3.6.1.B17: ATP-independent RNA helicase
This is an abbreviated version!
For detailed information about ATP-independent RNA helicase, go to the full flat file.
Word Map on EC 3.6.1.B17
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3.6.1.B17
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dengue
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nonstructural
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unwind
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poliovirus
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capsid
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enteroviruses
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replicons
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uncoating
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encapsidation
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anti-denv
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picornaviridae
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flaviviridae
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vp3
- 3.6.1.B17
- dengue
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nonstructural
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unwind
- poliovirus
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capsid
- enteroviruses
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replicons
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uncoating
-
encapsidation
-
anti-denv
- picornaviridae
- flaviviridae
- vp3
Reaction
In vitro the enzyme unwinds double-strandet RNA independently of ATP =
Synonyms
2CATPase, ATP-independent RNA annealing activity, ATP-independent RNA helicase, AtRH57, DEAD-box RNA helicase, DENV helicase, DENV NS3, nonstructural protein 3, NS3, NS3 helicase, p41, protein NS3, Prp28
ECTree
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Substrates Products
Substrates Products on EC 3.6.1.B17 - ATP-independent RNA helicase
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REACTION DIAGRAM
RNA hybrid helix + H2O
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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
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purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
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additional information
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purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
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additional information
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purified recombinant AtRH57-His protein unwinds double-stranded RNA independently of ATP in vitro, the enzyme AtRH57 might be an ATP-independent RNA helicase
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additional information
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the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
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additional information
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the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
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additional information
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enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
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additional information
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enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
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additional information
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the enzyme preferentially binds single-stranded RNA, while showing low affinity for single or double-stranded DNA (dsDNA) molecules. In addition, enzyme DENV NS3 unwinds RNA duplexes with a 3' to 5' directionality, moving along a tracking RNA strand. The DENV enzyme displays low processivity, unwinds dsDNA molecules inefficiently, and exhibits an RNA triphosphatase activity. In contrast to the requirements for the helicase activity, the RNA annealing activity does not require ATP. Viral enzyme NS3 modulates viral and non-viral RNA structures
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additional information
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enzyme DENV NS3 contains ATP-dependent RNA helicase activity and ATP-independent RNA strand annealing activity, it establishes an ATP-dependent steady-state between RNA unwinding and strand annealing
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additional information
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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
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additional information
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the enzyme has both ATP-dependent RNA helicase activity that unwinds RNA helices from both 5'->3' and 3'->5' directions and ATP-independent RNA-chaperoning activity that can remodel structured RNAs and facilitate strand annealing. Moreover, the enzyme can facilitate viral RNA synthesis in vitro by norovirus polymerase
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