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Information on EC 3.4.22.B79 - nsP2 protease and Organism(s) Chikungunya virus and UniProt Accession Q8JUX6
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3.4.22.B79 nsP2 proteaseSpecify your search results
Word Map
- 3.4.22.B79
- polyproteins
- viruses
- alphavirus
-
chikungunya
-
replicase
-
sindbis
-
chikv
- nsp1
-
semliki
-
subgenomic
-
positive-stranded
-
venezuelan
-
hp-prrsv
-
papain-like
-
noncytopathic
-
plus-stranded
-
positive-sense
-
minus-strand
- analysis
-
3c-like
- drug development
-
autoprotease
- medicine
The taxonomic range for the selected organisms is: Chikungunya virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
the enzymes processes the alphavirus nonstructural polyprotein (nsP1234). The enzyme from Venezuelan equine encephalitis virus shwos a preferens for Gly or Als in position P1', Ala or Cys in P1, and Gly in P2
Synonyms
nonstructural protein 2, nonstructural polyprotein, nsp2 protease, nsp2 protein, nsp2pro, ns polyprotein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans + H2O
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGG + YIFSE-Edans
-
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGG + YIFSS-Edans
-
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGGYI-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGG + YI-Edans
peptide representing the 1/2 site of the polyprotein. Substrate is processed by nsP2, but the reaction velocity cannot be saturated
-
-
?
DABCYL-Arg-Ala-Gly-Gly-Tyr-Ile-Phe-Ser-(Glu-EDANS) + H2O
DABCYL-Arg-Ala-Gly-Gly + Tyr-Ile-Phe-Ser-(Glu-EDANS)
-
-
-
?
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
-
corresponds to cleavage site P1/2 of the polyprotein
-
-
?
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
-
corresponds to cleavage site P2/3 of the polyprotein
-
-
?
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
-
corresponds to cleavage site P3/4 of the polyprotein
-
-
?
additional information
?
-
-
chikungunya nsP2 protease possesses different substrate specificity to the canonical alphavirus nsP2 polyprotein cleavage specificity
-
-
?
additional information
?
-
protease readily cleaves GFP-10:5-Trx substrates containing short P10-P5' sequences originating from the 1/2 and 3/4 cleavage sites of the polyprotein, but not from the 2/3 site. Enzyme prefers the 3/4 substrate for cleavage in trans
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
stimulation with substrates 2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) and 2-(N-methylamino)benzoyl-AGGGIIETk(Dnp), inhibition with substrate 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5E)-6-(4-methoxyphenyl)-4-oxo-N-(2-phenylethyl)hex-5-enamide
topographical peptidomimetic, binds covalently leading to permanent enzyme inactivation via Michael adduct formation between the alpha/beta-unsaturated ketone functionality and the active site. 100% inhibition at 0.059 mg/ml, EC50 for cell-based assay 0.0089 mg/ml
(5E)-N-benzyl-4-oxo-6-phenylhex-5-enamide
topographical peptidomimetic, binds covalently leading to permanent enzyme inactivation via Michael adduct formation between the alpha/beta-unsaturated ketone functionality and the active site. 100% inhibition at 0.068 mg/ml, EC50 for cell-based assay 0.0088 mg/ml
Mg2+
-
stimulation with substrates 2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) and 2-(N-methylamino)benzoyl-AGGGIIETk(Dnp), inhibition with substrate 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
PMSF
-
PMSF does not affect activity when using 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) as a substrate. With 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp), PMSF shows no effect on truncated protease and 30% inhibition of full-length NSP2
Zinc acetate
almost complete inhibition at 2 mM, also significantly reduces the virus load in Vero cells
Cu2+
-
strong inhibition with substrate 2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
additional information
-
not inhibitory to full-length enzyme: NaCl up to 2 M, but 30-40% inhibition at 1 M with truncated protease
-
additional information
-
not inhibitory: leupeptin, E-64. Poor inhibitors: chymostatin, PMSF
-
additional information
not inhibitory: PMSF, trypsin protease inhibitor I, pepstatin, EDTA
-
additional information
-
not inhibitory: PMSF, trypsin protease inhibitor I, pepstatin, EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans
30°C, pH not specified in the publication
0.00098
DABCYL-Arg-Ala-Gly-Gly-Tyr-Ile-Phe-Ser-(Glu-EDANS)
pH 8.0, temperature not specified in the publication
0.01
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
wild-type, pH not specified in the publication, temperature not specified in the publication
0.029
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
mutant N547A, pH not specified in the publication, temperature not specified in the publication
0.00023
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00033
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00041
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00104
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00301
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0066
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0093
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.0364
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.00041
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00043
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0007
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.00077
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.00109
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00184
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0045
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0099
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.00016
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00058
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00072
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00076
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00086
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.00269
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0074
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.009
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00052
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00076
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00084
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00164
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0027
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.0032
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0033
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0046
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0013
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00142
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0021
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0024
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0029
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0031
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0034
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.0075
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.00068
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0011
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0013
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.0014
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0015
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0016
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0017
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0019
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
mutant N547A, pH not specified in the publication, temperature not specified in the publication
0.41
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
wild-type, pH not specified in the publication, temperature not specified in the publication
0.072
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.091
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.29
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.35
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.361
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.65
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.15
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.179
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.21
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
nsP2 inhibits cellular transcription by inducing rapid degradation of Rpb1, a catalytic subunit of the RNAPII complex. This degradation of Rpb1 is independent of the nsP2-associated protease activity, but, instead, it proceeds through nsP2-mediated Rpb1 ubiquitination. This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation
physiological function
physiological function
-
a serine that is close to the catalytical dyad is catalytically interchangeable with the dyad cysteine residue. The enzyme retains activity upon alanine replacement of either residue but a replacement of both cysteine and serine residues results in no detectable activity
physiological function
upon transfection of HeLa cells, 21 differentially regulated (six upregulated, 15 downregulated) spots are observed. Ubiquitin-conjugating enzyme UBE2L3 is downregulated. Transfection of full length UBE2L3 into HEK293T/17 cells prior to CHIKV infection reduces levels of infection but does not alter RNA genome levels
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 71000, nsP2 protease GST-fusion protein with a dual (His6-GST) affinity tag
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
in virus-infected cells, nsP2 can be glutathionylated at residues C175, C214, C313, C462, C698, C755. The glutathionylation of nsP2 impacts on the protease activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology model of nsP2 protein based on the crystal structure of the nsP2 protein of Venezuelan equine encephalitis virus and proposal of the the pharmacophore features that must be present in an inhibitor of nsP2 protease
molecular dynamics simulation and virtual screening of inhibitors based on PDB entry 3TRK leads to identification of top hit compounds, together with the five potential binding pockets of the nsP2 protease. Pocket 4 in the N-terminal domain of the nsP2 protease has been identified as the active site by the presence of catalytic residues, Cys1013 and His1083
molecular dynamics simulations and comparison with papain. The active site scaffold is the same in both the proteases. The two structurally identical segments in both the proteases show considerable difference in terms of their mobility
to 2.59 A resolution. Protein consists of an N-terminal protease subdomain and a C-terminal methyltransferase subdomain. The substrate binding cleft is present at the interface of two subdomains. Access to the active site and substrate binding cleft is blocked by a flexible interdomain loop. This loop contains His548, the catalytic residue, and Trp549 and Asn547, the residues predicted to bind substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C478A
S482A
W479A
mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
W549A
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
W549F
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
additional information
-
preparation of both full length and a truncated protease domain from the C-terminus of the nsP2 protein. The protease domain alone has different properties compared with the full length nsP2 protease
C478A
residue Cys478 in the active site of CHIKV nsP2 is indispensable for polyprotein P1234 processing. Mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
C478A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
S482A
mutation has almost no negative effect on the protease activity
S482A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
10 min, 50.4% residual activity for wild-type, 53% for mutant C478A, 50.4% for mutant S482A, 52.9% for mutant W549A, 54% for mutant W549F
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Proteins are expressed as inclusion bodies under culturing at 37°C, and only partially expressed in a soluble form at 22°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
nsP2 protease-based cell free high throughput screening assay
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nguyen, P.; Yu, H.; Keller, P.
Identification of chikungunya virus nsP2 protease inhibitors using structure-base approaches
J. Mol. Graph. Model.
57
1-8
2015
Chikungunya virus (Q8JUX6), Chikungunya virus, Chikungunya virus S27 (Q8JUX6)
Singh, K.; Kirubakaran, P.; Nagarajan, S.; Sakkiah, S.; Muthusamy, K.; Velmurgan, D.; Jeyakanthan, J.
Homology modeling, molecular dynamics, e-pharmacophore mapping and docking study of Chikungunya virus nsP2 protease
J. Mol. Model.
18
39-51
2012
Chikungunya virus (Q8JUX6), Chikungunya virus, Chikungunya virus S27 (Q8JUX6)
Akhrymuk, I.; Kulemzin, S.V.; Frolova, E.I.
Evasion of the innate immune response: the Old World alphavirus nsP2 protein induces rapid degradation of Rpb1, a catalytic subunit of RNA polymerase II
J. Virol.
86
7180-7191
2012
Chikungunya virus (Q8JUX6), Chikungunya virus, Semliki forest virus (P08411), Sindbis virus
Saisawang, C.; Kuadkitkan, A.; Smith, D.R.; Ubol, S.; Ketterman, A.J.
Glutathionylation of chikungunya nsP2 protein affects protease activity
Biochim. Biophys. Acta
1861
106-111
2017
Chikungunya virus
El-labbad, E.M.; Ismail, M.A.; Abou Ei Ella, D.A.; Ahmed, M.; Wang, F.; Barakat, K.H.; Abouzid, K.A.
Discovery of novel peptidomimetics as irreversible CHIKV NsP2 protease inhibitors using quantum mechanical-based ligand descriptors
Chem. Biol. Drug Des.
86
1518-1527
2015
Chikungunya virus (C8YZ72), Chikungunya virus, Chikungunya virus 899 (C8YZ72)
Ramakrishnan, C.; Kutumbarao, N.H.V.; Suhitha, S.; Velmurugan, D.
Structure-function relationship of Chikungunya nsP2 protease A comparative study with papain
Chem. Biol. Drug Des.
89
772-782
2017
Chikungunya virus (Q8JUX6), Chikungunya virus, Chikungunya virus S27-African prototype (Q8JUX6)
Narwal, M.; Singh, H.; Pratap, S.; Malik, A.; Kuhn, R.J.; Kumar, P.; Tomar, S.
Crystal structure of chikungunya virus nsP2 cysteine protease reveals a putative flexible loop blocking its active site
Int. J. Biol. Macromol.
116
451-462
2018
Chikungunya virus (Q8JUX6), Chikungunya virus, Chikungunya virus S27-African prototype (Q8JUX6)
Ramphan, S.; Khongwichit, S.; Saisawang, C.; Kovanich, D.; Ketterman, A.J.; Ubol, S.; Auewarakul, P.; Roytrakul, S.; Smith, D.R.; Kuadkitkan, A.
Ubiquitin-conjugating enzyme E2 L3 is downregulated by the chikungunya virus nsP2 protease
Proteomics Clin. Appl.
12
e1700020
2018
Chikungunya virus (A0A0E3MZW7), Chikungunya virus
Saisawang, C.; Saitornuang, S.; Sillapee, P.; Ubol, S.; Smith, D.; Ketterman, A.
Chikungunya nsP2 protease is not a papain-like cysteine protease and the catalytic dyad cysteine is interchangeable with a proximal serine
Sci. Rep.
5
17125
2015
Chikungunya virus, Chikungunya virus ECSA E1:226V
Rausalu, K.; Utt, A.; Quirin, T.; Varghese, F.S.; Zusinaite, E.; Das, P.K.; Ahola, T.; Merits, A.
Chikungunya virus infectivity, RNA replication and non-structural polyprotein processing depend on the nsP2 proteases active site cysteine residue
Sci. Rep.
6
37124
2016
Chikungunya virus (Q1W368), Chikungunya virus ECSA (Q1W368)
Saha, A.; Acharya, B.; Priya, R.; Tripathi, N.; Shrivastava, A.; Rao, M.; Kesari, P.; Narwal, M.; Tomar, S.; Bhagyawant, S.; Parida, M.; Dash, P.
Development of nsP2 protease based cell free high throughput screening assay for evaluation of inhibitors against emerging Chikungunya virus
Sci. Rep.
8
10831
2018
Chikungunya virus (C7S7A0), Chikungunya virus
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