Information on EC 3.6.4.12 - DNA helicase and Organism(s) Drosophila melanogaster

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The taxonomic range for the selected organisms is: Drosophila melanogaster

The enzyme appears in selected 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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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
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
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RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 10% of the efficiency obtained with dATP
-
-
?
dATP + H2O
ADP + phosphate
show the reaction diagram
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. Unwinding of longer partial duplex DNA substrates requires a higher protein concentration than does unwinding of the 20bp partial duplex substrate. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. dATP is most effective. ATP supports helicase reaction with 45% of the efficiency obtained with dATP. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the ATPase activity of the protein
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 30% of the efficiency obtained with dATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 35% of the efficiency obtained with dATP
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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divalent cation required, optimum concentration: 0.5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed
dATP
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substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed
NaCl
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above 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
single-stranded DNA binding protein dRP-A
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stimulates the activity on substrates with more than 300 nucleotides double-stranded region
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
ATP
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pH 8.0, 30°C, in presence of ssDNA
0.25
dATP
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pH 8.0, 30°C, in presence of ssDNA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 15
ATP
0.25 - 23
dATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
P02299
Drosophila melanogaster;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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x * 54000, small isoform of RECQ5 helicase, SDS-PAGE
200000
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gel filtration, glycerol gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 54000, small isoform of RECQ5 helicase, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme recombinantly expressed in Escherichia coli
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