Information on EC 3.6.4.12 - DNA helicase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.4.12
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RECOMMENDED NAME
GeneOntology No.
DNA helicase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (DNA helix unwinding)
DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. Some of them unwind duplex DNA with a 3' to 5' polarity [1,3,5,8], others show 5' to 3' polarity [10,11,12,13] or unwind DNA in both directions [14,15]. Some helicases unwind DNA as well as RNA [9,10]. May be identical with EC 3.6.4.13 (RNA helicase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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dogfish
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Automatic Mining of ENzyme DAta
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replicase polyprotein 1ab
SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
gene 80
UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
salmon
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
shrimp
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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wild-type and mutant strains E233Sh (E233S double-crossover transformant generated with pMIDherA via herA downstream insertion, harboring the Tg arm pyrEF lacS Out-arm::In-arm), and mutant strain E233SherA (E233S with herA, herA on the complementing plasmid pSSR)
UniProt
Manually annotated by BRENDA team
wild-type and mutant strains E233Sh (E233S double-crossover transformant generated with pMIDherA via herA downstream insertion, harboring the Tg arm pyrEF lacS Out-arm::In-arm), and mutant strain E233SherA (E233S with herA, herA on the complementing plasmid pSSR)
UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
WNV
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
2'(3')-O-(N-methylanthraniloyl)ATP + H2O
2'(3')-O-(N-methylanthraniloyl)ADP + phosphate
show the reaction diagram
the fluorescent ATP analogue is used throughout all experiments to provide a complete ATPase cycle for a single nucleotide species
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2',3'-ATP + H2O
2',3'-ADP + phosphate
show the reaction diagram
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274% of the ability to support helicase catalyzed DNA unwinding compared to ATP
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2',3'-ddATP + H2O
2',3'-ddADP + phosphate
show the reaction diagram
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274% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
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2'-amino-ATP + H2O
2'-amino-ADP + phosphate
show the reaction diagram
2'-ara-ATP + H2O
2'-ara-ADP + phosphate
show the reaction diagram
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102% of the ability to support helicase catalyzed DNA unwinding compared to ATP
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?
2'-azido-ATP + H2O
2'-azido-ADP + phosphate
show the reaction diagram
2'-dATP + H2O
2'-dADP + phosphate
show the reaction diagram
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157% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
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?
2'-fluoro-ATP + H2O
2'-fluoro-ADP + phosphate
show the reaction diagram
2'-O-methyl-ATP + H2O
2'-O-methyl-ADP + phosphate
show the reaction diagram
2-amino-ATP + H2O
2-amino-ADP + phosphate
show the reaction diagram
3'-dATP + H2O
3'-dADP + phosphate
show the reaction diagram
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307% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
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ATP + H2O
ADP + phosphate
show the reaction diagram
CTP + H2O
CDP + phosphate
show the reaction diagram
dATP + H2O
ADP + phosphate
show the reaction diagram
dATP + H2O
dADP + phosphate
show the reaction diagram
dCTP + H2O
dCDP + phosphate
show the reaction diagram
dCTP + H2O
dCTP + phosphate
show the reaction diagram
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the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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dGTP + H2O
dGDP + phosphate
show the reaction diagram
dNTP + H2O
dNDP + phosphate
show the reaction diagram
dTTP + H2O
dTDP + phosphate
show the reaction diagram
dTTP + H2O
TDP + phosphate
show the reaction diagram
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helicase-catalyzed DNA unwinding by nonstructural protein 3 analyzed by molecular beacon-based helicase assay (MBHA), NTP binding occurs with similar affinities, dNTPs support faster DNA unwinding, dTTP supporting faster rates than any other canonical dNTP
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dUTP + H2O
dUDP + phosphate
show the reaction diagram
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GTP + H2O
GDP + phosphate
show the reaction diagram
N1-methyl-ATP + H2O
N1-methyl-ADP + phosphate
show the reaction diagram
N6-methyl-ATP + H2O
N6-methyl-ADP + phosphate
show the reaction diagram
NTP + H2O
NDP + phosphate
show the reaction diagram
TTP + H2O
TDP + phosphate
show the reaction diagram
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ability of various NTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay
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UTP + H2O
UDP + phosphate
show the reaction diagram
xanthosine 5'-triphosphate + H2O
xanthosine 5'-diphosphate + phosphate
show the reaction diagram
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7% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
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XTP + H2O
XDP + phosphate
show the reaction diagram
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7% of the ability to support helicase catalyzed DNA unwinding compared to ATP
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additional information
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