3.4.22.B79: nsP2 protease
This is an abbreviated version!
For detailed information about nsP2 protease, go to the full flat file.
Word Map on EC 3.4.22.B79
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3.4.22.B79
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polyproteins
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viruses
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alphavirus
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chikungunya
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replicase
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sindbis
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chikv
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nsp1
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semliki
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subgenomic
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positive-stranded
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venezuelan
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hp-prrsv
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papain-like
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noncytopathic
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plus-stranded
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positive-sense
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minus-strand
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analysis
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3c-like
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drug development
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autoprotease
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medicine
- 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
Reaction
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
non-structural polyprotein 2, nonstructural polyprotein, nonstructural protein, nonstructural protein 2, ns polyprotein, nsP2, nsP2 protease, nsp2 protein, nsp2pro, p39 nsp2 protease
ECTree
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Inhibitors
Inhibitors on EC 3.4.22.B79 - nsP2 protease
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(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
E64d
inhibitor binds beneath a beta-hairpin at the interface of the SAM MTase and protease domains
Mg2+
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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
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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
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strong inhibition with substrate 2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
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activity is reduced by approximately 20fold in the presence of 5% glycerol
glycerol
activity is reduced by approximately 20fold in the presence of 5% glycerol
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not inhibitory: leupeptin, E-64. Poor inhibitors: chymostatin, PMSF; not inhibitory to full-length enzyme: NaCl up to 2 M, but 30-40% inhibition at 1 M with truncated protease
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additional information
not inhibitory: PMSF, trypsin protease inhibitor I, pepstatin, EDTA
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additional information
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not inhibitory: PMSF, trypsin protease inhibitor I, pepstatin, EDTA
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additional information
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dithiothreitol and tris (2-carboxyethyl) phosphine hydrochloride have no discernable effect on the activity up to 5 mM. The enzyme is able to tolerate up to 10 mM of beta-mercaptoethanol
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additional information
nsp2pro can tolerate EDTA up to 10 mM with very little effect. Dithiothreitol and tris (2-carboxyethyl) phosphine hydrochloride have no discernable effect on the activity up to 5 mM. The enzyme is able to tolerate up to 10 mM of beta-mercaptoethanol
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additional information
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nsp2pro can tolerate EDTA up to 10 mM with very little effect. Dithiothreitol and tris (2-carboxyethyl) phosphine hydrochloride have no discernable effect on the activity up to 5 mM. The enzyme is able to tolerate up to 10 mM of beta-mercaptoethanol
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additional information
E64c, the carboxylic acid form of the E64d ester, does not inhibit the nsP2 protease
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additional information
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E64c, the carboxylic acid form of the E64d ester, does not inhibit the nsP2 protease
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