Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wen, G.; Xue, J.; Shen, Y.; Zhang, C.; Pan, Z.
    Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase (2009), Virus Res., 141, 63-70.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.13 additional information the NS3 protease domain enhances the helicase activity of NS3 but has no effect on its NTPase activity. For the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B Classical swine fever virus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.13 expression of wild-type and mutant His-tagged NS3 helicase domain in Escherichia coli Classical swine fever virus

Protein Variants

EC Number Protein Variants Comment Organism
3.6.4.13 K232A site-directed mutagenesis in the helicase domain of NS3 Classical swine fever virus
3.6.4.13 additional information for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B Classical swine fever virus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.13 Mg2+ activates Classical swine fever virus
3.6.4.13 Mg2+ the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+ Classical swine fever virus
3.6.4.13 Mn2+ the helicase activity requires divalent ions. Mn2+ is preferred over Mg2+ Classical swine fever virus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.13 additional information Classical swine fever virus NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules ?
-
?
3.6.4.13 additional information Classical swine fever virus CSFV NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.13 Classical swine fever virus
-
-
-
3.6.4.13 Classical swine fever virus Q9YS30 CSFV
-
3.6.4.13 Classical swine fever virus CSFV Q9YS30 CSFV
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.13 ATP + H2O
-
Classical swine fever virus ADP + phosphate
-
?
3.6.4.13 ATP + H2O helicase activity requires the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. CSFV NS3 helicase activity requires a longer 3'-end single-stranded overhang for efficient duplex unwinding and the directionality of NS3 helicase unwinding is 3' to 5' with respect to the template strand Classical swine fever virus ADP + phosphate
-
?
3.6.4.13 ATP + H2O
-
Classical swine fever virus CSFV ADP + phosphate
-
?
3.6.4.13 CTP + H2O helicase activity is about 85% of the activity with ATP Classical swine fever virus CDP + phosphate
-
?
3.6.4.13 dATP + H2O helicase activity is about 10% of the activity with ATP Classical swine fever virus dADP + phosphate
-
?
3.6.4.13 dCTP + H2O helicase activity is about 25% of the activity with ATP Classical swine fever virus dCDP + phosphate
-
?
3.6.4.13 dGTP + H2O helicase activity is about 10% of the activity with ATP Classical swine fever virus dGDP + phosphate
-
?
3.6.4.13 dTTP + H2O helicase activity is about 55% of the activity with ATP Classical swine fever virus dTDP + phosphate
-
?
3.6.4.13 GTP + H2O helicase activity is about 55% of the activity with ATP Classical swine fever virus GDP + phosphate
-
?
3.6.4.13 additional information nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus Classical swine fever virus ?
-
?
3.6.4.13 additional information NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules Classical swine fever virus ?
-
?
3.6.4.13 additional information NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules Classical swine fever virus CSFV ?
-
?
3.6.4.13 RNA + H2O NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview Classical swine fever virus ?
-
?
3.6.4.13 RNA + H2O NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview Classical swine fever virus CSFV ?
-
?
3.6.4.13 UTP + H2O helicase activity is about 55% of the activity with ATP Classical swine fever virus UDP + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.6.4.13 nonstructural protein 3
-
Classical swine fever virus
3.6.4.13 NS3
-
Classical swine fever virus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.13 37
-
assay at Classical swine fever virus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.4.13 6.5
-
ATPase assay at Classical swine fever virus
3.6.4.13 7.5
-
-
Classical swine fever virus
3.6.4.13 7.5
-
RNA helicase assay at Classical swine fever virus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.6.4.13 6.5
-
pH 6.5: about 50% of maximal activity, pH 8: about 80% of maximal activity Classical swine fever virus