the apoptotic pathways involving caspases-8 and -3. Activation of caspase-8 is essential to initiate apoptotic signaling in NS3-expressing cells
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B cofactor
-
The dengue virus NS2B-NS3 protease (NS2B-NS3p), an important antiviral target for drug development, has been reported to adopt an open or closed conformation in crystal structures with different NS2B C-terminus (NS2Bc) positioning. NS2Bc departs from NS3p in the open conformation, but it forms tight interactions with NS3p in the closed conformation
-
NS2B cofactor
the NS2B cofactor is covalently linked to the NS3 protease domain via a Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly (G4SG4) linker
-
NS2B cofactor
-
the unique cofactor region of zika virus NS2B-NS3 protease facilitates cleavage of key host proteins. The NS2B cofactor region from Zika virus protease is essential for recognition of host cell substrates. Replacing the NS2B region in another flavivirus protease enabled recognition of novel Zika-specific substrates by hybrid proteases, suggesting that the cofactor is the principal determinant in ZVP substrate selection
-
NS2B cofactor
-
the viral protease is a two-component serine protease formed by the N-terminal part of NS3 and the cofactor region of NS2B, a membrane protein essential for the membrane location of NS3. The NS2B mutant C143S cannot form the disulfide bond between C143 residues of neighboring NS3
-
NS2B protein
-
all cleavages of the flavivirus polyprotein mediated by the NS3 protease are believed to require cofactor activity of the NS2B protein
-
NS2B protein
the G(22) residue and the negatively charged patch D(32)DD(34) of NS2B are part of an important configuration required for NS2B-NS3pro activity
-
NS2B protein
-
tight complementarity of the protein sequences is necessary for NS2B-dependent activation of NS3. NS2B residues V88 and Q77 are critical for Alkhurma virus NS3 activation. Poor conservation of the NS2B cofactor sequence within members of the genus Flavivirus
-
additional information
-
characterization of structural determinants necessary for activation of the enzyme by the NS2B cofactor. Alanine substitutions at residues Trp62, Leu75, and Ile79 in the NS2B cofactor result in marked effects on autoprocessing at the NS2B/NS3 site. The activity of the mutant NS3 protease with the synthetic peptide substrate Gly-Arg-Arg-4-methylcoumarin 7-amide is mainly affected by significantly reduced kcat values
-
additional information
-
chimeric proteases with the NS2B cofactor from Langat virus and Dengue virus type 3 replacing the Alkhurma virus sequence activate NS3pro
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
kcat/Km values decrease by adding NaCl up to 100 mM. This results from the systematic increase in Km values with the increase in NaCl concentration in the range 1 to 10 mM
Zn2+
-
auto-cleavage and NS3 protease activity are zinc-dependent. NS2/3 auto-cleavage activity is more sensitive to zinc chelation by 1,10-phenanthroline than the NS3 protease activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1'R,2R,4'S,6S,8'R,10'E,12'S,14'E,16'E,21'R)-6-[(2S)-butan-2-yl]-12'-[[(2R,4S,5R,6R)-5-[[(2S,4S,5R,6S)-4,5-dihydroxy-6-methyltetrahydro-2H-pyran-2-yl]oxy]-4,6-dihydroxytetrahydro-2H-pyran-2-yl]oxy]-21',24'-dihydroxy-11',22'-dimethyl-3,4,5,6-tetrahydro-2'H-spiro[pyran-2,6'-[3,7,19]trioxatetracyclo[15.6.1.14,8.020,24]pentacosa[10,14,16,22]tetraen]-2'-one
-
-
(2aE,4E,5'S,6S,6'S,7S,8E,11R,13S,15S,17aS,20Z,20aR)-6'-cyclohexyl-20b-hydroxy-5',6,8,11,19-pentamethyl-20-(methylimino)-17-oxo-3',4',5',6,6',10,11,14,15,17,17a,20,20a,20b-tetradecahydro-2H,7H-spiro[11,15-methanofuro[4,3,2-pq][2,6]benzodioxacyclooctadecine
-
-
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
(3R,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
-
crystal structure analysis
(3R,7aS)-2-(4-nitrophenyl)-3-(4-(trifluoromethyl)-phenyl)-hexahydro-1H- pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition
(3R,7aS)-2-(4-nitrophenyl)-3-phenylhexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
67% inhibition
(3R,7aS)-3-(3-nitrophenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-chlorophenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition, crystal structure analysis
(3R,7aS)-3-(4-isopropylphenyl)-2-(4-nitrophenyl)-hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-methoxyphenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-nitrobenzyl)-2-(4-nitrophenyl)hexahydro-1Hpyrrolo[1,2-c]-imidaz-ol-1-one
-
below 50% inhibition
(3R,7aS)-3-benzyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
42% inhibition
(3R,7aS)-3-ethyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
60% inhibition
(3R,7aS)-3-isopropyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
34% inhibition
(3R,7aS)-3-methyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
42% inhibition
(3S,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
-
below 50% inhibition
(3S,7aS)-2-(4-nitrophenyl)-3-(4-(trifluoromethyl)-phenyl)hexahydro-1H- pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition
(3S,7aS)-3-(4-chlorophenyl)-2-(4-nitrophenyl)hexa-hydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(5-amino-1-phenylsulfonylpyrazol-3-yl) 2-bromobenzoate
-
100.8% inhibition at 0.05 mM
(5-amino-1-phenylsulfonylpyrazol-3-yl)thiophene-2-carboxylate
-
101.4% inhibition at 0.05 mM
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-cyanophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((4-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(S)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imida-zol-1-one
-
39% inhibition
(S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide
-
inhibitor-enzyme interaction analysis, crystal structure analysis of the complex, NMR spectrometry, overview
1,10-phenanthroline
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanol
-
-
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
-
-
1-(2-fluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
-
-
1-(3-[[2-(1H-benzimidazol-2-yl)hydrazinyl]methyl]-4-hydroxy-5-[(E)-[2-(3H-indol-2-yl)hydrazinylidene]methyl]phenyl)butane-1,2-dione
-
-
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
-
-
1-[(4-[2-[5-(4-fluorophenyl)-3-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4-yl]phenyl)sulfonyl]piperidine
-
-
1-[5-[(4-chloro-5-methyl-3-nitro-1H-pyrazol-1-yl)methyl]furan-2-yl]-2-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]ethanone
-
-
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
-
-
2-benzyl-N-[2-methyl-4-(4-methylpiperazin-1-yl)phenyl]-1,2,3,4-tetrahydrobenzo[b][1,6]naphthyridine-10-carboxamide
-
compound identified by a pharmacophore model based on X-ray crystal structure and predicted binding patterns. Compound shows good cell-based bioactivity
2-[(E)-[2-(3-bromophenyl)hydrazinylidene]methyl]-N'-[(1E)-2-phenylethylidene]quinoline-4-carbohydrazide
-
-
2-[1-(5-methyl-1,3,4-oxadiazol-2-yl)ethyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[[(4-methoxyphenyl)amino]methylidene]cyclohexane-1,3-dione
-
56% inhibition at 0.05 mM
3-[(8-benzoyl-1-methyl[1,2,4]triazolo[4,3-a]quinoxalin-4-yl)amino]benzoic acid
-
-
3-[[6-(3-fluorophenyl)pyridazin-3-yl]amino]-N-[2-(piperidin-1-yl)ethyl]benzamide
-
-
4-(aminomethyl)-Nalpha-benzoyl-N-[(1R)-4-carbamimidamido-1-(dihydroxyboranyl)butyl]-L-phenylalaninamide
cn-716, ZIKV protease in complex with a peptidomimetic boronic acid inhibitor reveals a cyclic diester between the boronic acid and glycerol, enzyme binding structure, binds to the active site, crystal structure analysis, detailed overview
4-guanidino-benzoic acid 4-nitrophenyl ester
-
the fold of Dengue NS2B-NS3pro in solution with and without bound inhibitor by nuclear magnetic resonance spectroscopy is analyzed. Multiple paramagnetic lanthanide tags are attached to different sites to generate pseudocontact shifts (PCS). The PCSs show, that in the presence of a positively charged low-molecular weight inhibitor, the enzyme assumes a closed state that is very similar to the closed state previously observed for the West Nile virus protease. To assess the open state, a binding site for a Gd3+ complex is created and paramagnetic relaxation enhancements is measured. The results show that the specific open conformation displayed in the crystal of DEN NS2B-NS3pro is barely populated in solution
4-hydroxypanduratin A
-
cyclohexenyl chalcone derivative, competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
4-methylumbelliferyl-alpha-D-mannopyranoside
-
i.e. compound 4282211 of ZINC database, identified by molecular docking. Inhibitor can efficiently bind to the NS2b/NS3 protease without changing the conformation of the protein, most active inhibitor identified, acitve against serotypes DENV1, DENV2, DENV3
4-[[3-(azepan-1-yl)-6-oxo-6H-anthra[1,9-cd][1,2]oxazol-5-yl]amino]butanoic acid
-
-
5,6-dichloro-2H-triazolo[4,5-b]pyrazine
NSC157058, the inhibitor decreases ZIKV infection in mice
5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate
-
the benzoyl moiety of the inhibitor forms a covalent bond with the side chain of S135. Structure and dynamics of bZiPro-inhibitor complex in solution
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,4-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,5,6-tetrafluoro-4-methylbenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,6-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,5-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,6-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,5-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-dichlorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluoro-3-methylbenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-fluoro-3-(trifluoromethyl)benzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 3-chlorothiophene-2-carboxylate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-3-carboxylate
-
-
5-methyl-2-[4-[(4-[[4-(4-methyl-4,5-dihydro-1H-imidazol-3-ium-2-yl)phenyl]amino]-4a,8a-dihydrophthalazin-1-yl)amino]phenyl]-4,5-dihydro-1H-imidazol-3-ium
-
-
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
-
-
5-[(E)-2-(2,6-difluorophenyl)ethenyl]-1-(4-methoxybenzyl)-3-methyl-1H-pyrazole
-
-
6-(4-chlorophenyl)-3-[[3-[[6-(4-chlorophenyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-3-yl]methoxy]phenoxy]methyl]-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
NSC716903
acetyl-K-agmatine
-
acetyl-K-agmatine is weakly bound by the ZIKV protease and does inhibit the enzyme. The Arg and Lys residues of acyl-KR-COOH occupy the S1 and S2 sites of the protease, respectively
benzoyl-Nle-KRR
homology model of the DV2 NS2B/NS3pro complexed with the peptidic inhibitor based on West nile virus structure
benzoyl-Nle-Lys-Arg-Arg-B(OH)2
-
dynamics of NS2B and NS3pro in the presence of the peptidic inhibitor
cardamonin
-
chalcone, non-competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-arginyl)
-
-
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl)
-
-
cyclo(L-alanylglycyl-L-alanyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-alanyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-alanyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-alanylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-L-phenylalanyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-alanyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-arginyl)
-
-
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl)
-
-
cyclo-[L-Pro-L-Phe-L-Leu-L-Lys-Gly-L-Val-L-Tyr-L-Glu-L-Asp-L-Phe-L-Phe-Gly]
-
-
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-N6-[CH2NH]-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-3-(2-naphthyl)-D-alanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
-
-
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-D-phenylalanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
-
-
cyclo[3-(2-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(2-naphthyl)-L-alanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl-L-arginyl-L-lysyl-L-seryl]
-
-
cyclo[D-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
-
-
cyclo[L-alany-(2R)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alany-(2S)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-(2R)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-(2S)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-D-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
-
-
cyclo[L-alanyl-L-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2R)-2-amino-4-phenylbutanoyl-L-cysteinyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-alanyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-cysteinyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-phenylglycyl-L-cysteinyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-L-prolyl-L-lysyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanylglycyl-L-lysyl]
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
completely inhibits autolysis of the NS2B-NS3pro construct
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate
-
12% inhibition
diphenyl (3-amino-1-[[(benzyloxy)carbonyl]amino]-3-oxopropyl)phosphonate
-
15% inhibition
diphenyl (3-amino-1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
12% inhibition
diphenyl ([4-(1H-benzimidazol-1-yl)phenyl][[(benzyloxy)carbonyl]amino]methyl)phosphonate
-
4% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(1H-pyrazol-1-yl)phenyl]methyl)phosphonate
-
5% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(4-methylpiperazin-1-yl)phenyl]methyl)phosphonate
-
3% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(morpholin-4-yl)phenyl]methyl)phosphonate
-
1% inhibition
diphenyl [(3-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
8% inhibition
diphenyl [(4-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
16% inhibition
diphenyl [1-[[(benzyloxy)carbonyl]amino]-3-(carbamimidoylsulfanyl)propyl]phosphonate
-
22% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](3-carbamimidamidophenyl)methyl]phosphonate
-
11% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](3-nitrophenyl)methyl]phosphonate
-
4% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidoylphenyl)methyl]phosphonate
-
22% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-cyanophenyl)methyl]phosphonate
-
8% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-nitrophenyl)methyl]phosphonate
-
3% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](6-carbamimidoylnaphthalen-2-yl)methyl]phosphonate
-
12% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](6-cyanonaphthalen-2-yl)methyl]phosphonate
-
2% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](carbamimidamido)methyl]phosphonate
-
-
EDTA
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
N'-(2-ethylhexyl)-N'-(6-[N'-[N-(3-methylheptan-2-yl)carbamimidoyl]carbamimidamido]hexyl)imidodicarbonimidic diamide (non-preferred name)
-
-
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
-
EC50 value 0.1 microM
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-3-[(4-nitrophenyl)sulfanyl]benzamide
-
EC50 value 0.3 microM
N-(9-ethylcarbazol-3-yl)-2-[(4-ethyl-5-furan-2-yl-1,2,4-triazol-3-yl)sulfanyl]acetamide
-
68.8% inhibition at 0.05 mM
N-benzyl-N,N-dimethyl-2-[2-[4-(2,2,3-trimethylpentan-3-yl)phenoxy]ethoxy]ethanaminium
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3R)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[4-(carbamimidamidomethyl)piperidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
-
-
N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide
-
-
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
-
C-terminal agmatine peptidomimetic inhibitor, competitive
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(trans-4-carbamimidamidocyclohexyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(2-carbamimidamidoethyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(3-carbamimidamidopropyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(5-carbamimidamidopentyl)-L-lysinamide
-
-
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
the compound inhibits both unlinked and linked protease with similar potency
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide
-
-
N2-[(3,4-dichlorophenyl)acetyl]-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
Na2SO4
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
NaOAc
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
nona-D-Arg-amide
-
completely inhibits autolysis of the NS2B-NS3pro construct
pinostrobin
-
flavanone, non-competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
Sodium citrate
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
[2-(2-cyanoethyl)-5-methylpyrazol-3-yl] benzoate
-
105.9% inhibition at 0.05 mM
[4-(2,3-dimethylphenyl)piperazin-1-yl]-(2-ethylsulfonyl-3,4-dihydro-1H-isoquinolin-3-yl)methanone
-
51.6% inhibition at 0.05 mM
[4-methyl-5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
[5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
107.7% inhibition at 0.05 mM
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
99.1% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] 2-bromobenzoate
-
112.5% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] benzoate
-
115.6% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
99.3% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
116.3% inhibition at 0.05 mM
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
96.6% inhibition at 0.05 mM
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
86.8% inhibition at 0.05 mM
[6-(4-methoxyphenyl)-4-methyl-5-(3-methylbut-2-en-1-yl)cyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
5.5% inhibition
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
-
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
10.8% inhibition
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
17.1% inhibition
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
-
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
-
Aprotinin
-
non-specific inhibitor of NS2B-NS3pro, full inhibition at 0.001 mM
Aprotinin
a 60-amino acid bovine pancreatic trypsin inhibitor and an efficient inhibitor of ZIKV NS2B-NS3pro
Bovine pancreatic trypsin inhibitor
pseudocontact shifts from a lanthanide tag show that NS2Bc remains in the closed conformation also in the complex with
-
diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate
-
-
diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate
-
11% inhibition
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
14.7% inhibition
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
-
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
31.1% inhibition
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
-
35.1% inhibition
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
-
26.3% inhibition
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
12.4% inhibition
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
32.3% inhibition
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
65.0% inhibition
NaCl
-
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
NaCl
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
-
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
panduratin A
-
cyclohexenyl chalcone derivative, competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
quercetin
-
molecular docking study. A total of six hydrogen bonds are formed, key residues are Asn152, Ala164, Lys74, Asn167, Leu149 and Gly87
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
cleavage products and their analogs do not appreciably inhibit the Dengue NS3 protease. Inhibitors with electrophilic warheads, such as aldehyde, trifluoromethyl ketone, and boronic acid, are needed to see effective inhibition of the enzyme activity. Among warheads, tetrapeptide boronic acid has the highest affinity
-
additional information
-
P2 Arg residue is more important for enzyme interactions than P1 Arg. Tri- and dipeptide aldehyde inhibitors afford low micromolar activity
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
inhibitor screening, a strong inhibitory potency is found for simple phenylacetyl-capped tripeptides containing a C-terminal P1 arginyl amide moiety and for their elongated derivatives with one or two glycine residues in the P1' and P2' positions. Inhibitory potencies of synthesized compounds, comparison to human furin, and West nile virus, structure-activity relationships, overview
-
additional information
-
unlinked NS2B-NS3 complex bound to a peptidic boronic acid inhibitor
-
additional information
-
in silico screening, alanine mutation, and density functional theory approaches for identification of NS2B/NS3 protease inhibitors, using molecular docking, free energy calculations, and simulation protocols in computational inhibitor screening, determination of ligand binding affinitites and protein interactions, overview
-
additional information
-
discovery of cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. The introduction of aromatic residues at the appropriate positions and conformational restriction generates the most promising cyclic peptide. Cyclic peptides with proper positioning of additional arginines and aromatic residues exhibit antiviral activity against DENV. Replacing the C-terminal amide bond of the polybasic amino acid sequence with an amino methylene moiety stabilizes the cyclic peptides against hydrolysis by NS2BNS3 protease, while maintaining their enzyme inhibitory activity and antiviral activity
-
additional information
-
identification of fused bicyclic derivatives of pyrrolidine and imidazolidinone as dengue virus-2 NS2B-NS3 protease inhibitors. The preliminary structure-activity relationship reveals that a substituent and its stereochemistry at C-3 position, substitution (X) at N-2 arene and a linker (Y) between C-3 position and its attached arene are important for the fused-ring scaffold of pyrrolidino [1,2-c]imidazolidinone to block the active site of NS2B-NS3 protease. The linear dipeptide L-methionyl-N-(4-nitrophenyl)-L-prolinamide) and the non-peptidic fused ring L-methionyl-N-(4-nitrophenyl)-L-prolinamide) show comparable activities against DENV-2 NS2B-NS3 protease and wild-type DENV-2 virus in a viral replication assay
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
structure-based identification of key residues and binding sites for inhibitor binding, design of non-competitive inhibitors for Dengue virus type 3 NS2b-NS3-protease, overview. The identified residues include 1. amino acids close to the beta sheet-loop-beta sheet known to be important in its closed conformation for NS2b 2. residues close to the active site, 3. several residues evenly spread on the NS2b-NS3 contact surface, and 4. some inner residues most likely related to the overall stability of the protease. Computational alanine scanning mutagenesis and similarity analysis based on sequence and structure homology, modeling. On the DENV NS3 protease, the residues Tyr23, Gly37, Phe46, Thr48, His51, Thr53, Leu58, Asp75, Tyr79, Trp89, and Thr156 are identified as class A and as the eleven highest ranked residues by both MLP models
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
EGTA or inhibitors of bacterial and mammalian metalloendopeptidases, aminopeptidase, angiotensin converting enzyme, and metalloprotease-disintegrins have no effect on NS2/3 auto-cleavage and NS3 protease activity. No inhibitory effect of the NS4A peptide on NS2/3 auto-cleavage. NS4A does not significantly affect the sensitivity of NS2/3 autocleavage to zinc chelation, but has a marked effect on NS3 protease activity, rendering this activity approximately 3fold more resistant to zinc chelation
-
additional information
enzyme ligand binding structure analysis
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
product inhibition of the protease by the cleaved C-terminus of NS2B. The reaction product Lys-Arg-COO- remains in the P2-P1 site after cleavage and effectively blocks the active site for both cis and trans substrates
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
inhibitor screening, a strong inhibitory potency is found for simple phenylacetyl-capped tripeptides containing a C-terminal P1 arginyl amide moiety and for their elongated derivatives with one or two glycine residues in the P1' and P2' positions. The compounds seem to be poor substrates of the WNV NS2BNS3 protease and therefore, act as competitive inhibitors. Inhibitory potencies of synthesized compounds, comparison to human furin, and West nile virus, structure-activity relationships, overview
-
additional information
-
development of a series of alpha-aminoalkylphosphonate diphenyl esters and their peptidyl derivatives as potent inhibitors of the NS2B/NS3 protease. Inhibitor synthesis and mechanism of serine proteases inhibition by alpha-aminoalkylphosphonate diphenyl esters involving the oxyanion hole, overview. Molecular docking
-
additional information
-
inhibitor potency is driven predominantely by interactions with amino acid residues in the S1 and S2 pockets, as substitutions in the P1 and P2 sites have the greates impact on inhibitor potency. P1 and P2 positions are most important for inhibitor binding, whilst the P3 and P4 positions have much less effect
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
identification of structural scaffolds for allosteric small-molecule inhibitors of this protease, overview. Molecular modeling of the protease-inhibitor complexes suggests that these compounds bind to the druggable cavity in the NS2B-NS3 protease interface and affect productive interactions of the protease domain with its cofactor. The most potent compound demonstrate efficient inhibition of ZIKV propagation in vitro in human fetal neural progenitor cells and in vivo in SJL mice. Docking study and in silico modeling of ZIKV NS2B-NS3pro complexed with inhibitors
-
additional information
-
identification of structural scaffolds for allosteric small-molecule inhibitors of this protease, overview. Molecular modeling of the protease-inhibitor complexes suggests that these compounds bind to the druggable cavity in the NS2B-NS3 protease interface and affect productive interactions of the protease domain with its cofactor. The most potent compound demonstrate efficient inhibition of ZIKV propagation in vitro in human fetal neural progenitor cells and in vivo in SJL mice. Docking study and in silico modeling of ZIKV NS2B-NS3pro complexed with inhibitors
-
additional information
screening for potential intracellular substrates of NS3 and development of specific inhibitors of ZIKV protease, overview
-
additional information
-
screening for potential intracellular substrates of NS3 and development of specific inhibitors of ZIKV protease, overview
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM) and in a mouse model of Zika virus infection. X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
structural dynamics of Zika virus NS2B-NS3 protease binding to dipeptide inhibitors, overview. The unlinked protease forms the closed conformation and the aldehyde group from the inhibitor forms a covalent bond with the side chain of S135. Compounds derived from protease substrate bind to the protease active site. Nuclear magnetic resonance studies demonstrate that the protease-inhibitor complex is in the closed conformation in solution. No inhibition by acyl-KR-COOH
-
additional information
-
structural insights into the inhibition of Zika virus NS2B-NS3 protease by a small-molecule inhibitor, structure and dynamics, overview. 5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate stabilizes the closed conformation of ZIKV protease. Upon hydrolysis in situ into two fragments, the benzoyl group of the inhibitor forms a covalent bond with the side chain of catalytic residue S135, whereas the second fragment exhibits no obvious molecular interactions with the protease, detailed mechanism of action of a covalent inhibitor. Unique adduct of the benzoyl moiety to residue S135
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
presence of basic residues at the P3 and P4 positions significantly promotes reactivity
-
additional information
-
auto-cleavage and NS3 protease activity show an absolute requirement for cysteine residues 1123, 1125 and 1171 within NS3, whereas cysteine 922 (within NS2) is only required for NS2/3 auto-cleavage activity and histidine 1175 is only required for NS3 activity. Complete NS3 protease domain (including the C-terminal alpha-helix) is required for NS2/3 auto-cleavage, whereas activity of the NS3 protease is not essential
-
additional information
-
formation of an active protease does not require neither cleavage of NS2B from NS3 nor a free NS3 N-terminus
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00418
Ac-Arg-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.006
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.0042
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.00799
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.01385
Ac-Nle-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
6
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.146
Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37°C, wild-type NS3 protease with wild-tyüe NS2B cofactor
0.111 - 0.444
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
0.298
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.354
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.0088
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.0177
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.026
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0021
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0039
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.03
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.027
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
8.6
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.0062
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.012
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.012
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
7.3
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.034
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.18
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.202
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
52
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.046
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.053
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.071
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
72
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.0066
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.011
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.013
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
8.6
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.076
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.22
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.36
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
210
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.143
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.707
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.004
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
mutant G22S
0.03
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
wild-type
0.0013
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme T52V, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.0588
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme K48A, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.071
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.089
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme R76L, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.111
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 7.4, 37°C, phosphate buffer
0.444
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 8.5, 37°C, Tris-CHAPS-glycerol buffer
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant A125C/V162C
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C/K117C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant I73C/P106C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117A
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant S75C/K117C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form wild-type enzyme
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117R
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant A125C/V162C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant I73C/P106C
0.07
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form wild-type enzyme
0.08
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant K117A
0.6
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
deltaNS2B-NS3pro
2.6
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
chimeric proteases with the NS2B cofactor from Langat virus replacing the Alkhurma virus sequence
15.9
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant Q77A
0.0087
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0073
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.02
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0066
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0076
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0006
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.002
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.00013
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.014
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0015
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0096
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0138
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.004
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
mutant G22S
0.03
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
wild-type
0.059
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
mutant K48A
0.036
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
mutant K48A
0.324
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.415
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.465
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.505
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
2.18
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
2.7
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.181
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.53
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.563
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
1.249
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
3.74
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.12
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.125
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.15
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
180
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
additional information
additional information
kinetics of cysteine-substituted mutant variants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.43
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
4.64
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
7.99
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
2.9
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
300
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.02
Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37°C, wild-type NS3 protease with wild-tyüe NS2B cofactor
25.94 - 343.73
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
0.172
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.022
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.03
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.02
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.04
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.025
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.04
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.17
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.04
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.32
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.61
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
1.4
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
2.8
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.97
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
1.1
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
1.4
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
4.9
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.28
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.58
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.76
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
1.1
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.05
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.1
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.2
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.43
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.17
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.21
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.33
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.48
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.013
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme T52V, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
5.25
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme K48A, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
6.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
7.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme R76L, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
25.94
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 7.4, 37°C, phosphate buffer
343.73
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 8.5, 37°C, Tris-CHAPS-glycerol buffer
0.006
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117A
0.01
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant A125C/V162C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant A125C/V162C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C/K117C
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant I73C/P106C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117R
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form wild-type enzyme
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant K117A
0.07
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant S75C/K117C
0.08
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant I73C/P106C
0.09
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form wild-type enzyme
0.0004
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88D
0.0006
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88K
0.0018
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G81A
0.0018
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant W60A
0.0051
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
chimeric proteases with the NS2B cofactor from Langat virus replacing the Alkhurma virus sequence
0.0058
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G68A
0.008
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant Q77A
0.0089
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant L73A
0.015
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
deltaNS2B-NS3pro
0.001
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.01
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.061
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.004
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.097
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.012
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.026
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.002
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.06
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.12
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.29
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.007
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.044
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.073
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.075
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.101
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.163
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.006
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.007
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.039
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.083
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.153
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.03
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.07
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.09
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.13
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
258.37
Ac-Arg-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
905
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
1104.76
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
1000
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
317.69
Ac-Nle-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
235 - 7760
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
0.11
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1.37
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
3.04
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.6
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
12.8
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
20
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
13
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
18.16
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
4.08
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
3.33
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
12.5
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
11.9
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
82
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme R76L, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
88
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
89.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme K48A, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
100
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme T52V, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
235
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 7.4, 37°C, phosphate buffer
7760
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 8.5, 37°C, Tris-CHAPS-glycerol buffer
0.44
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form wild-type enzyme
0.57
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant S75C/K117C
0.625
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant I73C/P106C
0.71
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form wild-type enzyme
0.8
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C
1.25
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117R
1.33
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant I73C/P106C
1.5
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant A125C/V162C
1.5
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C/K117C
1.6
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant K117A
2.5
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117C
5
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant A125C/V162C
6.67
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0442 - 5.5
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
0.0136 - 10.8
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
0.0216
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
0.0853 - 17.1
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
0.0034
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
-
serotype 4, pH 7.5, 37°C
0.0049
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
serotype 4, pH 7.5, 37°C
0.004
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
-
serotype 4, pH 7.5, 37°C
0.000264
antibody D05320
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.0004
antibody D05321
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.00017
antibody D05322
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000031
antibody D05323
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000058
antibody D05444
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000035
antibody D05445
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000288
antibody D05446
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.0013
Bz-Nle-(3-amino)-Phe-(3-imino)-Phe-(3,4-dimethoxy)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-(3-guanidino)-Phe-(4-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0002
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-(4-amino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.002
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0017
Bz-Nle-(4-amino)-Phe-(3-imino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-(4-amino)-Phe-(4-guanidino)-Phe-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0015
Bz-Nle-Arg-(3-guanidino)-Phe-(4-amino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0001
Bz-Nle-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0008
Bz-Nle-His-(3-guanidino)-Phe-beta-(2-naphthyl)-Ala
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0017
Bz-Nle-His-(3-imino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-His-(4-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0009
Bz-Nle-His-(4-guanidino)-Phe-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0005
Bz-Nle-homo-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0019
Bz-Nle-homoHis-(3-guanidino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0014
Bz-Nle-homoHis-(4-guanidino)-Phe-(4-phenyl)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0016
Bz-Nle-Lys-Arg-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.013
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
pH 8.5, 37°C
0.022
diphenyl (5-amino-1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
pH 8.5, 37°C
0.01
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
pH 8.5, 37°C
0.004
diphenyl [[[(benzyloxy)carbonyl]amino](carbamimidamido)methyl]phosphonate
-
pH 8.5, 37°C
0.0182 - 14.7
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
0.0994
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0756
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.134
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0289
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
pH 8.5, 22°C
0.0298
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.0296 - 31.1
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
0.044
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.000039
N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
-
pH 8.5, 37°C
0.00075
N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide
-
pH 8.5, 37°C
0.0025
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
-
pH 8.0, 25°C
0.000006
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-Lys-L-Arg-aldehyde
-
pH 8.5, 37°C
0.00156
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
-
pH 8.5, 22°C
0.015
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
-
pH 8.5, 22°C
0.017
N2-(phenylacetyl)-L-lysyl-N-(5-amino-5-oxopentyl)-L-lysinamide
-
pH 8.5, 22°C
0.0012
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.0222
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.00471 - 12.4
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
0.00013
N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide
-
pH 8.5, 37°C
0.00011
N2-[(3,4-dichlorophenyl)acetyl]-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.0018
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysylglycinamide
-
pH 8.5, 22°C
0.00036
N2-[[3-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00018
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00038
N2-[[4-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00645 - 0.0831
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00065 - 0.0116
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00082 - 0.00122
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.0057 - 0.0773
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00011
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.01984
[4-methyl-5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
0.02436
[5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
0.03968
[6-(4-methoxyphenyl)-4-methyl-5-(3-methylbut-2-en-1-yl)cyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
0.0442
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
5.5
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
0.0136
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
10.8
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
0.0853
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
17.1
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
0.0111
agathisflavone
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0153
agathisflavone
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.00002
Aprotinin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.0047
myricetin
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0257
myricetin
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0182
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
14.7
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0296
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
31.1
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.00471
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
12.4
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.00645
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0831
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00065
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0116
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00082
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00122
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0057
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0773
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0199
quercetin
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0227
quercetin
-
serovar DENV2, pH 9.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
(3R,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0036
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
Dengue virus
-
pH 8.5, 37°C
0.0022
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((4-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
Dengue virus
-
pH 8.5, 37°C
0.000208
(S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide
Zika virus
-
pH and temperature not specified in the publication
0.1
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanol
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0239
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0388
1-(2-fluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00926
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00871
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00403
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl benzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00943
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00804
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.000019
2,6-difluoro-benzoyl-Nle-Lys-Arg-Arg-CF3-ketone
Dengue virus
-
pH 7.4, temperature not specified in the publication, versus the linked NS2B-NS3 complex
0.0039
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.1
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanol
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanone
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0125
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.0015
5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate
Zika virus
-
20xa0mM Tris pH 8.5, 10% glycerol, 0.01% Triton X-100, 37°C
0.01192
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,4-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.01069
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,5,6-tetrafluoro-4-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00097
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,6-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.02618
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,5-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00183
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,6-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00196
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0049
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,5-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-dichlorobenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00428
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00031
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-ethoxybenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.04549
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-fluoro-3-(trifluoromethyl)benzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00355
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-nitrobenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00122
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 3-chlorothiophene-2-carboxylate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.005
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-3-carboxylate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0156
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.0138
5-[(E)-2-(2,6-difluorophenyl)ethenyl]-1-(4-methoxybenzyl)-3-methyl-1H-pyrazole
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.000038
benzoyl-Nle-Lys-Arg-Arg-B(OH)2
Dengue virus
-
pH 7.4, temperature not specified in the publication, versus the linked NS2B-NS3 complex
0.0023
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-arginyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0037
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-alanyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-alanyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-alanyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-alanylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0393
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-L-phenylalanyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0574
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-alanyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.114
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0038
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-arginyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0038
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0017
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0016
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0021
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-N6-[CH2NH]-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0011
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-3-(2-naphthyl)-D-alanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0017
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-D-phenylalanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0015
cyclo[3-(2-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0026
cyclo[3-(2-naphthyl)-L-alanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl-L-arginyl-L-lysyl-L-seryl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0033
cyclo[D-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0151
cyclo[L-alany-(2R)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0222
cyclo[L-alany-(2S)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0162
cyclo[L-alanyl-(2R)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0256
cyclo[L-alanyl-(2S)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0076
cyclo[L-alanyl-D-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0285
cyclo[L-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0198
cyclo[L-alanyl-L-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0387
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2R)-2-amino-4-phenylbutanoyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0184
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-alanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0092
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0221
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-phenylglycyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00095
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.052
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-L-prolyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.005
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanylglycyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0012
L-methionyl-N-(4-nitrophenyl)-L-prolinamide
Dengue virus type 2
-
pH and temperature not specified in the publication
0.021 - 0.022
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
0.026
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-3-[(4-nitrophenyl)sulfanyl]benzamide
Dengue virus
-
protease of serotype DENV-2, pH not specified in the publication, temperature not specified in the publication
0.04771
N-(9-ethylcarbazol-3-yl)-2-[(4-ethyl-5-furan-2-yl-1,2,4-triazol-3-yl)sulfanyl]acetamide
West Nile virus
-
-
0.1
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3R)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C, value above
0.02
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C
0.1
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[4-(carbamimidamidomethyl)piperidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C, value above
0.0049
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0047
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.1
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(trans-4-carbamimidamidocyclohexyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.0612
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(2-carbamimidamidoethyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(3-carbamimidamidopropyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(5-carbamimidamidopentyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.00104 - 0.00106
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
0.0182
N2-acetyl-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.001353
SID-3717586
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00011
SID-4245669
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.000105
SID-852843
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.03857
[4-(2,3-dimethylphenyl)piperazin-1-yl]-(2-ethylsulfonyl-3,4-dihydro-1H-isoquinolin-3-yl)methanone
West Nile virus
-
-
0.001161
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.001651
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl]furan-2-carboxylate
West Nile virus
-
-
0.000297
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] 2-bromobenzoate
West Nile virus
-
-
0.000553
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
West Nile virus
-
-
0.00011
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.01439
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
West Nile virus
-
-
0.002405
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.0151
agathisflavone
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0175
agathisflavone
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0223
myricetin
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0293
myricetin
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.021
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
Dengue virus
-
protease of serotype DENV-3, pH not specified in the publication, temperature not specified in the publication
0.022
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
Dengue virus
-
protease of serotype DENV-2, pH not specified in the publication, temperature not specified in the publication
0.00104
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
Zika virus
recombinant linked protease, pH 8.5, 37°C
0.00106
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
Zika virus
recombinant unlinked protease, pH 8.5, 37°C
0.0227
quercetin
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0352
quercetin
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10.5
7 - 10.5
-
at pH 9.0 the enzyme is 5times more active than at pH 7.0, and more than 3times more active than at pH 10.5
7 - 10.5
at pH 9.0 the enzyme is 5times more active than at pH 7.0, and more than 3times more active than at pH 10.5
7 - 10.5
is less sensitive to pH variations compared to other flaviviruses, with a reduction in the enzymatic activity lower than 50% at pH 7.0 and 10.5 compared to the maximum activity at pH 9.0
7 - 10.5
-
at pH 9.0 the enzyme is 5times more active than at pH 7.0, and more than 3times more active than at pH 10.5
7 - 10.5
-
at pH 9.0 the enzyme is 5times more active than at pH 7.0, and more than 3times more active than at pH 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Dengue virus type 2 Thailand/16681/1984
Zika virus Puerto Rico isolate
genome polyprotein; ZIKV, the ZIKV isolate is from Puerto Rico, which stems from the Asian lineage and is relevant to the 2015-2016 outbreak in North and South America
UniProt
brenda
-
81434, 81436, 663540, 667404, 681687, 691252, 691254, 717102, 717682, 717880, 731146, 731236, 731284, 731486, 731644, 732547, 732872
-
-
brenda
-
-
-
brenda
genome polyprotein; ZIKV, the ZIKV isolate is from Puerto Rico, which stems from the Asian lineage and is relevant to the 2015-2016 outbreak in North and South America
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
cytoplasmic localization with membrane association
-
brenda
additional information
-
NS2B is membrane component of viral replication process, presumably responsible for membrane localization of NS3
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
Dengue virus type 2 Thailand/16681/1984
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
dengue virus type I Nauru/West Pac/1974
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
-
cytoplasmic localization with membrane association
-
brenda
additional information
-
viral enzyme acting in cytoplasma of host cell
-
brenda
additional information
-
NS2B is membrane component of viral replication process, presumably responsible for membrane localization of NS3
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
Murray Valley encephalitis virus MVE-1-51
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
-
cytoplasmic localization with membrane association
-
brenda
additional information
-
viral enzyme acting in cytoplasma of host cell
-
brenda
additional information
-
viral enzyme acting in cytoplasma of host cell
-
brenda
additional information
-
NS2B is membrane component of viral replication process, presumably responsible for membrane localization of NS3
-
brenda
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
brenda
additional information
Yellow fever virus 17D vaccine
-
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
comparative analysis of the substrate specificity reveals that ZIKV NS3 protease follows the typical pattern for flaviviruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
physiological function
-
autophagy-related protein 16-1 (ATG16L1) and eukaryotic translation initiation factor 4 gamma 1 (eIF4G1) are dramatically depleted during Zika virus infection. ATG16L1 and eIF4G1 mediate type-II interferon production and host-cell translation, respectively, likely aiding immune system evasion and driving the Zika life cycle
physiological function
enzyme NS2B-NS3pro has a critical role in polyprotein maturation and viral infectivity
physiological function
NS2B-NS3 protease consists of the NS2B cofactor and the NS3 protease domain and is essential for cleavage of the ZIKV polyprotein precursor and generation of fully functional viral proteins. Cell toxicity assays. The enzyme cleaves human Sox2 protein, which plays a critical role in neural stem cells by maintaining the activity of multiple genes involved in self-renewal and by priming the epigenetic landscape for the onset of neuronal differentiation. Sox2 is cleaved by ZIKV NS2B-NS3pro only at a very high enzyme/substrate ratio Sox2 insufficiency results in a plethora of developmental neuronal malformations in the human brain
physiological function
-
the complex of NS2B and NS3 (NS2B/NS3) in the serine protease enzyme is essential for viral replication
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the NS2B-NS3 protease is essential for the dengue virus (DENV) replication process
physiological function
-
the two-component viral protease NS2B-NS3 is required for the production of mature viruses and plays a key role in maintaining infectivity
physiological function
the viral protease that processes viral polyproteins
physiological function
the virus possesses a two-component (NS2B/NS3) serine protease that cleaves the viral precursor proteins
physiological function
the Zika virus (ZIKV) relies on its NS2B/NS3 protease for polyprotein processing
physiological function
the ZIKV NS2B/NS3 protease is responsible for cleavage of the viral polyprotein at five sites
physiological function
-
viral NS2B-NS3 protease processes viral polyprotein and is essential for the virus replication
physiological function
ZIKV expresses the serine protease NS3 which is responsible for viral protein processing and replication
physiological function
Dengue virus type 2 Thailand/16681/1984
-
enzyme NS2B-NS3pro has a critical role in polyprotein maturation and viral infectivity
-
physiological function
Dengue virus type 2 Thailand/16681/1984
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
Yellow fever virus 17D vaccine
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the NS2B-NS3 protease is essential for the dengue virus (DENV) replication process
-
physiological function
Zika virus Puerto Rico isolate
-
the ZIKV NS2B/NS3 protease is responsible for cleavage of the viral polyprotein at five sites
-
physiological function
dengue virus type I Nauru/West Pac/1974
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the virus possesses a two-component (NS2B/NS3) serine protease that cleaves the viral precursor proteins
-
physiological function
Zika virus Brazilian isolate BeH823339
-
the Zika virus (ZIKV) relies on its NS2B/NS3 protease for polyprotein processing
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
Murray Valley encephalitis virus MVE-1-51
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
additional information
-
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
additional information
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition, overview. Although all substrates are in the active conformation for cleavage reaction by NS2B/NS3 protease, their binding strength is different. The simulated results of intermolecular hydrogen bonds and decomposition energies suggest that among the ten substrate residues (P5-P5') the P1 and P2 subsites play a major role in the binding with the focused protease. The arginine residue at these two subsites shows preferential binding at the active site. Besides, the P3, P1', P2' and P4' subsites show a less contribution in binding interaction. The catalytic water is detected nearby the carbonyl oxygen of the P1 reacting center of the capsid, intNS3, 2A/2B and 4B/5 peptides. The order of absolute binding free energy between these substrates and the NS2B/NS3 protease is capsid, intNS3, 2A/2B, 4B/5, 3/4A, 2B/3 in descending order in a relative correspondence with previous experimentally derived values. Hydrogen bond patterns of substrate binding
additional information
-
solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation
additional information
structure of the NS2B-NS3 protease from Zika virus after self-cleavage. Analysis of the post-proteolysis state structure of the enzyme during viral polyprotein processing providing insights into peptide substrate recognition by the protease, Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
structure of the NS2B-NS3 protease from Zika virus after self-cleavage. Analysis of the post-proteolysis state structure of the enzyme during viral polyprotein processing providing insights into peptide substrate recognition by the protease, Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
structure-function studies of ZIKV NS2B-NS3 protease
additional information
-
the enzyme is a complex of NS2B cofactor and NS3 protein. It adopts an open or closed conformation in crystal structures with different NS2B C-terminus (NS2Bc) positioning. In solution, NS2B-NS3p forms a mixture of open, closed and maybe other intermediate conformations. Analysis of the conformational changes using 19F NMR spectroscopy and enzyme mutant H51A/S75C. Low pH or bovine pancreatic trypsin inhibitor (BPTI) binding promote the conformation change from open to closed, showing the importance of charge forces in the interaction between NS2Bc and NS3p. NS3p residue His51 plays a crucial role in the pH-dependent conformational exchange by charge interacting with NS2Bc
additional information
the protease is a two-component system such that a portion of NS2B in addition to the protease portion of NS3 is also required for proteolytic activity. The enzymatic activity appears to be dependent on the movement of NS2B and may rely on the flexibility of the protease core. Locking the enzyme into the closed conformation dramatically increases the activity, strongly suggesting that the closed conformation is the active conformation. The observed resting state of the enzyme depends largely on the construct used to express the NS2B-NS3pro complex. In an unlinked construct, in which the NS2B and NS3 regions exist as independent, co-expressed polypeptides, the enzyme rests predominantly in a closed, active conformation. In contrast, in a linked construct, in which NS2B and NS3 are attached by a nine-amino acid linker, NS2B-NS3pro adopts a more relaxed, alternative conformation. Nevertheless, even the unlinked construct samples both the closed and other alternative conformations. 4-(2-Aminoethyl)benzenesulfonyl fluoride (AEBSF) induction of the closed conformation. Structure-function analysis, overview
additional information
-
the unique cofactor region of zika virus NS2B-NS3 protease facilitates cleavage of key host proteins
additional information
-
the unlinked NS2B-NS3 protease adopts a closed conformation in which NS2B engages NS3 to form an empty substrate-binding site
additional information
-
the viral protease is a two-component serine protease formed by the N-terminal part of NS3 and the cofactor region of NS2B, a membrane protein essential for the membrane location of NS3
additional information
-
the viral protease is a two-component serine protease formed by the N-terminal part of NS3 and the cofactor region of NS2B, a membrane protein essential for the membrane location of NS3
additional information
Dengue virus type 2 Thailand/16681/1984
-
the protease is a two-component system such that a portion of NS2B in addition to the protease portion of NS3 is also required for proteolytic activity. The enzymatic activity appears to be dependent on the movement of NS2B and may rely on the flexibility of the protease core. Locking the enzyme into the closed conformation dramatically increases the activity, strongly suggesting that the closed conformation is the active conformation. The observed resting state of the enzyme depends largely on the construct used to express the NS2B-NS3pro complex. In an unlinked construct, in which the NS2B and NS3 regions exist as independent, co-expressed polypeptides, the enzyme rests predominantly in a closed, active conformation. In contrast, in a linked construct, in which NS2B and NS3 are attached by a nine-amino acid linker, NS2B-NS3pro adopts a more relaxed, alternative conformation. Nevertheless, even the unlinked construct samples both the closed and other alternative conformations. 4-(2-Aminoethyl)benzenesulfonyl fluoride (AEBSF) induction of the closed conformation. Structure-function analysis, overview
-
additional information
Dengue virus type 2 Thailand/16681/1984
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
Yellow fever virus 17D vaccine
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
Zika virus Puerto Rico isolate
-
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
-
additional information
dengue virus type I Nauru/West Pac/1974
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition, overview. Although all substrates are in the active conformation for cleavage reaction by NS2B/NS3 protease, their binding strength is different. The simulated results of intermolecular hydrogen bonds and decomposition energies suggest that among the ten substrate residues (P5-P5') the P1 and P2 subsites play a major role in the binding with the focused protease. The arginine residue at these two subsites shows preferential binding at the active site. Besides, the P3, P1', P2' and P4' subsites show a less contribution in binding interaction. The catalytic water is detected nearby the carbonyl oxygen of the P1 reacting center of the capsid, intNS3, 2A/2B and 4B/5 peptides. The order of absolute binding free energy between these substrates and the NS2B/NS3 protease is capsid, intNS3, 2A/2B, 4B/5, 3/4A, 2B/3 in descending order in a relative correspondence with previous experimentally derived values. Hydrogen bond patterns of substrate binding
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
Murray Valley encephalitis virus MVE-1-51
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). POLG_KOKV
3410
16
378066
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_KUNJM
3433
18
381369
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_LANVT
3414
19
378023
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_LIV
3414
15
378412
Swiss-Prot
other Location (Reliability: 5)
POLG_MCFA
3341
15
373267
Swiss-Prot
other Location (Reliability: 2)
POLG_MVEV5
3434
18
380577
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_OHFV
3414
17
378686
Swiss-Prot
other Location (Reliability: 4)
POLG_ALKV
3416
17
378122
Swiss-Prot
other Location (Reliability: 3)
POLG_BANV
3393
18
375607
Swiss-Prot
other Location (Reliability: 5)
POLG_BUSV
3429
14
379101
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_DEN4D
3387
11
378385
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN4H
Dengue virus type 4 (strain Thailand/0476/1997)
3387
13
378577
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN4P
Dengue virus type 4 (strain Philippines/H241/1956)
3387
13
378408
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN4S
Dengue virus type 4 (strain Singapore/8976/1995)
3387
11
378484
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN4T
Dengue virus type 4 (strain Thailand/0348/1991)
3387
13
378438
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_EHV
3401
19
377294
Swiss-Prot
other Location (Reliability: 3)
POLG_ROCV
3425
20
380351
Swiss-Prot
other Location (Reliability: 5)
POLG_STEVM
3412
18
378483
Swiss-Prot
other Location (Reliability: 5)
POLG_ILHV
3424
21
379057
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_JAEV1
3432
18
380211
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_JAEV5
3432
18
380182
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_JAEVJ
3432
16
380166
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_JAEVM
3432
18
380083
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_JAEVN
1440
12
158185
Swiss-Prot
other Location (Reliability: 4)
POLG_KFDV
3416
17
377417
Swiss-Prot
other Location (Reliability: 3)
POLG_DEN1S
Dengue virus type 1 (strain Singapore/S275/1990)
3391
13
379086
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_DEN1W
Dengue virus type 1 (strain Nauru/West Pac/1974)
3392
7
378702
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN26
Dengue virus type 2 (strain Thailand/16681/1984)
3391
11
379547
Swiss-Prot
other Location (Reliability: 5)
POLG_DEN27
3391
11
379884
Swiss-Prot
other Location (Reliability: 4)
POLG_DEN28
3391
11
379394
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN2J
Dengue virus type 2 (strain Jamaica/1409/1983)
3391
11
379250
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_DEN2N
Dengue virus type 2 (strain Thailand/NGS-C/1944)
3391
11
379501
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN2P
Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)
3388
11
379219
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN2Q
Dengue virus type 2 (strain Peru/IQT2913/1996)
3391
11
379787
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_DEN2T
Dengue virus type 2 (strain Tonga/EKB194/1974)
1683
4
187440
Swiss-Prot
other Location (Reliability: 2)
POLG_DEN3C
Dengue virus type 3 (strain China/80-2/1980)
3390
13
378159
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN3I
Dengue virus type 3 (strain Singapore/8120/1995)
3390
13
377970
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN3M
Dengue virus type 3 (strain Martinique/1243/1999)
3390
13
377956
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN3P
3390
13
378063
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_DEN3S
Dengue virus type 3 (strain Sri Lanka/1266/2000)
3390
13
377923
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_YEFV1
Yellow fever virus (strain 17D vaccine)
3411
21
379518
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVA
Yellow fever virus (strain Ghana/Asibi/1927)
3411
21
379169
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVC
Yellow fever virus (isolate Ivory Coast/1999)
3411
21
378956
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVE
Yellow fever virus (isolate Ethiopia/Couma/1961)
3412
19
378659
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVF
Yellow fever virus (strain French neurotropic vaccine FNV)
3411
19
379189
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVI
Yellow fever virus (isolate Ivory Coast/85-82H/1982)
3411
19
379172
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVN
Yellow fever virus (isolate Angola/14FA/1971)
3412
17
378939
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVT
Yellow fever virus (strain Trinidad/TRINID79A/1979)
3411
19
379223
Swiss-Prot
other Location (Reliability: 4)
POLG_YEFVU
Yellow fever virus (isolate Uganda/A7094A4/1948)
3412
19
378817
Swiss-Prot
other Location (Reliability: 4)
POLG_ZIKV
3419
21
378736
Swiss-Prot
other Location (Reliability: 5)
POLG_ZIKVF
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013)
3423
18
379113
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_ZIKVK
3423
18
379109
Swiss-Prot
Mitochondrion (Reliability: 3)
POLG_DEN1B
Dengue virus type 1 (strain Brazil/97-11/1997)
3392
9
378905
Swiss-Prot
Mitochondrion (Reliability: 4)
POLG_TBEVH
3414
15
378545
Swiss-Prot
other Location (Reliability: 5)
POLG_TBEVS
Tick-borne encephalitis virus Far Eastern subtype (strain Sofjin)
3412
17
377981
Swiss-Prot
other Location (Reliability: 4)
POLG_TBEVW
Tick-borne encephalitis virus European subtype (strain Neudoerfl)
3414
17
378322
Swiss-Prot
other Location (Reliability: 5)
POLG_USUV
3434
16
380313
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_WNV
3430
20
380110
Swiss-Prot
other Location (Reliability: 5)
POLG_WNV9
3433
22
381176
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_WSLV
3405
13
378677
Swiss-Prot
Mitochondrion (Reliability: 5)
POLG_POWVL
3415
19
378570
Swiss-Prot
other Location (Reliability: 4)
D0EPS0_9FLAV
3391
0
379773
TrEMBL
other Location (Reliability: 2)
Q5I3B6_9FLAV
3383
0
378345
TrEMBL
other Location (Reliability: 3)
Q9II02_9FLAV
3392
0
379069
TrEMBL
Mitochondrion (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
1 * 21000 plus 1 * 10000, SDS-PAGE, corresponding to the NS3pro protease domain only, and the His-tagged NS2B(H) cofactor
21000
-
1 * 21000 plus 1 * 10000, SDS-PAGE, corresponding to the NS3pro protease domain only, and the His-tagged NS2B(H) cofactor
30000
-
truncated form resulting from a proteolytic cleavage near the C-terminus of the protein, immunoprecipitation
74000
-
1 * 74000, SAXS experiments with the complete NS3 molecule fused to 18 residues of the NS2B cofactor
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
-
the biologically active viral protease of NS2B/NS3 complex is termed as heterodimeric
monomer
-
1 * 74000, SAXS experiments with the complete NS3 molecule fused to 18 residues of the NS2B cofactor
additional information
dimer
-
heterodimer of NS3 and NS2B, i.e. serine protease and viral activator protein resp.
dimer
-
1 * 21000 plus 1 * 10000, SDS-PAGE, corresponding to the NS3pro protease domain only, and the His-tagged NS2B(H) cofactor
dimer
-
Zika protease is able to form a dimer, and a disulfide bond between C143 residues of neighboring NS3 in the crystal is observed
additional information
tagging of subunit NS3pro with paramagnetic tags and measurement of pseudocontact shifts by NMR to position NS2B cofactor relative to NS3pro. NS2B-NS3 protease in solution predominantly assumes the closed conformation in the absence of inhibitors and any open conformation is hardly populated
additional information
-
tagging of subunit NS3pro with paramagnetic tags and measurement of pseudocontact shifts by NMR to position NS2B cofactor relative to NS3pro. NS2B-NS3 protease in solution predominantly assumes the closed conformation in the absence of inhibitors and any open conformation is hardly populated
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
structure of the NS2B-NS3 protease from Zika virus after self-cleavage
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking of compound 22 shows hydrophobic interactions with Trp50, His51, Arg54, Arg73, Asn74, Asp75, Asn152, and Gly153. The O2 atom of pyrimidine group of compound 22 has two H-bonds, one with the hydroxyl group of Ser135 at 2.76 A and the other with amine group of Asn152 at 2.84 A
-
molecular docking study using flavonoids rom Carica papaya. Highest binding energy is sen with quercetin
-
pseudocontact shifts from a lanthanide tag show that NS2Bc remains in the closed conformation also in the complex with bovine pancreatic trypsin inhibitor. The closed conformation is the best template for drug discovery
purified recombinant linked NS2B-NS3pro, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
analysis of enzyme structures, PDB IDs 2FOM, 2M9P, 2M9Q, 2BHR, and 2BMF
analysis of enzyme structures, PDB IDs 2JLQ, 2JLR, 2JLU, 2JLV, 2JLW, 2JLX, 2JLY, 2JLZ, 2WHX, 2WZQ, and 2VBC
complete NS3 molecule fused to 18 residues of the NS2B cofactor, by hanging-drop vapor diffusion method, at 3.15 A resolution. Protease domain sits beneath the ATP binding site, giving the molecule an elongated shape. Domain arrangement in the crystal structure fits into an envelope, suggesting a stable molecular conformation. A basic patch located at the surface of the protease domain increases the affinity for nucleotides and may also participate in RNA binding, explaining the higher unwinding activity of the full-length enzyme compared to that of the isolated helicase domain
-
the identification of an alternative stable conformation for the full-length NS2B18NS3 protein is reported. In this second conformation refined to a resolution of 2.2 A, the protease domain has rotated by an angle of 161° relative to the helicase domain
by hanging-drop vapour diffusion at 4°C, at 2.3 A resolution. Crystal structure of the catalytic domain of NS2-3 protease, using native and selenomethionine-containing protein yields two crystal forms with the same space group P21. Dimeric cysteine protease with two composite active sites. For each active site, the catalytic histidine and glutamate residues are contributed by one monomer, and the nucleophilic cysteine by the other. Carboxy-terminal residues remain coordinated in the two active sites, predicting an inactive post-cleavage form
-
analysis of enzyme structures, PDB IDs 2YOL, 3E90, 2FP7, 2IJO, and 2GGV
NS2B-NS3 complex complexed with benzoyl-Nle-Lys-Thr-Arg-H, and trypsin digested NS2B-NS3 complex
-
purified bZiPro (C143S)-inhibitor 5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate complex and bZiPro (C143S)-Ac-Lys-Arg complex, X-ray diffraction structure determination and analysis at 1.90 A and 1.51 A resolution, respectively
-
purified enzyme complex with bound inhibitor (S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
purified free NS2B-NS3 protease and complexed with a peptide reversely oriented at the active site, X-ray diffraction structure determination and analysis at 1.58 A resolution. A second protease in the same crystal binds to the residues K14K15G16E17 from the neighboring NS3 in reverse orientation, resisting proteolysis
-
purified NS2B-NS3 protease complexed with the last four amino acids of the NS2B cofactor bound at the NS3 active site, sitting drop vapour diffusion method, mixing of 0.001 ml of 40 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.2 M Na-malonate, pH 4.0, 10% PEG 3350, 18°C, two days, X-ray diffraction structure determination and analysis at 1.84 A resolution
purified ZIKV protease in complex with a peptidomimetic boronic acid inhibitor, X-ray diffraction structure determination and analysis at 2.7 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G68A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
G81A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
L73A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
Q77A
-
substitution in the NS2B sequence, mutation has greater effects on substrate binding than on the reaction rate
W60A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
D129A
-
mutant shows 39fold reduction in catalytic efficacy compared to wild-type
I165A
-
mutant shows a drastic decrease in catalytic efficacy and a drastic increase in Km
N152A
-
mutant shows no a complete inactivation but a 60fold reduced catalytic activity
S135A
S163A
-
mutant shows 12fold reduction in catalytic efficacy compared to wild-type
T134A
-
mutant shows 2.2fold reduction in catalytic efficacy compared to wild-type
A125C/V162C
site-directed mutagenesis, the mutant shows 32% reduction in activity due to the cysteine substitution. Linked A125C/V162C, in which both mutations are within the protease domain, does not migrate differently without DTT. The unlinked either trap does not form intermolecular disulfide bonds
H51A
-
site-directed mutagenesis, the mutation of NS3 protein impairs the charge interaction and the pH dependence of the conformational changes. It stabilizes the open conformation, while the addition of BPTI still converts NS2B-NS3p from open to closed conformation
I73C/P106C
site-directed mutagenesis, the linked open trap mutant does not form intermolecular disulfide bonds appreciably, as evidenced by the lack of higher-molecular weight bands. Unlinked I73C/P106C forms a small amount of NS2BS-SNS3pro, which shows retarded migration as NS2B and NS3pro electrophorese as a single disulfide-bonded complex
K117R/T122R
-
mutant is analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
P176G
-
mutation in the 11-amino acid linker region (169-179): a 70% reduction in luciferase reporter signal and a similar reduction in the level of viral RNA synthesis are observed
S75C
S75C/K117C
site-directed mutagenesis, linked S75C/K117C is induced to form the NS2BS-SNS3pro closed conformation in the presence of active site inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride, suggesting that the mutation forms a disulfide bond when the enzyme is resting in the active conformation. The S75C/K117C pair is close together in the closed conformation but far apart in the open conformation and should therefore trap this variant in the closed conformation upon intramolecular disulfide bond formation
A125C/V162C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, the mutant shows 32% reduction in activity due to the cysteine substitution. Linked A125C/V162C, in which both mutations are within the protease domain, does not migrate differently without DTT. The unlinked either trap does not form intermolecular disulfide bonds
-
I73C/P106C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, the linked open trap mutant does not form intermolecular disulfide bonds appreciably, as evidenced by the lack of higher-molecular weight bands. Unlinked I73C/P106C forms a small amount of NS2BS-SNS3pro, which shows retarded migration as NS2B and NS3pro electrophorese as a single disulfide-bonded complex
-
K117A
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis
-
S75C/K117C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, linked S75C/K117C is induced to form the NS2BS-SNS3pro closed conformation in the presence of active site inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride, suggesting that the mutation forms a disulfide bond when the enzyme is resting in the active conformation. The S75C/K117C pair is close together in the closed conformation but far apart in the open conformation and should therefore trap this variant in the closed conformation upon intramolecular disulfide bond formation
-
C1123A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1125A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1171A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1185A
-
has no effect on either auto-cleavage of the NS2/3 precursor and NS3 protease activities
C184A
-
mutation in the NS2 active site, is defective in NS2-3 processing. When Hepatitis C virus polyproteins with NS2 containing a C184A mutation are co-expressed, NS2 and NS3 cleavage products are detected
C922A
-
reduces NS2/3 auto-cleavage, but has no significant effect on NS3 protease activity
H1175A
-
reduces NS3 protease activity. Auto-cleavage activity is indistinguishable from wild-type
H143A
-
mutation in the NS2 active site, is defective in NS2-3 processing. When Hepatitis C virus polyproteins with NS2 containing a H143A mutation are co-expressed, NS2 and NS3 cleavage products are detected
H143A/C184A
-
mixing wild-type Flag-NS2-3 with double-mutant HA-NS2-3(H143A/C184A) or vice versa yields only cleaved wild-type NS2, whereas the double-mutant polypeptide remains unprocessed because neither of the composite active sites is functional, when a wild-type and a double-mutant NS2-3 dimerize
H952A
-
totally abolishes auto-cleavage of the NS2/3 precursor, whereas NS3 protease activity is not abolished
L1026P/A1027P
-
totally abolishes auto-cleavage of the NS2/3 precursor, whereas NS3 protease activity is not abolished
S1165A
-
completely abrogates NS3 protease activity, but has no effect on NS2/3 auto-cleavage
D42G
has no dramatic effect on either the catalytic activity (50% of wild-type) or self-proteolysis of NS2B-NS3pro. Aprotinin efficiently inhibits proteolytic activity
G22S
G460L
-
no autolytic cleavage, but is an efficient enzyme against the artificial substrate CFP-LQYTKRGGVLWD-YFP
H51A
K48A
P131K/T132P
-
decrease in kcat, which is partially compensated by an improvement in the substrate binding. Shift of the cleavage preferences toward that of the Dengue virus proteinase
R76L
S135A
T52V
D42G
-
has no dramatic effect on either the catalytic activity (50% of wild-type) or self-proteolysis of NS2B-NS3pro. Aprotinin efficiently inhibits proteolytic activity
-
G22S
G460L
-
no autolytic cleavage, but is an efficient enzyme against the artificial substrate CFP-LQYTKRGGVLWD-YFP
-
H51A
K48A
R76L
-
the mutant displays reduced catalytic efficiency compared to the wild type enzyme
-
T52V
-
the mutant displays increased catalytic efficiency compared to the wild type enzyme
-
C143S
-
site-directed mutagenesis, the NS2B mutant cannot form the disulfide bond between C143 residues of neighboring NS3
R95*A/R29G
additional information
G22S
resistant to autoproteolysis at the flexible linker region, retains 3% residual activity
H51A
-
devoid of any proteolytic activity and incapable of autolytically cleaving either the NS2B sequence or the NS3pro-hel boundary. Resistant to the proteolysis in trans by the external, highly active NS2B-NS3pro construct
K48A
-
is a single-chain protein and fully resistant to autolysis at the linker region, exhibits high stability and functional activity, cleaves pyroglutamic acid-Arg-Thr-Lys-Arg-7-amino-4-methylcoumarin
K48A
-
mutation of the C-terminal amino acid residue of the NS2B sequence, inactivates the autolytic cleavage site. Does not have any significant effect on the catalytic activity. Readily cleaved in cis by the integral NS2B-NS3pro activity
K48A
resistant to autoproteolysis at the flexible linker region. Aprotinin efficiently inhibits proteolytic activity
K48A
-
the mutant displays slightly increased catalytic efficiency compared to the wild type enzyme
R76L
-
kinetic parameters are similar to those of the wild-type. Shift of the cleavage preferences toward that of the Dengue virus proteinase
R76L
-
the mutant displays reduced catalytic efficiency compared to the wild type enzyme
T52V
-
exhibits a significant loss of kcat, which is compensated by an improvement in substrate binding. Does not cause any significant differences in the cleavage subsite specificity. Cleavage preferences of the T52V mutant construct are similar to those of the original West Nile virus proteinase
T52V
-
the mutant displays increased catalytic efficiency compared to the wild type enzyme
G22S
-
resistant to autoproteolysis at the flexible linker region, retains 3% residual activity
-
H51A
-
devoid of any proteolytic activity and incapable of autolytically cleaving either the NS2B sequence or the NS3pro-hel boundary. Resistant to the proteolysis in trans by the external, highly active NS2B-NS3pro construct
-
K48A
-
mutation of the C-terminal amino acid residue of the NS2B sequence, inactivates the autolytic cleavage site. Does not have any significant effect on the catalytic activity. Readily cleaved in cis by the integral NS2B-NS3pro activity
-
K48A
-
the mutant displays slightly increased catalytic efficiency compared to the wild type enzyme
-
K48A
-
resistant to autoproteolysis at the flexible linker region. Aprotinin efficiently inhibits proteolytic activity
-
R95*A/R29G
construction of a complex containing residues 45 to 95 of the NS2B cofactor linked via a Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly (G4SG4) linker to the NS3 protease to avoid auto-proteolysis and create the linked protease, the last arginine residue of the NS2B cofactor before the G4SG4 linker is mutated to alanine (R95*A), and arginine 29 of the NS3 protease domain is mutated to glycine (R29G)
R95*A/R29G
Zika virus Puerto Rico isolate
-
construction of a complex containing residues 45 to 95 of the NS2B cofactor linked via a Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly (G4SG4) linker to the NS3 protease to avoid auto-proteolysis and create the linked protease, the last arginine residue of the NS2B cofactor before the G4SG4 linker is mutated to alanine (R95*A), and arginine 29 of the NS3 protease domain is mutated to glycine (R29G)
-
additional information
-
random mutagenesis study. Among 103 clones, 58 represent functionally inactive mutants. All tested alanine-substituted mutants exhibit impaired autolytic activity
additional information
-
separate expression of dengue virus NS3 protease and its NS2B cofactor domain and efficient co-refolding to form a stable complex, method evaluation, overview. This straightforward and robust method allows for separate isotope labeling of the two proteins, facilitating analysis by NMR spectroscopy, detailed overview. Unlinked NS2B-NS3pro behaves better in NMR spectroscopy than linked NS2B-NS3pro, which has resulted in the backbone resonance assignment of the unlinked NS2B-NS3 complex bound to a peptidic boronic acid inhibitor
additional information
-
16 possible mutants bearing and an exchanged Ile to Val are analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
additional information
-
7 Ser to Ala mutants are analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
additional information
multiple types of protein constructs have been used for NS2B-NS3pro expression. In one type, a Gly4SerGly4 linker joins NS2B to NS3pro, reported to improve expression and purification, while another type requires co-expression of the unlinked NS2B and NS3 regions. The catalytic activity is slightly different between the linked and unlinked protein constructs, with the unlinked form showing activity approximately 0-5fold greater than that of the linked form, likely due to constraints introduced by the synthetic linker
additional information
Dengue virus type 2 Thailand/16681/1984
-
multiple types of protein constructs have been used for NS2B-NS3pro expression. In one type, a Gly4SerGly4 linker joins NS2B to NS3pro, reported to improve expression and purification, while another type requires co-expression of the unlinked NS2B and NS3 regions. The catalytic activity is slightly different between the linked and unlinked protein constructs, with the unlinked form showing activity approximately 0-5fold greater than that of the linked form, likely due to constraints introduced by the synthetic linker
-
additional information
mutation in the 11-amino acid linker region (169-179): a Gly residue before Pro174 is introduced in DENV4 NS2B18NS3: The mutant protein having a glycine insertion in its linker region adopts another conformation where the protease domain has not rotated by an angle of 161° relative to the helicase domain
additional information
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
additional information
-
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
additional information
-
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
-
additional information
-
mutation studies at the residues His94, Asp118 and Ser176 reveal that Asp118-His94 bond play an important role in the structural stability of NS2B-NS3 complex
additional information
construction of eZiPro that contains the NS2B cofactor region (residues 45-96) linked with NS3 protein (residues 1-177) through the last five residues of NS2B (K126TGKR130), and the gZiPro construct, which is similar except that the G4SG4 linker replaced K126TGKR130 of NS2B. Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
construction of eZiPro that contains the NS2B cofactor region (residues 45-96) linked with NS3 protein (residues 1-177) through the last five residues of NS2B (K126TGKR130), and the gZiPro construct, which is similar except that the G4SG4 linker replaced K126TGKR130 of NS2B. Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
construction of the NS2B cofactor region linked to the NS3 protease domain via a glycine-rich flexible linker (Gly4-Ser-Gly4 linker), structural dynamics of this conventional Zika protease (gZiPro) using NMR spectroscopy, overview. Although the glycine-rich linker in gZiPro does not alter the overall folding of the protease in solution, gZiPro is not homogenous in ion exchange chromatography. Compared to the unlinked protease construct, the artificial linker affects the chemical environment of many residues including H51 in the catalytic triad. Direct comparison of ZIKV protease constructs with and without an artificial linker, namely gZiPro (with the Gly4-Ser-Gly4 linker), bZiPro (unlinked NS2B NS3protease), and eZiPro (NS2B-NS3 junction sequence KTGKR as the linker). Solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation. Effect of the linker on the chemical environment of residues, dynamics of the linked protease, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
various truncations and mutations in the cNS2B sequence show that conformational integrity of the entire 47 amino acids is critical for protease activity. DENV-2 NS3 protease can be pulled-down and is trans-activated by cNS2B cofactors from DENV-1, -3, -4, and West Nile Virus
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion-exchange chromatography
by immobilized-metal affinity chromatography, ion exchange chromatography and gel filtration
-
complete NS3 molecule fused to 18 residues of the NS2B cofactor or NS3 helicase (residues 177 to 618) purified by gel filtration
-
expression and purification of a natural form of DENV protease containing the full-length NS2B protein and the protease domain of NS3. Purified protein in lyso-myristoyl phosphatidylcholine, Fos-14 and Fos15 exhibits protease activity, while almost no activity is observed in Lyso-myristoyl phosphatidylglycerol micelles. The purified protease also exhibits self-cleavage activity when it is purified in lyso-myristoyl phosphatidylcholine micelles, but not in other detergent micelles
-
expression of NS2B(H)-NS3pro complex in E.scherichiacoli predominantly as insoluble protein and purification to 95% purity
-
NS2B-NS3pro construct purified by Co2+-chelating Sepharose Fast Flow chromatography
NS2B-NS3pro constructs purified by Co2+ affinity chromatography
NS2B-NS3pro wild-type and K48A constructs purified by Co2+ affinity chromatography and gel filtration, to homogeneity
-
on Ni-NTA column
protocol for the preparation of the full-length NS2B/NS3 complex from dengue serotype 2 virus by utilizing a Mistic-fusion expression cassette in Escherichia coli. The protease complex is successfully solubilized and stabilized from the bacterial membrane and purified with the use of foscholine-14 detergent. The detergent-solubilized protease complex retains autolytic activity and exists as a robust trimer, implying a molecular assembly in the membrane
-
purified from insoluble inclusion bodies by solubilization in 6 M guanidine hydrochloride and metal chelate resin affinity chromatography
-
recombinant DV NS2B-NS3pro, C-terminally tagged with a hexahistidine tag, purified by Co2+ affinity chromatography
-
recombinant His-tagged enzyme complex mutant H51A/S75C from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage via thrombin, dialysis, and gel filtration
recombinant His6-SUMO-tagged linked and unlinked NS3-NS2B(45-95) complex linked from Escherichia coli strain BL21 Codon Plus (DE3) by nickel affinity chromatography, tag cleavage by yeast SUMO Protease 1, followed by another step of nickel affinity chromatography, and gel filtration
recombinant His6-tagged protease DENV2 NS2B-NS3pro linked and form from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant unlinked enzyme is purified by anion exchange chromatography
recombinant separately expressed His-tagged NS2B and NS3pro from Escherichia coli, refolded and forming the active complex, by nickel affinity chromatography, tag cleavage by thrombin and/or TEV protease, and another step of nickel affinity chromatography, and gel filtration
-
wild-type and mutant NS2B-NS3pro and NS2B-NS3prohel constructs, C-terminally tagged with a hexahistidine tag, purified by Co2+ affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CF40glyNS3pro chimeric protease tagged with six consecutive histidines expressed in Escherichia coli strain SG13009
-
cloning of the NS3 protease domain (NS3 S1-E171), the active deltaNS2BNS3pro complex (NS3pro domain fused with NS2B M48-A94 and L126-R131 regions), the deltaNS2B-NS3pro HDA complex (with S138A), mutated proteins and chimeric proteases with the NS2B cofactor from Langat virus and Dengue virus type 3 replacing the Alkhurma virus sequence. PCR products cloned into pET-DEST42 vector
-
codon optimized cDNA encoding NS2B-NS3, recombinant expression of His-tagged wild-type enzyme and constructs in Escherichia coli strain BL21(DE3)
complete NS3 molecule fused to 18 residues of the NS2B cofactor or NS3 helicase (residues 177 to 618) cloned into pET32b vector and expressed in Escherichia coli BL21-CodonPlus
-
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
expression in Escherichia coli BL21(DE3)
into the pET101 and expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
mutant K48A cloned into pET101/D-TOPO vector and expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
NS2B-NS3pro construct cloned into the pET101/D-TOPO vector C-terminally tagged with the His x 6 tag and expressed in Escherichia coli BL21(DE3) Codon Plus cells
NS2B-NS3pro wild-type and K48A constructs cloned into pET101 vector and expressed in Escherichia coli BL21 (DE3) Codon Plus cells
-
NS2pro (NS2 residues 94-217), a truncated form of NS2 shown to be proteolytically active in the context of an NS2-3 precursor that includes the NS3 protease domain, expressed in Escherichia coli. NS2 containing wild-type or mutant active site residues expressed in mammalian cells in the context of a full-length viral polyprotein or as NS2-3 precursor with an N-terminal Flag or HA tag
-
plasmid pDV2-NS2B40-G4SG4-ASR-NS3FL expressed in Escherichia coli strain Rosetta2
plasmid pJEVNS2B40-G4SG4-ASR-NS3FL expressed in Escherichia coli strain Rosetta2
-
plasmid pYFV-NS2B40-G4SG4-HM-NS3FL expressed in Escherichia coli strain Rosetta2
-
protocol for the preparation of the full-length NS2B/NS3 complex from dengue serotype 2 virus by utilizing a Mistic-fusion expression cassette in Escherichia coli
-
recombinant expression of an active NS3pro domain fused with the NS2B cofactor (NS2BLNNS3pro) in a prokaryotic expression system
recombinant expression of codon-optimized N-terminally His6-tagged dengue virus serotype 2 protease (DENV2 NS2B-NS3pro)from linked and unlinked constructs in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme complex mutant H51A/S75C in Escherichia coli strain BL21(DE3)
-
recombinant overexpression of His6-SUMO-tagged linked and unlinked NS3-NS2B(45-95) complex linked via G4SG4 linker in Escherichia coli strain BL21 Codon Plus (DE3)
separate recombinant expression of N-terminally His-tagged DENV virus 2 NS2B and NS3pro in Escherichia coli in inclusion bodies
-
single-chain complex of NS2B/NS3 protease (CF40-gly-NS3pro190) expressed as an N-terminally His-tagged fusion protein in Escherichia coli
-
the dengue 2 NS2B-NS3pro construct contains 255 residues, including a (Gly)4-Ser-(Gly)4 linker between NS2B (47 residues) and NS3pro (185 residues). In addition, it contains a His-tag at the C-terminus and the T7 gene 10 N-terminal peptide MASMTG at the N-terminus followed by a two-residue cloning artifact (LE), resulting in a 27 kDa protein. To suppress slow autocleavage detected by SDS-PAGE, most samples have the mutation Lys15Ala which cause no significant changes in the appearance of the NMR spectra. Protein is expressed in Escherichia coli
-
using recombinant vaccinia virus expression system
wild-type Dengue virus and West Nile virus NS2B-NS3pro, together with West Nile virus/Dengue virus chimeras expressed with C-terminal His tags in Escherichia coli BL21(DE3) Codon Plus cells
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
plasmid pDV2-NS2B40-G4SG4-ASR-NS3FL expressed in Escherichia coli strain Rosetta2
-
plasmid pDV2-NS2B40-G4SG4-ASR-NS3FL expressed in Escherichia coli strain Rosetta2
-
wild-type Dengue virus and West Nile virus NS2B-NS3pro, together with West Nile virus/Dengue virus chimeras expressed with C-terminal His tags in Escherichia coli BL21(DE3) Codon Plus cells
-
wild-type Dengue virus and West Nile virus NS2B-NS3pro, together with West Nile virus/Dengue virus chimeras expressed with C-terminal His tags in Escherichia coli BL21(DE3) Codon Plus cells
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant separately expressed His-tagged NS2B and NS3pro from Escherichia coli are co-refolded by one-step dialysis overnight at 4°C in a 2:1 M NS2B:NS3pro ratio to maximize formation of the active complex. The refolding buffer is 25 mM Tris, pH 8.5 (set at 4°C), 5% glycerol, and 100 mM NaCl
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
-
to validate NS2B as a potential target in allosteric inhibitor development, a cNS2B specific human monoclonal antibody (3F10) is used. 3F10 disrupts the interaction between cNS2B and NS3 in vitro and reduces DENV viral replication in HEK293 cells
molecular biology
-
it is demonstrated that the WNV NS2B/NS3pro-hel is an active endoproteolytic enzyme at the ER membrane and the in-cell selectivity profiling of the membrane-anchored flaviviral protease is reported
synthesis
-
expression and purification of a natural form of DENV protease containing the full-length NS2B protein and the protease domain of NS3. The protease is expressed in Escherichia coli and purified in detergent micelles necessary for its folding. This purified protein is active in detergent micelles such as lyso-myristoyl phosphatidylcholine
analysis
-
NS2B-NS3pro K48A mutant construct is well suited for follow-up purification and structural and drug design studies
analysis
-
two sets of prediction approaches. Secondary structure prediction performed using available structure prediction servers. A second approach makes use of the information on the secondary structures extracted from structure prediction servers, threading techniques and DSSP database of some of the templates used in the threading techniques. Consensus on the one-dimensional secondary structure of Dengue virus type 2 protease obtained from each approach and evaluated against data from the recently crystallised Dengue virus type 2 NS2B/NS3 obtained from the Protein Data Bank. The second approach shows higher accuracy compared to the use of prediction servers only and thus is applicable to the initial stage of structural studies of proteins with low amino acid sequence homology against other available proteins in the Protein Data Bank
drug development
-
characteristics of Yellow fever virus protease are very similar to those reported for dengue and West Nile virus proteases, and suggest that pan-flavivirus NS3 protease drugs may be developed for flaviviral diseases
drug development
-
proteolysis through formation of a composite active site in NS2-3 protease occurs in the context of the viral polyprotein expressed in mammalian cells. This offers new opportunities for antiviral drug design
drug development
-
switched cleavage preferences of West Nile virus NS2B-NS3(pro)teinase may provide valuable data for the design of optimized substrates and substrate-based selective inhibitors of flaviviral proteinases
drug development
-
unique cleavage preferences of the Dengue virus protease promise novelty for the design of potent inhibitors that may be selective for the flaviviral proteases over proteases of the host cell and thus provide a solid base for follow-on structural and functional studies
drug development
-
unique cleavage preferences of the West Nile virus protease promise novelty for the design of potent inhibitors that may be selective for the flaviviral proteases over proteases of the host cell and thus provide a solid base for follow-on structural and functional studies
drug development
useful for the development of specific allosteric inhibitors designed to interfere with the productive interactions of NS2B with NS3pro
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
-
the dengue virus NS2B-NS3 protease (NS2B-NS3p) is an important antiviral target for drug development
drug development
-
the enzyme is a target for the development of structure-based antiviral drugs against ZIKV and related pathogenic flaviviruses
drug development
-
the viral serine protease NS2B/NS3 is an attractive target for the development of anti-WNV agents
drug development
Dengue virus type 2 Thailand/16681/1984
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
Yellow fever virus 17D vaccine
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
-
the essential enzyme is a target for drug design
-
drug development
Dengue virus type 2 16681
-
unique cleavage preferences of the Dengue virus protease promise novelty for the design of potent inhibitors that may be selective for the flaviviral proteases over proteases of the host cell and thus provide a solid base for follow-on structural and functional studies
-
drug development
dengue virus type I Nauru/West Pac/1974
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
-
unique cleavage preferences of the West Nile virus protease promise novelty for the design of potent inhibitors that may be selective for the flaviviral proteases over proteases of the host cell and thus provide a solid base for follow-on structural and functional studies
-
drug development
-
useful for the development of specific allosteric inhibitors designed to interfere with the productive interactions of NS2B with NS3pro
-
drug development
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
drug development
Murray Valley encephalitis virus MVE-1-51
-
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
-
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Flavivirus genome organization, expression, and replication
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Dengue virus, Flavivirus sp., Yellow fever virus
brenda
Cah, A.; Falgout, B.; Lai, C.J.
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Dengue virus
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Lin, C.; Amberg, S.M.; Chambers, T.J.; Rice, C.M.
Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
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1993
Yellow fever virus
brenda
Chambers, T.J.; Nestorowicz, A.; Rice, C.M.
Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication
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1600-1605
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Yellow fever virus
brenda
Murthy, H.M.K.; Judge, K.; DeLucas, L.; Clum, S.; Padmanabhan, R.
Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman-Birk inhibitor
Acta Crystallogr. Sect. D
55
1370-1372
1999
Dengue virus
-
brenda
Krishna Murthy, H.M.; Clum, S.; Padmanabhan, R.
Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects
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274
5573-5580
1999
Dengue virus
brenda
Droll, D.A.; Krishna Murthy, H.M.; Chambers, T.J.
Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function
Virology
275
335-347
2000
Yellow fever virus
brenda
D'Arcy, A.; Chaillet, M.; Schiering, N.; Villard, F.; Lim, S.P.; Lefeuvre, P.; Erbel, P.
Purification and crystallization of dengue and West Nile virus NS2B-NS3 complexes
Acta Crystallogr. Sect. F
62
157-162
2006
Dengue virus, West Nile virus
brenda
Li, J.; Lim, S.P.; Beer, D.; Patel, V.; Wen, D.; Tumanut, C.; Tully, D.C.; Williams, J.A.; Jiricek, J.; Priestle, J.P.; Harris, J.L.; Vasudevan, S.G.
Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries
J. Biol. Chem.
280
28766-28774
2005
Dengue virus
brenda
Niyomrattanakit, P.; Winoyanuwattikun, P.; Chanprapaph, S.; Angsuthanasombat, C.; Panyim, S.; Katzenmeier, G.
Identification of residues in the dengue virus type 2 NS2B cofactor that are critical for NS3 protease activation
J. Virol.
78
13708-13716
2004
Dengue virus type 2
brenda
Ramanathan, M.P.; Chambers, J.A.; Pankhong, P.; Chattergoon, M.; Attatippaholkun, W.; Dang, K.; Shah, N.; Weiner, D.B.
Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway
Virology
345
56-72
2006
West Nile virus
brenda
Lin, C.W.; Lin, K.H.; Lyu, P.C.; Chen, W.J.
Japanese encephalitis virus NS2B-NS3 protease binding to phage-displayed human brain proteins with the domain of trypsin inhibitor and basic region leucine zipper
Virus Res.
116
106-113
2006
Japanese encephalitis virus
brenda
Chanprapaph, S.; Saparpakorn, P.; Sangma, C.; Niyomrattanakit, P.; Hannongbua, S.; Angsuthanasombat, C.; Katzenmeier, G.
Competitive inhibition of the dengue virus NS3 serine protease by synthetic peptides representing polyprotein cleavage sites
Biochem. Biophys. Res. Commun.
330
1237-1246
2005
Dengue virus
brenda
Gouvea, I.E.; Izidoro, M.A.; Judice, W.A.; Cezari, M.H.; Caliendo, G.; Santagada, V.; dos Santos, C.N.; Queiroz, M.H.; Juliano, M.A.; Young, P.R.; Fairlie, D.P.; Juliano, L.
Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates
Arch. Biochem. Biophys.
457
187-196
2007
Dengue virus
brenda
Johnston, P.A.; Phillips, J.; Shun, T.Y.; Shinde, S.; Lazo, J.S.; Huryn, D.M.; Myers, M.C.; Ratnikov, B.I.; Smith, J.W.; Su, Y.; Dahl, R.; Cosford, N.D.; Shiryaev, S.A.; Strongin, A.Y.
HTS identifies novel and specific uncompetitive inhibitors of the two-component NS2B-NS3 proteinase of West Nile virus
Assay Drug Dev. Technol.
5
737-750
2007
West Nile virus
brenda
Shiryaev, S.A.; Kozlov, I.A.; Ratnikov, B.I.; Smith, J.W.; Lebl, M.; Strongin, A.Y.
Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of Dengue and West Nile viruses
Biochem. J.
401
743-752
2007
West Nile virus, Dengue virus type 2, Dengue virus type 2 16681, West Nile virus NY99
brenda
Othman, R.; Wahab, H.A.; Yusof, R.; Rahman, N.A.
Analysis of secondary structure predictions of dengue virus type 2 NS2B/NS3 against crystal structure to evaluate the predictive power of the in silico methods
In Silico Biol.
7
215-224
2007
Dengue virus type 2
brenda
Bera, A.K.; Kuhn, R.J.; Smith, J.L.
Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease
J. Biol. Chem.
282
12883-12892
2007
Japanese encephalitis virus, West Nile virus, Yellow fever virus, Dengue virus type 2, Dengue virus type 4, West Nile virus NY99
brenda
Pastorino, B.A.; Peyrefitte, C.N.; Grandadam, M.; Thill, M.C.; Tolou, H.J.; Bessaud, M.
Mutagenesis analysis of the NS2B determinants of the Alkhurma virus NS2B-NS3 protease activation
J. Gen. Virol.
87
3279-3283
2006
Alkhumra hemorrhagic fever virus
brenda
Loehr, K.; Knox, J.E.; Phong, W.Y.; Ma, N.L.; Yin, Z.; Sampath, A.; Patel, S.J.; Wang, W.L.; Chan, W.L.; Rao, K.R.; Wang, G.; Vasudevan, S.G.; Keller, T.H.; Lim, S.P.
Yellow fever virus NS3 protease: peptide-inhibition studies
J. Gen. Virol.
88
2223-2227
2007
Yellow fever virus
brenda
Radichev, I.; Shiryaev, S.A.; Aleshin, A.E.; Ratnikov, B.I.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Structure-based mutagenesis identifies important novel determinants of the NS2B cofactor of the West Nile virus two-component NS2B-NS3 proteinase
J. Gen. Virol.
89
636-641
2008
West Nile virus (P06935), West Nile virus, West Nile virus NY99 (P06935)
brenda
Tedbury, P.R.; Harris, M.
Characterisation of the role of zinc in the hepatitis C virus NS2/3 auto-cleavage and NS3 protease activities
J. Mol. Biol.
366
1652-1660
2007
Hepacivirus C
brenda
Shiryaev, S.A.; Ratnikov, B.I.; Aleshin, A.E.; Kozlov, I.A.; Nelson, N.A.; Lebl, M.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Switching the substrate specificity of the two-component NS2B-NS3 flavivirus proteinase by structure-based mutagenesis
J. Virol.
81
4501-4509
2007
Dengue virus, West Nile virus
brenda
Luo, D.; Xu, T.; Hunke, C.; Grueber, G.; Vasudevan, S.G.; Lescar, J.
Crystal structure of the NS3 protease-helicase from dengue virus
J. Virol.
82
173-183
2008
Dengue virus type 4
brenda
Lorenz, I.C.; Marcotrigiano, J.; Dentzer, T.G.; Rice, C.M.
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
Nature
442
831-835
2006
Hepacivirus C
brenda
Shiryaev, S.A.; Aleshin, A.E.; Ratnikov, B.I.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Expression and purification of a two-component flaviviral proteinase resistant to autocleavage at the NS2B-NS3 junction region
Protein Expr. Purif.
52
334-339
2007
West Nile virus
brenda
Bessaud, M.; Pastorino, B.A.; Peyrefitte, C.N.; Rolland, D.; Grandadam, M.; Tolou, H.J.
Functional characterization of the NS2B/NS3 protease complex from seven viruses belonging to different groups inside the genus Flavivirus
Virus Res.
120
79-90
2006
Yellow fever virus, Zika virus, Saint Louis encephalitis virus, Bussuquara virus, Langat virus (P29837), Dengue virus type 3 (Q6YMS4), dengue virus type I (Q91NH1), Yellow fever virus Asibi, Dengue virus type 3 Sri Lanka/1266/2000 (Q6YMS4), dengue virus type I D1/H/IMTSSA/98/606 (Q91NH1), Langat virus TP21 (P29837), Zika virus Ar-D-41644, Saint Louis encephalitis virus MSI-7
brenda
Niyomrattanakit, P.; Yahorava, S.; Mutule, I.; Mutulis, F.; Petrovska, R.; Prusis, P.; Katzenmeier, G.; Wikberg, J.E.
Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides
Biochem. J.
397
203-211
2006
Dengue virus type 2
brenda
Kiat, T.S.; Pippen, R.; Yusof, R.; Ibrahim, H.; Khalid, N.; Rahman, N.A.
Inhibitory activity of cyclohexenyl chalcone derivatives and flavonoids of fingerroot, Boesenbergia rotunda (L.), towards dengue-2 virus NS3 protease
Bioorg. Med. Chem. Lett.
16
3337-3340
2006
Dengue virus type 2
brenda
Yin, Z.; Patel, S.J.; Wang, W.; Wang, G.; Chan, W.; Rao, K.R.; Alam, J.; Jeyaraj, D.A.; Ngew, X.; Patel, V.; Beer, D.; Lim, S.P.; Vasudevan, S.G.; Keller, T.H.
Peptide inhibitors of dengue virus NS3 protease. Part 1: Warhead
Bioorg. Med. Chem. Lett.
16
36-39
2006
Dengue virus
brenda
Yin, Z.; Patel, S.J.; Wang, W.; Chan, W.; Ranga Rao, K.R.; Wang, G.; Ngew, X.; Patel, V.; Beer, D.; Knox, J.E.; Ma, N.L.; Ehrhardt, C.; Lim, S.P.; Vasudevan, S.G.; Keller, T.H.
Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitors
Bioorg. Med. Chem. Lett.
16
40-43
2006
Dengue virus
brenda
Schrauf, S.; Schlick, P.; Skern, T.; Mandl, C.W.
Functional analysis of potential carboxy-terminal cleavage sites of tick-borne encephalitis virus capsid protein
J. Virol.
82
2218-2229
2008
Flavivirus sp.
brenda
Shiryaev, S.A.; Radichev, I.A.; Ratnikov, B.I.; Aleshin, A.E.; Gawlik, K.; Stec, B.; Frisch, C.; Knappik, A.; Strongin, A.Y.
Isolation and characterization of selective and potent human Fab inhibitors directed to the active-site region of the two-component NS2B-NS3 proteinase of West Nile virus
Biochem. J.
427
369-376
2010
West Nile virus, West Nile virus NY99
brenda
Sidique, S.; Shiryaev, S.A.; Ratnikov, B.I.; Herath, A.; Su, Y.; Strongin, A.Y.; Cosford, N.D.
Structure-activity relationship and improved hydrolytic stability of pyrazole derivatives that are allosteric inhibitors of West Nile Virus NS2B-NS3 proteinase
Bioorg. Med. Chem. Lett.
19
5773-5777
2009
West Nile virus
brenda
Schueller, A.; Yin, Z.; Brian Chia, C.S.; Doan, D.N.; Kim, H.K.; Shang, L.; Loh, T.P.; Hill, J.; Vasudevan, S.G.
Tripeptide inhibitors of dengue and West Nile virus NS2B-NS3 protease
Antiviral Res.
92
96-101
2011
Dengue virus, West Nile virus
brenda
Kondo, M.Y.; Oliveira, L.C.; Okamoto, D.N.; de Araujo, M.R.; Duarte dos Santos, C.N.; Juliano, M.A.; Juliano, L.; Gouvea, I.E.
Yellow fever virus NS2B/NS3 protease: hydrolytic properties and substrate specificity
Biochem. Biophys. Res. Commun.
407
640-644
2011
Yellow fever virus
brenda
Kannappan, P.; Narayanan, S.
Mutation and docking studies on NS2b-NS3 complex from yellow fever virus towards drug discovery
Bioinformation
6
303-306
2011
Yellow fever virus
brenda
Condotta, S.A.; Martin, M.M.; Boutin, M.; Jean, F.
Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates
Biol. Chem.
391
549-559
2010
West Nile virus
brenda
Phong, W.Y.; Moreland, N.J.; Lim, S.P.; Wen, D.; Paradkar, P.N.; Vasudevan, S.G.
Dengue protease activity: the structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target
Biosci. Rep.
31
399-409
2011
Dengue virus type 2
brenda
Lim, H.A.; Joy, J.; Hill, J.; San Brian Chia, C.
Novel agmatine and agmatine-like peptidomimetic inhibitors of the West Nile virus NS2B/NS3 serine protease
Eur. J. Med. Chem.
46
3130-3134
2011
West Nile virus
brenda
Frimayanti, N.; Chee, C.F.; Zain, S.M.; Rahman, N.A.
Design of new competitive dengue ns2b/ns3 protease inhibitors-a computational approach
Int. J. Mol. Sci.
12
1089-1100
2011
Dengue virus
brenda
de la Cruz, L.; Nguyen, T.H.; Ozawa, K.; Shin, J.; Graham, B.; Huber, T.; Otting, G.
Binding of Low Molecular Weight Inhibitors Promotes Large Conformational Changes in the Dengue Virus NS2B-NS3 Protease: Fold Analysis by Pseudocontact Shifts
J. Am. Chem. Soc.
133
19205-19215
2011
Dengue virus type 2
brenda
Luo, D.; Wei, N.; Doan, D.N.; Paradkar, P.N.; Chong, Y.; Davidson, A.D.; Kotaka, M.; Lescar, J.; Vasudevan, S.G.
Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications
J. Biol. Chem.
285
18817-18827
2010
Dengue virus type 2, Dengue virus type 4 (Q2YHF0)
brenda
Salaemae, W.; Junaid, M.; Angsuthanasombat, C.; Katzenmeier, G.
Structure-guided mutagenesis of active site residues in the dengue virus two-component protease NS2B-NS3
J. Biomed. Sci.
17
68
2010
Dengue virus
brenda
Frecer, V.; Miertus, S.
Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of Dengue virus NS2B-NS3 protease
J. Comput. Aided Mol. Des.
24
195-212
2010
Dengue virus type 2
brenda
Wu, H.; Bock, S.; Snitko, M.; Berger, T.; Weidner, T.; Holloway, S.; Kanitz, M.; Diederich, W.E.; Steuber, H.; Walter, C.; Hofmann, D.; Weissbrich, B.; Spannaus, R.; Acosta, E.G.; Bartenschlager, R.; Engels, B.; Schirmeister, T.; Bodem, J.
Novel dengue virus NS2B/NS3 protease inhibitors
Antimicrob. Agents Chemother.
59
1100-1109
2015
Dengue virus
brenda
Verma, R.; Jatav, V.; Sharma, S.
Identification of inhibitors of dengue virus (Denv1, Denv2 and Denv3) NS2B/NS3 serine protease: A molicular docking and simulation approach
Asian J. Pharm. Clin. Res.
8
287-292
2015
Dengue virus
-
brenda
Junaid, M.; Angsuthanasombat, C.; Wikberg, J.E.; Ali, N.; Katzenmeier, G.
A straightforward experimental approach to expression, purification, refolding, and enzymatic analysis of recombinant dengue virus NS2B(H)-NS3pro protease
Biochemistry (Moscow)
78
920-924
2013
Dengue virus
brenda
Choksupmanee, O.; Hodge, K.; Katzenmeier, G.; Chimnaronk, S.
Structural platform for the autolytic activity of an intact NS2B-NS3 protease complex from dengue virus
Biochemistry
51
2840-2851
2012
Dengue virus
brenda
Senthilvel, P.; Lavanya, P.; Kumar, K.M.; Swetha, R.; Anitha, P.; Bag, S.; Sarveswari, S.; Vijayakumar, V.; Ramaiah, S.; Anbarasu, A.
Flavonoid from Carica papaya inhibits NS2B-NS3 protease and prevents Dengue 2 viral assembly
Bioinformation
9
889-895
2013
Dengue virus
brenda
Liu, H.; Wu, R.; Sun, Y.; Ye, Y.; Chen, J.; Luo, X.; Shen, X.; Liu, H.
Identification of novel thiadiazoloacrylamide analogues as inhibitors of dengue-2 virus NS2B/NS3 protease
Bioorg. Med. Chem.
22
6344-6352
2014
Dengue virus
brenda
de Sousa, L.R.; Wu, H.; Nebo, L.; Fernandes, J.B.; da Silva, M.F.; Kiefer, W.; Kanitz, M.; Bodem, J.; Diederich, W.E.; Schirmeister, T.; Vieira, P.C.
Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: inhibition kinetics and docking studies
Bioorg. Med. Chem.
23
466-470
2015
Dengue virus
brenda
Li, L.; Basavannacharya, C.; Chan, K.W.; Shang, L.; Vasudevan, S.G.; Yin, Z.
Structure-guided discovery of a novel non-peptide inhibitor of dengue virus NS2B-NS3 protease
Chem. Biol. Drug Des.
86
255-264
2015
Dengue virus
brenda
Ang, M.J.; Yong, G.H.; Poulsen, A.; Then, S.W.; Li, Z.; Joy, J.; Hill, J.; Chia, C.S.
Substrate-based peptidomimetic inhibitors of the Murray Valley encephalitis virus NS2B/NS3 serine protease: a P1-P4 SAR study
Eur. J. Med. Chem.
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2013
Murray Valley encephalitis virus
brenda
de la Cruz, L.; Chen, W.N.; Graham, B.; Otting, G.
Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B-NS3 protease
FEBS J.
281
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2014
Dengue virus (Q91H74), Dengue virus
brenda
Chen, W.N.; Loscha, K.V.; Nitsche, C.; Graham, B.; Otting, G.
The dengue virus NS2B-NS3 protease retains the closed conformation in the complex with BPTI
FEBS Lett.
588
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2014
Dengue virus (Q91H74), Dengue virus
brenda
Nguyen, T.; Lee, S.; Wang, H.; Chen, H.; Wu, Y.; Lin, S.; Kim, D.; Kim, D.
In vitro evaluation of novel inhibitors against the NS2B-NS3 protease of dengue fever virus type 4
Molecules
18
15600-15612
2013
Dengue virus
brenda
Ang, M.J.; Li, Z.; Lim, H.A.; Ng, F.M.; Then, S.W.; Wee, J.L.; Joy, J.; Hill, J.; Chia, C.S.
A P2 and P3 substrate specificity comparison between the Murray Valley encephalitis and West Nile virus NS2B/NS3 protease using C-terminal agmatine dipeptides
Peptides
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2014
West Nile virus, Murray Valley encephalitis virus
brenda
Huang, Q.; Li, Q.; Joy, J.; Chen, A.S.; Ruiz-Carrillo, D.; Hill, J.; Lescar, J.; Kang, C.
Lyso-myristoyl phosphatidylcholine micelles sustain the activity of Dengue non-structural (NS) protein 3 protease domain fused with the full-length NS2B
Protein Expr. Purif.
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156-162
2013
Dengue virus
brenda
Hill, M.E.; Kumar, A.; Wells, J.A.; Hobman, T.C.; Julien, O.; Hardy, J.A.
The unique cofactor region of zika virus NS2B-NS3 protease facilitates cleavage of key host proteins
ACS Chem. Biol.
13
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2018
Zika virus
brenda
Luo, D.; Vasudevan, S.G.; Lescar, J.
The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development
Antiviral Res.
118
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2015
Yellow fever virus (P03314), Murray Valley encephalitis virus (P05769), West Nile virus (P06935), Kunjin virus (P14335), dengue virus type I (P17763), Japanese encephalitis virus (P27395), Dengue virus type 2 (P29990), Dengue virus type 4 (Q2YHF0), Kokobera virus (Q32ZD5), Dengue virus type 3 (Q6YMS3), Dengue virus type 2 Thailand/16681/1984 (P29990), Dengue virus type 3 Martinique/1243/1999 (Q6YMS3), Yellow fever virus 17D vaccine (P03314), Dengue virus type 4 Thailand/0348/1991 (Q2YHF0), dengue virus type I Nauru/West Pac/1974 (P17763), Japanese encephalitis virus SA-14 (P27395), Kunjin virus MRM61C (P14335), Murray Valley encephalitis virus MVE-1-51 (P05769)
brenda
Rut, W.; Zhang, L.; Kasperkiewicz, P.; Poreba, M.; Hilgenfeld, R.; Drag, M.
Extended substrate specificity and first potent irreversible inhibitor/activity-based probe design for Zika virus NS2B-NS3 protease
Antiviral Res.
139
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2017
Zika virus (A0A024B7W1), Zika virus
brenda
Shiryaev, S.A.; Farhy, C.; Pinto, A.; Huang, C.T.; Simonetti, N.; Elong Ngono, A.; Dewing, A.; Shresta, S.; Pinkerton, A.B.; Cieplak, P.; Strongin, A.Y.; Terskikh, A.V.
Characterization of the Zika virus two-component NS2B-NS3 protease and structure-assisted identification of allosteric small-molecule antagonists
Antiviral Res.
143
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2017
Zika virus (A0A024B7W1), Zika virus
brenda
Zhu, L.; Yang, J.; Li, H.; Sun, H.; Liu, J.; Wang, J.
Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy
Biochem. Biophys. Res. Commun.
461
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2015
Dengue virus type 2
brenda
Aguilera-Pesantes, D.; Robayo, L.E.; Mendez, P.E.; Mollocana, D.; Marrero-Ponce, Y.; Torres, F.J.; Mendez, M.A.
Discovering key residues of dengue virus NS2b-NS3-protease new binding sites for antiviral inhibitors design
Biochem. Biophys. Res. Commun.
492
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2017
Dengue virus type 3 (Q5UB51), Dengue virus type 3 Singapore/8120/1995 (Q5UB51)
brenda
Kuiper, B.D.; Slater, K.; Spellmon, N.; Holcomb, J.; Medapureddy, P.; Muzzarelli, K.M.; Yang, Z.; Ovadia, R.; Amblard, F.; Kovari, I.A.; Schinazi, R.F.; Kovari, L.C.
Increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease
Biochem. Biophys. Res. Commun.
492
668-673
2017
Zika virus (A0A384KRS4), Zika virus, Zika virus Puerto Rico isolate (A0A384KRS4)
brenda
Balajee, R.; Srinivasadesikan, V.; Sakthivadivel, M.; Gunasekaran, P.
In silico screening, alanine mutation, and DFT approaches for identification of NS2B/NS3 protease inhibitors
Biochem. Res. Int.
2016
7264080
2016
Dengue virus type 2
brenda
Hill, M.E.; Yildiz, M.; Hardy, J.A.
Cysteine disulfide traps reveal distinct conformational ensembles in dengue virus NS2B-NS3 protease
Biochemistry
58
776-787
2019
Dengue virus type 2 (P29990), Dengue virus type 2 Thailand/16681/1984 (P29990)
brenda
Takagi, Y.; Matsui, K.; Nobori, H.; Maeda, H.; Sato, A.; Kurosu, T.; Orba, Y.; Sawa, H.; Hattori, K.; Higashino, K.; Numata, Y.; Yoshida, Y.
Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity
Bioorg. Med. Chem. Lett.
27
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2017
Dengue virus type 2
brenda
Weng, Z.; Shao, X.; Graf, D.; Wang, C.; Klein, C.D.; Wang, J.; Zhou, G.C.
Identification of fused bicyclic derivatives of pyrrolidine and imidazolidinone as dengue virus-2 NS2B-NS3 protease inhibitors
Eur. J. Med. Chem.
125
751-759
2017
Dengue virus type 2
brenda
Gruba, N.; Rodriguez Martinez, J.I.; Grzywa, R.; Wysocka, M.; Skorenski, M.; Burmistrz, M.; Lecka, M.; Lesner, A.; Sienczyk, M.; Pyrc, K.
Substrate profiling of Zika virus NS2B-NS3 protease
FEBS Lett.
590
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Zika virus (Q32ZE1), Zika virus
brenda
Li, Y.; Phoo, W.W.; Loh, Y.R.; Zhang, Z.; Ng, E.Y.; Wang, W.; Keller, T.H.; Luo, D.; Kang, C.
Structural characterization of the linked NS2B-NS3 protease of Zika virus
FEBS Lett.
591
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2017
Zika virus
brenda
Yao, Y.; Huo, T.; Lin, Y.L.; Nie, S.; Wu, F.; Hua, Y.; Wu, J.; Kneubehl, A.R.; Vogt, M.B.; Rico-Hesse, R.; Song, Y.
Discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease
J. Am. Chem. Soc.
141
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2019
Dengue virus, West Nile virus, Zika virus
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Kouretova, J.; Hammamy, M.Z.; Epp, A.; Hardes, K.; Kallis, S.; Zhang, L.; Hilgenfeld, R.; Bartenschlager, R.; Steinmetzer, T.
Effects of NS2B-NS3 protease and furin inhibition on West Nile and Dengue virus replication
J. Enzyme Inhib. Med. Chem.
32
712-721
2017
Dengue virus, West Nile virus
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Skorenski, M.; Milewska, A.; Pyrc, K.; Sienczyk, M.; Oleksyszyn, J.
Phosphonate inhibitors of West Nile virus NS2B/NS3 protease
J. Enzyme Inhib. Med. Chem.
34
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2019
West Nile virus
brenda
Yotmanee, P.; Rungrotmongkol, T.; Wichapong, K.; Choi, S.B.; Wahab, H.A.; Kungwan, N.; Hannongbua, S.
Binding specificity of polypeptide substrates in NS2B/NS3pro serine protease of dengue virus type 2 A molecular dynamics study
J. Mol. Graph. Model.
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24-33
2015
Dengue virus type 2 (Q91H74), Dengue virus type 2 Thailand/NGS-C/1944 (Q91H74)
brenda
Phoo, W.W.; Li, Y.; Zhang, Z.; Lee, M.Y.; Loh, Y.R.; Tan, Y.B.; Ng, E.Y.; Lescar, J.; Kang, C.; Luo, D.
Structure of the NS2B-NS3 protease from Zika virus after self-cleavage
Nat. Commun.
7
13410
2016
Zika virus (H8XX12), Zika virus
brenda
Woestenenk, E.; Agback, P.; Unnerstale, S.; Henderson, I.; Agback, T.
Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR
Protein Expr. Purif.
140
16-27
2017
Dengue virus
brenda
Lei, J.; Hansen, G.; Nitsche, C.; Klein, C.D.; Zhang, L.; Hilgenfeld, R.
Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor
Science
353
503-505
2016
Zika virus (A0A140DLX4), Zika virus, Zika virus Brazilian isolate BeH823339 (A0A140DLX4)
brenda
Zhang, Z.; Li, Y.; Loh, Y.R.; Phoo, W.W.; Hung, A.W.; Kang, C.; Luo, D.
Crystal structure of unlinked NS2B-NS3 protease from Zika virus
Science
354
1597-1600
2016
Zika virus
brenda
Li, Y.; Zhang, Z.; Phoo, W.W.; Loh, Y.R.; Wang, W.; Liu, S.; Chen, M.W.; Hung, A.W.; Keller, T.H.; Luo, D.; Kang, C.
Structural dynamics of Zika virus NS2B-NS3 protease binding to dipeptide inhibitors
Structure
25
1242-1250
2017
Zika virus
brenda
Li, Y.; Zhang, Z.; Phoo, W.W.; Loh, Y.R.; Li, R.; Yang, H.Y.; Jansson, A.E.; Hill, J.; Keller, T.H.; Nacro, K.; Luo, D.; Kang, C.
Structural insights into the inhibition of Zika virus NS2B-NS3 protease by a small-molecule inhibitor
Structure
26
555-564.e3
2018
Zika virus
brenda
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