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Literature summary for 3.6.1.B17 extracted from

  • Xia, H.; Wang, P.; Wang, G.C.; Yang, J.; Sun, X.; Wu, W.; Qiu, Y.; Shu, T.; Zhao, X.; Yin, L.; Qin, C.F.; Hu, Y.; Zhou, X.
    Human enterovirus nonstructural protein 2CATPase functions as both an RNA helicase and ATP-independent RNA chaperone (2015), PLoS Pathog., 11, e1005067 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.B17

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli or baculovirus-infected Sf9 insect cells Enterovirus A71

Inhibitors

Inhibitors Comment Organism Structure
Mn2+ 2.5 mM Mn2+ blocks the helix unwinding by the enzyme Enterovirus A71
Zn2+ 0.5 mM Zn2+ completely blocks the helix unwinding by the enzyme Enterovirus A71

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme requires the presence of Mg2+ to reach its optimal unwinding activity, it is still able to unwind a portion of the RNA helix in the absence of Mg2+ or any divalent ions Enterovirus A71
additional information 2.5 mM Ca2+ is dispensable for the helix unwinding activity of the enzyme Enterovirus A71

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
600000
-
 gel filtration Enterovirus A71

Organism

Organism UniProt Comment Textmining
Enterovirus A71
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylase affinity column chromatography Enterovirus A71

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA hybrid helix + H2O least efficient substrate Enterovirus A71 ?
-
 ?
additional information the enzyme functions not only as an RNA helicase that 3'-to-5' unwinds RNA and DNA helices in an ATP-dependent manner, but also as an RNA chaperone that destabilizes helices bidirectionally and facilitates strand annealing and complex RNA structure formation independently of ATP Enterovirus A71 ?
-
-
RNA hybrid helix + H2O although the the enzyme unwinds the 3'-protruded helix in an ATP-dependent manner, it unwinds the 5'-protruded helix exactly like an RNA chaperone, which is able to unwind the helix in the absence of ATP, and increasing ATP concentrations cannot further enhance the helix unwinding Enterovirus A71 ?
-
 ?
RNA-DNA hybrid with longer DNA strand + H2O
-
 Enterovirus A71 ?
-
 ?
RNA-DNA hybrid with longer RNA strand + H2O
-
 Enterovirus A71 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 85000, recombinant enzyme, SDS-PAGE Enterovirus A71

Synonyms

Synonyms Comment Organism
2CATPase functions as both an RNA helicase and ATP-independent RNA chaperone Enterovirus A71

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Enterovirus A71

General Information

General Information Comment Organism
malfunction when the enzyme helicase activity is impaired, enterovirus 71 RNA replication and virion production are mostly abolished in cells Enterovirus A71
physiological function enzyme-mediated RNA remodeling plays a critical role in the enteroviral life cycle Enterovirus A71