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

BRENDA support

Literature summary extracted from

  • Lescar, J.; Luo, D.; Xu, T.; Sampath, A.; Lim, S.P.; Canard, B.; Vasudevan, S.G.
    Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target (2008), Antiviral Res., 80, 94-101.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.6.4.13 drug development the multifunctional NS3 protein from Dengue virus is a target for the design of antiviral inhibitors Dengue virus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.4.13 benzoyl-Nle-Lys-Arg-Arg competitive inhibition, structure-activity relationship Dengue virus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.13 Mg2+ can be substituted by a Mn2+ ion for the enzymatic reaction Dengue virus
3.6.4.13 Mn2+ can substitute for a Mg2+ ion in the enzymatic reaction Dengue 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 Dengue virus The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.13 Dengue virus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.13 ATP + H2O ATPase activity, ATP binding mode, the ATP binding site is housed between these two subdomains. In the ATP binding pocket, a Mg ion is coordinated in a octahedral manner by the beta- and gamma-phosphate oxygen atoms from ATP, two equatorial water molecules and oxygen atoms from residues Glu285 in motif II, and Thr200 in motif I, overview Dengue virus ADP + phosphate
-
 ?
3.6.4.13 additional information The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins Dengue virus ?
-
 ?
3.6.4.13 additional information the C-terminal region of NS3 forms the RNA helicase domain, an ATP-driven molecular motor Dengue virus ?
-
 ?
3.6.4.13 RNA + H2O RNA helicase actiivty Dengue virus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.4.13 More the C-terminal region of NS3 forms the RNA helicase domain. The ATP binding site is housed between these two subdomains, structure modelling, overview Dengue virus

Synonyms

EC Number Synonyms Comment Organism
3.6.4.13 ATPase
-
 Dengue virus
3.6.4.13 ATPase/helicase
-
 Dengue virus
3.6.4.13 non-structural 3
-
 Dengue virus
3.6.4.13 NS3
-
 Dengue virus
3.6.4.13 RTPase
-
 Dengue virus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.6.4.13 0.007
-
 benzoyl-Nle-Lys-Arg-Arg full-length enzyme in presence of cofactor CF40-Gly4-Ser-Gly4-NS3FL Dengue virus