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
-
nonstructural
-
unwind
- poliovirus
-
capsid
- enteroviruses
-
replicons
-
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
3.6.1.B17 ATP-independent RNA helicaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.6.1.B17 - ATP-independent RNA helicase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D284A/E285A
site-directed mutagenesis, inactive mutant showing no ATP hydrolysis. A mutant NS3-hel carrying a two amino acid substitution (D284A-E285A) in the conserved motif II, which corresponds to the Mg2+ co-factor binding loop
H51A
site-directed mutagenesis, the mutation in the protease catalytic site abolishes autoproteolysis of the enzyme
D284A/E285A
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site-directed mutagenesis, inactive mutant showing no ATP hydrolysis. A mutant NS3-hel carrying a two amino acid substitution (D284A-E285A) in the conserved motif II, which corresponds to the Mg2+ co-factor binding loop
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H51A
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site-directed mutagenesis, the mutation in the protease catalytic site abolishes autoproteolysis of the enzyme
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additional information
additional information
construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
additional information
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construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
additional information
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construction of enzyme-deficient mutant rh57-1, the mutant is affected in the glucose metabolism and shows reduced function of protein synthesis, rh57-1 mutants show resistance to antibiotics, phenotypes, overview
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additional information
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
additional information
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generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
additional information
-
generation of two recombinant variants of DENV NS3: the first single polypeptide mimics the NS2B-NS3 complex containing the full-length NS3 (618 amino acids) linked to the NS2B hydrophilic region (47 amino acids), this variant named NS3-FL, also carried a mutation in the protease catalytic site (H51A) to avoid autoproteolysis. The second variant NS3-hel represents a truncated NS3, containing the helicase domain (amino acids 171 to 618), ATPase/helicase defective NS3-hel mutant (NS3Amut) conserves the RNA annealing activity
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