EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
   3.6.4.13 | -999 |
- |
biochemical properties and enzymatic activity of the RNA-helicase domain, functional characterization to get information about the flavivirus replication mechanism, NTPase-deficient mutant generated, RNA binding features, electrostatic interaction with RNA, basal ATPase activity insensitive to high ionic strength |
697955 |
| 3.6.4.13 | -999 |
- |
development of continuous fluorescence assay based on fluorescence resonance energy transfer for the monitoring of RNA helicase activity in vitro. This assay will be useful for monitoring the detailed kinetics of RNA unwinding mechanisms and screening RNA helicase inhibitors at high throughput |
711089 |
| 3.6.4.13 | -999 |
- |
helicase capable of unwinding duplex RNA or DNA, ambiguous |
693688 |
| 3.6.4.13 | -999 |
- |
overview of sequences of NTPase/helicase motifs VI derived peptides and their deleted derivatives, kinetic analyses reveals that binding of the peptides do not interfere with the NTPase activity, peptides do not interact with the ATP binding site |
696133 |
| 3.6.4.13 | -999 |
- |
RNA replication, RNA protection, spherule formation size, relative ATPase activity, RNA accumulation and stabilization, of wild-type and mutant enzymes, overview |
670083 |
| 3.6.4.13 | -999 |
- |
specificities and activities of wild-type and mutant enzymes |
669358 |
| 3.6.4.13 | -999 |
- |
structural characterization of catalytic domain, mutation analysis of residue substitution in the Walker A motif (Gly199, Lys200 and Thr201), within the NTP-binding pocket (Gln457, Arg461 and Arg464) and of Arg458 in the outside of the pocket in the motif IV, residues crucial for ATPase and RNA helicase activities and virus replication, Lys200 cannot be substituted by other residues to establish sufficient activities, structure of the NTP-binding pocket well conserved among the viruses of the Flaviviridae |
690191 |
| 3.6.4.13 | -999 |
- |
structural characterization of the C-terminal portion containing the ATPase/helicase domain, encompasses residues 181-619, monomer structure determined by analytical centrifugation and gel filtration, SDS-PAGE and immunoblotting, structure determined by circular dichroism and fluorescence spectroscopy, ATPase activity stimulated by RNA and ssDNA, no RNA helicase activity at protein concentrations up to 500 nM, linker region between the protease and the helicase domains predicted as a prerequisite for protein-protein interactions leading to the formation of the active oligomer |
701395 |
| 3.6.4.13 | -999 |
- |
structure of nucleic base and ribose fragment of NTP molecule has a slight effect on inhibitory properties |
696161 |
| 3.6.4.13 | -999 |
- |
surface of domain 2 of the NS3 NTPase/helicase in direct vicinity to a flexible loop that is localized between Val1458 and Thr1476, accessibility of the Arg-rich amino acid motif by this loop for protein kinase C inhibition analyzed, two variants of domain 2 generated, in vitro protein kinase C (PKC) phosphorylation studies, binding and competition assays, modelling of ribbon diagrams, presence of the intact loop abolishes the binding of domain 2 to a tailed duplex RNA, binding of dsDNA not affected, loop structure reduces the extent of inhibition of protein kinase C (PKC) by domain 2 and regulates the binding of dsRNA, various mechanisms by which the NS3 protein perturb signal transduction in infected cells |
696490 |
