Information on EC 3.6.1.B17 - ATP-independent RNA helicase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.B17
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
ATP-independent RNA helicase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
In vitro the enzyme unwinds double-strandet RNA independently of ATP
show the reaction diagram
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-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene AtRH57
UniProt
Manually annotated by BRENDA team
gene AtRH57
UniProt
Manually annotated by BRENDA team
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U87411
UniProt
Manually annotated by BRENDA team
-
U87411
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
CTP + H2O
CDP + phosphate
show the reaction diagram
U87411
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-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
U87411
required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Single-stranded RNA
U87411
viral ATPases, including NS3 from flaviviruses, are stimulated by single-stranded RNA. At RNA saturation, an increase of 13.5fold and 9.6fold is achieved with respect to the basal activities for recombinant mutant NS3-FL and NS3-hel, respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 0.031
ATP
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 2.8
ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
U87411
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
U87411
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparison of crystal structures of the full-length NS3 from Dengue virus and Hepatitis C virus indicates a major difference in the relative orientations between the protease and helicase domains in the two proteins. Specifically, a beta-strand in the HCV NS3 clamps the protease domain next to the helicase domain, thereby creating a compact conformational state that differs from the extended conformation observed in the DENV protein
U87411
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta pLac by nickel affinity chromatography, dialysis, and ultrafiltration
U87411
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene AtRH57, quantitative RT-PCR enzyme expression analysis, overexpression of His-tagged enzyme in Escherichia coli, transient recombinant expression of EGFP-tagged enzyme in onion cells in the nucleus and nucleolus
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rosetta pLac
U87411
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcript of AtRH57 is significantly induced by abscisic acid, high Glc and salt
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D284A/E285A
U87411
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
U87411
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