Information on EC 3.6.4.12 - DNA helicase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.6.4.12
-
RECOMMENDED NAME
GeneOntology No.
DNA helicase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
-
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
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; recombinant HCV helicase constructs, nonstructural protein 3
-
-
Manually annotated by BRENDA team
subtype 1b
SwissProt
Manually annotated by BRENDA team
viral genotype 1a, version H77
-
-
Manually annotated by BRENDA team
replicase polyprotein 1ab
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii DSM 12428
-
SwissProt
Manually annotated by BRENDA team
replicase polyprotein 1ab
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
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
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
Sulfolobus tokodaii DSM 16993
-
SwissProt
Manually annotated by BRENDA team
West Nile virus WNV
WNV
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
HDHB knockdown impairs recovery from replication stress
malfunction
-
in Pfh1-deficient cells X-shaped molecules accumulate at replication termination sites. Physical evidence is provided that these X-shaped molecules are converging replication forks and show that they accumulate even at replication fork barriers where Pfh1 does not perform its sweepase function
malfunction
Q384Y1
RNAi of TbPIF1 causes a growth defect and kinetoplast DNA loss. Minicircle replication intermediates decrease during RNAi, and there is an accumulation of multiply interlocked, covalently closed minicircle dimers (fraction U)
malfunction
F0NFK8
gene knockout (herA) cells generated from the herA merodiploid cells fail to form colonies in the presence of 5-fluoroorotic acid. Helicase HerA is essential for cell viability
malfunction
-
gene knockout (herA) cells generated from the herA merodiploid cells fail to form colonies in the presence of 5-fluoroorotic acid. Helicase HerA is essential for cell viability
-
physiological function
-
cellular exposure to UV irradiation, camptothecin, or hydroxyurea induces accumulation of HDHB on chromatin in a dose- and time-dependent manner, preferentially in S phase cells. Replication stress-induces recruitment of HDHB to chromatin is independent of checkpoint signaling but correlates with the level of replication protein A recruited to chromatin
physiological function
-
in Sulfolobus acidocaldarius, the Mre11 protein and the RadA recombinase might play an active role in the repair of DNA damage introduced by gamma rays and/or may act as DNA damage sensors. The functional interaction between Mre11, Rad50 and the HerA helicase suggest that each protein play different roles when acting on its own or in association with its partners. Interaction of the Mre11 protein with both Rad50 and the HerA bipolar helicase
physiological function
-
Pfh1 promotes fork merging at replication termination sites
physiological function
Q384Y1
TbPIF1 functions in minicircle replication
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
physiological function
Q974S1
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
physiological function
D0KN27
one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates
physiological function
Sulfolobus tokodaii DSM 16993
-
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
-
physiological function
-
one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
P56255
the fluorescent ATP analogue is used throughout all experiments to provide a complete ATPase cycle for a single nucleotide species
-
-
?
2',3'-ATP + H2O
2',3'-ADP + phosphate
show the reaction diagram
-
274% of the ability to support helicase catalyzed DNA unwinding compared to ATP
-
-
?
2',3'-ddATP + H2O
2',3'-ddADP + phosphate
show the reaction diagram
-
274% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2'-amino-ATP + H2O
2'-amino-ADP + phosphate
show the reaction diagram
-
28% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 28% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2'-ara-ATP + H2O
2'-ara-ADP + phosphate
show the reaction diagram
-
102% of the ability to support helicase catalyzed DNA unwinding compared to ATP
-
-
?
2'-azido-ATP + H2O
2'-azido-ADP + phosphate
show the reaction diagram
-
61% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 61% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2'-dATP + H2O
2'-dADP + phosphate
show the reaction diagram
-
157% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2'-fluoro-ATP + H2O
2'-fluoro-ADP + phosphate
show the reaction diagram
-
145% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 145% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2'-O-methyl-ATP + H2O
2'-O-methyl-ADP + phosphate
show the reaction diagram
-
34% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 34% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
2-amino-ATP + H2O
2-amino-ADP + phosphate
show the reaction diagram
-
78% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 78% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
3'-dATP + H2O
3'-dADP + phosphate
show the reaction diagram
-
307% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P04014
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P07271
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P20356
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P15043
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q6Y5A8
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9H611
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P46063
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8I3W6
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q12039
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8VID5
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9WY48
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q06218
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P56255
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9BX63
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8U3I4
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
D0KN27
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q14191
3'-5' helicase activity. WRN helicase is involved in preserving DNA integrity during replication. It is proposed that WRN helicase can function in coordinating replication fork progression with replication stress-induced fork remodeling
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UUA2
5' to 3' DNA helicase. ATPase/helicase activity of Pfh1p is essential. Maintenance of telomeric DNA is not the sole essential function of Pfh1p. Although mutant spores depleted for Pfh1p proceed through S phase, they arrest with a terminal cellular phenotype consistent with a postinitiation defect in DNA replication. Telomeric DNA is modestly shortened in the absence of Pfh1p
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P07271
5' to 3' DNA helicase. The ATPase/helicase activity of Rrm3p is required for its role in telomeric and subtelomeric DNA replication. Because Rrm3p is telomere-associated in vivo, it likely has a direct role in telomere replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
A8D930
AvDH1 belonging to the DEAD-box helicase family is induced by salinity, functions as a typical helicase to unwind DNA and RNA, and may play an important role in salinity tolerance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q12039
DNA helicase Hmi1p is involved in the maintenance of mitochondrial DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UXG1
during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O24736
helicase UvrD protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8I3W6
helicases play an essential role in nearly all the nucleic acid metabolic processes, catalyzing the transient opening of the duplex nucleic acids in an ATP-dependent manner
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q6Y5A8
involved in DNA recombination, repair and genome stability maintenance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P51979
meiosis-specific MER3 protein is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8DPU8
PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q19546
the ability of CeWRN-1 to unwind DNA structures may improve the access for DNA repair and replication proteins that are important for preventing the accumulation of abnormal structures, contributing to genomic stability
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide, suggesting a role of the enzyme in Okazaki fragment processing. The ability of the enzyme to target DNA replication/repair intermediates may be relevant to its role in genome stability maintenance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is the helicase at the mitochondrial DNA replication fork
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q14191
3'-5' helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UUA2
5' to 3' DNA helicase
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
5'-3' unwinding activity, enzymatic functions of the two subunit helicase-primase complex (enzyme complex consisting of UL5 and UL52 gene functions): DNA-dependent ATPase, DNA primase, and DNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P03018
as a DNA-dependent ATPase, helicase II translocates processively along single-stranded DNA. The translocation of helicase II along single-stranded DNA is unidirectional and in th 3 to 5 direction with respect to the DNA strand on which the enzyme is bound
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP hydrolysis is required for unwinding of DNA catalyzed by the DNA helicase, the enzyme moves in the 5 to 3 direction on a single-stranded DNA to catalyze unwinding of double-stranded regions of DNA in the 3' to 5' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP is the most active NTP. DNA helicase unwinds DNA unidirectionally from 3 to 5. DNA helicase can unwind a 17-bp duplex whether it has unpaired single-stranded tails at both the 5 end and 3 end, at the 5 end or at the 3 end only, or at neither end. However, it fails to act on a blunt-ended 17-bp duplex DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q19546
ATP-dependent 3' to 5' helicase capable of unwinding a variety of DNA structures such as forked duplexes, Holliday junctions, bubble substrates, D-loops, and flap duplexes, and 3'-tailed duplex substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. ATP binding enhances DNA binding by the helicase. ATPase activity is substantially enhanced in presence of DNA. MCM protein binds DNA ends better than long circular substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UXG1
ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. Very limited stimulation of its ATPase activity by DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent DNA unwinding enzyme. HDH VI unwinds exclusively DNA duplexes with an annealed portion smaller than32 bp and prefers a replication fork-like structure of the substrate. It cannot unwind blunt-end duplexes and is inactive also on DNA-RNA or RNA-RNA hybrids. HDH VI unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand. ATP and dATP are equally good substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O14867
BACH1 preferentially binds and unwinds a forked duplex substrate compared with a duplex flanked by only one single-stranded DNA (ssDNA) tail. BACH1 helicase requires a minimal 5' ssDNA tail of 15 nucleotides for unwinding of conventional duplex DNA substrates. However, the enzyme is able to catalytically release the third strand of the homologous recombination intermediate D-loop structure irrespective of DNA tail status. In contrast, BACH1 completely fails to unwind a synthetic Holliday junction structure. Moreover, BACH1 requires nucleic acid continuity in the 5' ssDNA tail of the forked duplex substrate within six nucleotides of the ssDNA-dsDNA junction to initiate efficiently DNA unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
BcMCM displays 3' to 5' helicase and ssDNA-stimulated ATPase activity. BcMCM is an active ATPase, and this activity is restricted to the MCM-AAA module
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q06218
Dbp9p exhibits DNA-DNA and DNA-RNA helicase activity in the presence of ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
Dhel I moves 5' to 3' on the DNA strand to which it is bound. Unwinding activity decreases with increasing length of the double-stranded region suggesting a distributive mode of action. ATP and dATP are the only nucleoside-5'-triphosphates that support the strand displacement reaction. Both have an optimal concentration range between 1 and 2 mM
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P40562
DNA helicase activity has a 3' to 5' polarity with respect to the DNA strand on which this protein translocates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q89270
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P38935
DNA unwinding in 5' to 3' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P35187
exhibits an ATPase activity in the presence of single- or double-stranded DNA. Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex. The efficiency of unwinding is found to correlate inversely with the length of the duplex region. The recombinant Sgs1 fragment is found to bind more tightly to a forked DNA substrate than to either single or double-stranded DNA. Like the DNA-DNA helicase activity, unwinding of the DNA-RNA hybrid is driven by the hydrolysis of ATP or dATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP. ATP is hydrolyzed far faster than DNA is unwound in the presence of both Mn2+ and Mg2+
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hPifHD (core helicase domain) only unwinds the substrate with a 5' single-stranded DNA (ssDNA) overhang and is a 5' to 3' helicase. Pif1 specifically recognizes and unwinds DNA structures resembling putative stalled replication forks. Notably, the enzyme requires both arms of the replication fork-like structure to initiate efficient unwinding of the putative leading replication strand of such substrates. This DNA structure-specific mode of initiation of unwinding is intrinsic to the conserved core helicase domain (hPifHD) that also possesses a strand annealing activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolyzes ATP and dATP with equal efficiency. ATPase activity of the enzyme is absolutely DNA-dependent. DNA sequences containing pyrimidine stretches are more effective activators than those containing purine stretches. poly(dC) appears to be the most effective activator of the ATPase activity. DNA helicase migrates on a DNA template in 5' to 3' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8DPU8
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' DNA helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P9WMP9
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q6I4A9
PcrA shows 3' to 5' as well as 5' to 3' helicase activities, with substrates containing a duplex region and a 3' or 5' ss poly(dT) tail. PcrA also efficiently unwinds oligonucleotides containing a duplex region and a 5' or 3' ss tail with the potential to form a secondary structure
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
A8D930
purified recombinant protein contains ATP-dependent DNA helicase activity, ATP-independent RNA helicase activity, and DNA- or RNA-dependent ATPase activity
-
-
?
ATP + 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. dATP is most effective. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the dATPase activity of the protein
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q81JI8
strong 5' to 3' DNA helicase activity. At both 0.1 and 0.5 mM, dATP produces comparable or slightly higher levels of unwinding than ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P56255
the chemical cleavage step is the rate-limiting step in the ATPase cycle and is essentially irreversible and results in the bound ATP complex being a major component at steady state. This cleavage step is greatly accelerated by bound DNA, producing the high activation of this protein compared to the protein alone. The data suggest the possibility that ADP is released in two steps, which results in bound ADP also being a major intermediate, with bound ADP*phosphate being a very small component. It therefore seems likely that the major transition in structure occurs during the cleavage step, rather than phosphate release
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme can unwind 17-bp partial duplex substrates with equal efficiency whether or not they contain a fork. It translocates unidirectionally along the bound strand in the 3' to 5' direction. NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP. The optimum concentration of ATP for DNA helicase activity is 1.0 mM. At 8 mM ATP the DNA unwinding activity of PDH120 is inhibited. No significant difference in the DNA unwinding activity of PDH120 with forked or nonforked substrates. The enzyme fails to unwind synthetic blunt-ended duplex DNA suggesting that PDH120 requires ssDNA adjacent to the duplex as a loading zone
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P0C6X7
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme moves unidirectionally in the 3' to 5' direction along the bound strand and prefers a fork-like substrate structure and could not unwind blunt-ended duplex DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
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
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme unwinds DNA in the 3'-5' direction with respect to the strand to which the enzyme is bound
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the helicase is capable of displacing DNA fragments up to 140 nucleotides in length, but is unable to displace a DNA fragment 322 nucleotides in length. Preference for displacing primers whose 5' terminus is fully annealed as opposed to primers with a 12 nucleotide 5' unannealed tail. The presence of a 12 nucleotide 3' tail has no effect on the rate of displacement. DNA helicase E is capable of displacing a primer downstream of either a four nucleotide gap, a one nucleotide gap or a nick in the DNA substrate. Helicase E is inactive on a fully duplex DNA 30 base pairs in length
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the NTP hydrolysis step is significantly faster for the purine NTPs than for the pyrimidine NTPs, both in the absence and in the presence of the DNA. The nature of intermediates of the purine nucleotide, ATP, is different from the nature of the analogous intermediates of the pyrimidine nucleotide CTP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the number of ATP hydrolysis events per unwinding cycle is not a constant value. At optimum Mg2+ and saturating ATP concentrations 1 pmol of the enzyme unwinds 5.5 fmol (given as nucleotide bases) of the DNA duplex per s
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the protein binds RNA and DNA in a sequence specific manner. ATP hydrolysis is stimulated by some nucleic acid polymers much better than it is stimulated by others. The range is quite dramatic. Poly(G) RNA does not stimulate at any measurable level, and poly(U) RNA (or DNA) stimulates best (up to 50 fold). HCV helicase unwinds a DNA duplex more efficiently than an RNA duplex. ATP binds HCV helicase between two RecA-like domains, causing a conformational change that leads to a decrease in the affinity of the protein for nucleic acids. One strand of RNA binds in a second cleft formed perpendicular to the ATP-binding cleft and its binding leads to stimulation of ATP hydrolysis. RNA and/or ATP binding likely causes rotation of domain 2 of the enzyme relative to domains 1 and 3, and somehow this conformational change allows the protein to move like a motor
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P0C6X1
the recombinant protein has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity. The DNA helicase activity of the enzyme preferentially unwinds 5'-oligopyrimidine-tailed, partial-duplex substrates and requires a tail length of at least 10 nucleotides for effective unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P51979
unwinds DNA in the 3' to 5' direction relative to single-stranded regions in the DNA substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
unwinds partial duplex DNA substrates, as long as 343 base pairs in length, in a reaction that is dependent on either ATP or dATP hydrolysis. The direction of the unwinding reaction is 5' to 3' with respect to the strand of DNA on which the enzyme is bound
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
catalytic DNA helicase activity is coupled with NTPase and is stimulated by ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DNA-unwinding activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
multifunctional enzyme possessing serine protease, NTPase, DNA and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
genome structure, crystals and three-dimensional structure determined, structure of NTP-binding region, conserved residues within the NTP-binding pocket
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
modified malachite green assay, DNA unwinding by nonstructural protein 3, pH 6.5, 5 mM MgCl2, 2 mM ATP, and 0.1mg/ml polyU, initiated by adding 5100 nM enzyme
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
peptide inhibitors derived from amino acid sequence of motif VI analyzed, binding of the inhibitory peptides does not interfere with the NTPase activity, 4.7 pM DNA substrate used for determination of helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no DNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme is capable of unwinding a 70 bp duplex DNA flanked by unpaired single-stranded tails at both ends
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA. The site of interaction is mapped. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O57849
DNA helicase activity in 5' to 3' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
can unwind a bubble substrate consistent with a role in nucleotide excision repair
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q974S1
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q971R4
5' to 3' helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
a steric exclusion and wrapping (SEW) model for MCM helicases is proposed, which the hexamer complex is stabilized by wrapping of the displaced 5'-strand around the exterior surface, resembling a spool of thread
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
Arg329 is a key residue in the communication between the DNA-binding site of SsoMCM and the trans component of the ATPase active site
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P95949
ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q4JC68
ATP-dependent 5'3' DNA helicases, DNA-dependent ATPase
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent DNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
binding preference for forked substrates relative to partial or full duplex substrates. The nature of binding ogf the enzyme to Y-shaped substrates is distinct in that MCM loads on the 3'-tail while interacting with the 5'-tail likely via the MCM surface
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
dATP and ATP support DNA unwinding reaction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DNA duplexes that contains a 30-nucleotide 5'-tail. The ability of the enzyme to bind single- but not double-stranded DNA is required for the unwinding function
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DNA substrates with overhangs of 0, 6 or 9 nucleotides are unwound at similar rates and remain only partially unwound at the end of the reaction. Overhangs of 12, 15 or 20 nucleotides are unwound progressively more quickly and to completion. XPD can overcome single backbone or base modifications in both the translocated and the displaced strand. It can unwind DNA containing the bulky extrahelical adduct fluorescein and a cyclopyrimidine dimer
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
helicase activity with a 85-mer oligonucleotide
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P95949
only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
StoHjm has two main modules, the N-terminal ATPase and DNA binding module (1431) and the C-terminal helicase regulation module (414704). While the N-terminal module is active alone to hydrolyze ATP and to bind different types of DNA substrates, it does not show any helicase activity. DNA unwinding by the StoHjm protein requires the presence of domain III and IV of the C-terminal module in addition to the N-terminal module
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the central AAA+ domain possesses ATPase and helicase activity. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Addition of the N-terminus influences both the processivity of the helicase and the choice of substrate that can be melted by the ATPase domain. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Extensive regulatory inter-domain communication within the MCM complex
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O73946
the enzyme preferentially binds to fork-related Y-structured DNAs and unwinds their double-stranded regions
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q974S1
the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37C to 75C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q96YR7
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9HM14
utilizes the energy from ATP hydrolysis to unwind DNA with 5' to 3' polarity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
utilizes the energy from ATP hydrolysis to unwind DNA with 5' to 3' polarity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Pyrococcus horikoshii DSM 12428
O57849
DNA helicase activity in 5' to 3' direction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination, the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q4JC68
ATP-dependent 5'3' DNA helicases, DNA-dependent ATPase
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q96YR7
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Sulfolobus tokodaii 7
Q971R4
5' to 3' helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Sulfolobus tokodaii DSM 16993
Q974S1
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks, the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P9WMP9
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37C to 75C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent DNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P95949
ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity, only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail, dATP and ATP support DNA unwinding reaction
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DNA duplexes that contains a 30-nucleotide 5'-tail. The ability of the enzyme to bind single- but not double-stranded DNA is required for the unwinding function
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
West Nile virus WNV
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no DNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
D0KN27
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
Q89270
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
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
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
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
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
the NTP hydrolysis step is significantly faster for the purine NTPs than for the pyrimidine NTPs, both in the absence and in the presence of the DNA. The nature of intermediates of the purine nucleotide, ATP, is different from the nature of the analogous intermediates of the pyrimidine nucleotide, CTP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
ability of various NTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
ATP hydrolysis is required for unwinding of DNA catalyzed by the DNA helicase, the enzyme moves in the 5 to 3 direction on a single-stranded DNA to catalyze unwinding of double-stranded regions of DNA in the 3' to 5' direction. dATP shows 95% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
ATP-dependent DNA unwinding enzyme. HDH VI unwinds exclusively DNA duplexes with an annealed portion smaller than32 bp and prefers a replication fork-like structure of the substrate. It cannot unwind blunt-end duplexes and is inactive also on DNA-RNA or RNA-RNA hybrids. HDH VI unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand. ATP and dATP are equally good substrates
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
dATP shows 25% of the activity compared to ATP. DNA helicase unwinds DNA unidirectionally from 3 to 5
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
Dhel I moves 5' to 3' on the DNA strand to which it is bound. Unwinding activity decreases with increasing length of the double-stranded region suggesting a distributive mode of action. ATP and dATP are the only nucleoside-5'-triphosphates that support the strand displacement reaction. Both have an optimal concentration range between 1 and 2 mM
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
Q89270
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP. dATP is as efficient as ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
P35187
exhibits an ATPase activity in the presence of single- or double-stranded DNA. Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex. The efficiency of unwinding is found to correlate inversely with the length of the duplex region. The recombinant Sgs1 fragment is found to bind more tightly to a forked DNA substrate than to either single or double-stranded DNA. Like the DNA-DNA helicase activity, unwinding of the DNA-RNA hybrid is driven by the hydrolysis of ATP or dATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
hydrolyzes ATP and dATP with equal efficiency. ATPase activity of the enzyme is absolutely DNA-dependent
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
Q8DPU8
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
P9WMP9
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
Q81JI8
strong 5' to 3' DNA helicase activity. At both 0.1 and 0.5 mM, dATP produces comparable or slightly higher levels of unwinding than ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
structure-specific DNA helicase. DmRECQ5 preferentially unwinds specific DNA structures including a 3'flap, a three-strand junction and a three-way junction. Unwinding of a Holliday junction, 5'flap and 12 nt bubble structures, which can be unwound by other RecQ proteins (WRN, BLM and/or Escherichia coli RecQ), can not be detected or requires significantly higher protein concentrations
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
P0C6X7
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
the enzyme moves unidirectionally in the 3' to 5' direction along the bound strand and prefers a fork-like substrate structure and could not unwind blunt-ended duplex DNA. dATP supports unwinding at 42% of the efficiency of ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
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
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
unwinds partial duplex DNA substrates, as long as 343 base pairs in length, in a reaction that is dependent on either ATP or dATP hydrolysis. The direction of the unwinding reaction is 5' to 3' with respect to the strand of DNA on which the enzyme is bound
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
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
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
P9WMP9
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
dATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
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
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
P0C6X7
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
-
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
-
-
?
dCTP + H2O
dCTP + phosphate
show the reaction diagram
-
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
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
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
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-
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
-
-
?
dGTP + H2O
dGDP + phosphate
show the reaction diagram
-
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
-
-
?
dNTP + H2O
dNDP + phosphate
show the reaction diagram
-
dNTPs support faster DNA unwinding mediated by nonstructural protein 3, ability of various NTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay
-
-
?
dTTP + H2O
dTDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
dTTP + H2O
dTDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dTTP + H2O
dTDP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
-
-
?
dTTP + H2O
dTDP + phosphate
show the reaction diagram
-
in the absence of ssDNA, gp4 hydrolyzes dTTP poorly but the rate of hydrolysis increases approximately 40fold in the presence of ssDNA
-
-
?
dTTP + H2O
TDP + phosphate
show the reaction diagram
-
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
-
-
?
dUTP + H2O
dUDP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Q89270
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP. 21% of the ability to support NS3h_1b(con1)-catalyzed DNA unwinding compared to ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
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
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
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
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
the NTP hydrolysis step is significantly faster for the purine NTPs than for the pyrimidine NTPs, both in the absence and in the presence of the DNA. The nature of intermediates of the purine nucleotide, ATP, is different from the nature of the analogous intermediates of the pyrimidine nucleotide, CTP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
-
-
?
N1-methyl-ATP + H2O
N1-methyl-ADP + phosphate
show the reaction diagram
-
47% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 47% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
N6-methyl-ATP + H2O
N6-methyl-ADP + phosphate
show the reaction diagram
-
122% of the ability to support helicase catalyzed DNA unwinding compared to ATP, 122% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
NTP + H2O
NDP + phosphate
show the reaction diagram
-
different NTP binding rate and processivity, DNA unwinding of nonstructural protein 3, ability of various dNTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay
-
-
?
TTP + H2O
TDP + phosphate
show the reaction diagram
-
ability of various NTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
HCV helicase unwinds DNA at different rates depending on the nature and concentration of NTPs in solution. The fastest reactions are observed in the presence of CTP followed by ATP, UTP, and GTP. 3'-deoxy-NTPs generally support faster DNA unwinding, with dTTP supporting faster rates than any other canonical (d)NTP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
O24736
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
-
-
?
xanthosine 5'-triphosphate + H2O
xanthosine 5'-diphosphate + phosphate
show the reaction diagram
-
7% relative ability to support DNA unwinding by nonstructural protein 3, reported as percentage relative to ATP
-
-
?
XTP + H2O
XDP + phosphate
show the reaction diagram
-
7% of the ability to support helicase catalyzed DNA unwinding compared to ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
ability of various NTPs to support HCV helicase-catalyzed DNA unwinding by nonstructural protein 3 using a molecular-beacon-based helicase assay, 21% relative ability to support DNA unwinding, reported as percentage relative to ATP
-
-
?
additional information
?
-
Q06218
exhibits RNA unwinding and binding activity in the absence of NTP, and this activity is abolished by a mutation in the RNA-binding domain
-
-
-
additional information
?
-
Q89270
no helicase activity is observed with UTP, dCTP or dTTP, low levels of helicase activity is observed with dGTP
-
-
-
additional information
?
-
-
non-hydrolysable ATP analogues do not support helicase activity. DNA helicase II lacks any detectable RNA-unwinding activity
-
-
-
additional information
?
-
Q8DPU8
the enzyme is inefficient in in vitro replication of pT181, and perhaps as a consequence, this plasmid can not be established in Streptococcus pneumoniae
-
-
-
additional information
?
-
-
the helicase is capable of unwinding DNA substrates coated with various proteins, including histones, transcription inhibitors, and the transcription initiation complex. Thus, the helicase can displace at least some of the proteins associated with chromatin
-
-
-
additional information
?
-
-
the mature NS3 protein comprises 5 domains: the N-terminal 2 domains form the serine protease along with the NS4A cofactor, and the C-terminal 3 domains form the helicase. The helicase portion of NS3 can be separated form the protease portion by cleaving a linker. Since the protease portion is more hydrophobic, removing it allows the NS3 helicase fragment to be expressed as a more soluble protein at higher levels in Escherichia coli. The fragment of NS3 possessing helicase activity is referred to as HCV helicase
-
-
-
additional information
?
-
-
HDHB interacts with the N-terminal domain of replication protein A 70-kDa subunit
-
-
-
additional information
?
-
-
the loading of TWINKLE onto a circular ssDNA in vitro is examined. TWINKLE is able to load onto circular ssDNA without the help of a loading factor and can support initiation of DNA replication on a closed circular dsDNA substrate in combination with only mitochondrial DNA polymerase gamma
-
-
-
additional information
?
-
-
efficiency of unwinding is enhanced in the presence of a heterologous single strand-binding protein or a single-stranded (ss) DNA that is complementary to the unwound strand. TWINKLE has an antagonistic activity of annealing two complementary ssDNAs that interferes with unwinding in the absence of gp2.5 single strand-binding protein or ssDNA trap. Only ssDNA and not dsDNA competitively inhibits the annealing activity, although both DNAs bind with high affinities
-
-
-
additional information
?
-
-
Mtb XPB efficiently catalyzes DNA unwinding. Enzyme requires a DNA substrate with a 39 overhang of 15 nucleotides or more. Enzyme is not active on substrates containing a 39 RNA tail. Mtb XPB efficiently catalyzes ATP-independent annealing of complementary DNA strands
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P0C6X7
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q06218
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P56255
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P27395
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q14191
3'-5' helicase activity. WRN helicase is involved in preserving DNA integrity during replication. It is proposed that WRN helicase can function in coordinating replication fork progression with replication stress-induced fork remodeling
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UUA2
5' to 3' DNA helicase. ATPase/helicase activity of Pfh1p is essential. Maintenance of telomeric DNA is not the sole essential function of Pfh1p. Although mutant spores depleted for Pfh1p proceed through S phase, they arrest with a terminal cellular phenotype consistent with a postinitiation defect in DNA replication. Telomeric DNA is modestly shortened in the absence of Pfh1p
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P07271
5' to 3' DNA helicase. The ATPase/helicase activity of Rrm3p is required for its role in telomeric and subtelomeric DNA replication. Because Rrm3p is telomere-associated in vivo, it likely has a direct role in telomere replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
A8D930
AvDH1 belonging to the DEAD-box helicase family is induced by salinity, functions as a typical helicase to unwind DNA and RNA, and may play an important role in salinity tolerance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q12039
DNA helicase Hmi1p is involved in the maintenance of mitochondrial DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9UXG1
during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q9QY16
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O24736
helicase UvrD protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8I3W6
helicases play an essential role in nearly all the nucleic acid metabolic processes, catalyzing the transient opening of the duplex nucleic acids in an ATP-dependent manner
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q6Y5A8
involved in DNA recombination, repair and genome stability maintenance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
P51979
meiosis-specific MER3 protein is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q8DPU8
PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q19546
the ability of CeWRN-1 to unwind DNA structures may improve the access for DNA repair and replication proteins that are important for preventing the accumulation of abnormal structures, contributing to genomic stability
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide, suggesting a role of the enzyme in Okazaki fragment processing. The ability of the enzyme to target DNA replication/repair intermediates may be relevant to its role in genome stability maintenance
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q96RR1
TWINKLE is the helicase at the mitochondrial DNA replication fork
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
catalytic DNA helicase activity is coupled with NTPase and is stimulated by ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DNA-unwinding activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
multifunctional enzyme possessing serine protease, NTPase, DNA and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA. The site of interaction is mapped. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
can unwind a bubble substrate consistent with a role in nucleotide excision repair
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q974S1
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Sulfolobus tokodaii DSM 16993
Q974S1
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
West Nile virus WNV
-
-
-
-
?
NTP + H2O
NDP + phosphate
show the reaction diagram
-
different NTP binding rate and processivity, DNA unwinding of nonstructural protein 3
-
-
?
dNTP + H2O
dNDP + phosphate
show the reaction diagram
-
dNTPs support faster DNA unwinding mediated by nonstructural protein 3
-
-
?
additional information
?
-
-
HDHB interacts with the N-terminal domain of replication protein A 70-kDa subunit
-
-
-
additional information
?
-
-
the loading of TWINKLE onto a circular ssDNA in vitro is examined. TWINKLE is able to load onto circular ssDNA without the help of a loading factor and can support initiation of DNA replication on a closed circular dsDNA substrate in combination with only mitochondrial DNA polymerase gamma
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S cluster
-
the enzyme contains a 4Fe-4S cluster
Ca2+
P51979
MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity
Ca2+
Q12039
ATP hydrolysis in the presence of MgCl2 is 2fold higher than in the presence of either MnCl2 or CaCl2
Co2+
P9WMP9
supports activity similar to that with Mg2+
Co2+
-
activity 3-5-fold lower when magnesium ions are replaced by
Fe-S
-
Fe-S domain is not essential for SaXPD protein stability, the enzyme's ability to bind to single-stranded DNA, or its ATPase activity, but is required for helicase activity
Iron-sulfur cluster
Q4JC68
; is essential for the helicase activity
K+
-
activation at 100-300 mM, inhibition above 500 mM
KCl
-
optimum concentration: 250 mM. Completely inhibited at 400 mM
KCl
A8D930
optimal concentration for ATPase activity: 200 mM. Optimal concentration for helicase activity: 60 mM
KCl
-
optimal concentration: 100 mM. Inhibition at 200 mM
Mg2+
-
required, optimum concentration for ATPase reaction is 1-3 mM, optimum concentration for helicase reaction is 0.3-5 mM
Mg2+
P27395
no ATPase activity of the wild-type in the absence of
Mg2+
-
the enzyme requires MgCl2 for its activity. It is not active in the presence of MnCl2 or CaCl2 (1 mM)
Mg2+
Q19546
little or no unwinding is observed when Mg2+ was replaced with Zn2+
Mg2+
-
Mg2+ or Mn2+ required, optimum concentration of MgCl2 is 1 mM
Mg2+
-
absolute requirement for divalent cations. Mg2+ at 2.0 mM concentration optimally fulfills this requirement. At 8.0 mM MgCl2 the activity is totally inhibited
Mg2+
O24736
requirement for divalent metal ions. Helicase activity is stimulated most by MgCl2 at a concentration of 1.5 mM
Mg2+
-
requires divent cation, Mg2+ or Mn2+
Mg2+
-
required
Mg2+
P51979
MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity
Mg2+
P0C6X7
activity is dependent on
Mg2+
P40562
maximal activity is obtained with Mg2+, whereas Co2+ and Ca2+ are much less effective in this regard. No activity is observed with Mn2+ or Zn2+
Mg2+
A8D930
required for ATPase and DNA-unwinding activity, optimal concentration for DNA unwinding reaction: 2.0 mM, optimal concentration for ATP-independent RNA unwinding reaction: 2 mM
Mg2+
-
divalent metal cations are absolutely required for HCV helicase-catalyzed DNA unwinding. When compared with unwinding in the presence of Mg2+, Mn2+ supports 10 times faster rates than Mg2+ regardless of the concentration of metal in solution. All NTPs support faster unwinding when 2 mM Mn2+ is used instead of 2 mM Mg2+. The specificity profile remains mostly unchanged in the presence of Mn2+, while the absolute magnitude of the rates increases; influences DNA unwinding rates of recombinant nonstructural protein 3, metal ion specificity suggests that NTPs bind two different enzyme conformations
Mg2+
Q89270
Mg2+ or Mn2+ required, optimal activity at 4 mM MgCl2
Mg2+
-
required for maximal activity, optimal concentration: 0.8 mM. Inhibition at 4 mM
Mg2+
-
divalent cation required, optimum concentration: 0.5 mM
Mg2+
-
unwinding activity requires Mg2+
Mg2+
Q12039
ATP hydrolysis in the presence of MgCl2 is 2fold higher than in the presence of either MnCl2 or CaCl2
Mg2+
-
maximal NTPase activity achieved in the presence of 1.5-2 mM MgCl2
Mg2+
-
-
Mg2+
-
required
Mg2+
O57849
required for activity
Mg2+
Q974S1
Mg2+-dependent enzyme
Mg2+
-
the enzyme requires a divalent cation (Mg2+, Mn2+, or Ca2+) for its helicase activity, with Mg2+ being the preferred cofactor. The enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP)
MgCl2
P9WMP9
required, optimal concentration: 5 mM
MgUTP
-
MgUTP stabilizes hexamers over higher oligomers
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
2.0 mM, supports 80% of the activity compared to Mg2+
Mn2+
O24736
MnCl2 stimulates activity, though not as well as the MgCl2
Mn2+
P9WMP9
supports ATPase activity with 2fold lower efficiency compared to Mg2+
Mn2+
-
can substitute for Mg2+, less effective
Mn2+
-
requires divent cation, Mg2+ or Mn2+
Mn2+
P51979
MER3 ATPase activity requires a divalent cation. Maximal activity can be observed in the presence of either Ca2+, Mg2+, or Mn2+, whereas Zn2+ does not support the ATPase activity
Mn2+
P0C6X7
can substitute for Mg2+, 40% of the efficiency with Mg2+ at 2.5 mM
Mn2+
-
divalent metal cations are absolutely required for HCV helicase-catalyzed DNA unwinding. When compared with unwinding in the presence of Mg2+, Mn2+ supports 10 times faster rates than Mg2+ regardless of the concentration of metal in solution. All NTPs support faster unwinding when 2 mM Mn2+ is used instead of 2 mM Mg2+. The specificity profile remains mostly unchanged in the presence of Mn2+, while the absolute magnitude of the rates increases; influences DNA unwinding rates of recombinant nonstructural protein 3, supports about 10 times faster unwinding than Mg2+, unlike Mg2+, Mn2+ does not support helicase-catalyzed ATP hydrolysis in the absence of stimulating nucleic acids, metal ion specificity suggests that NTPs bind two different enzyme conformations
Mn2+
Q89270
Mg2+ or Mn2+ required
Mn2+
Q12039
ATP hydrolysis in the presence of MgCl2 is 2fold higher than in the presence of either MnCl2 or CaCl2
Mn2+
-
activity 3-5-fold lower when magnesium ions are replaced by
Na+
-
activation at 100-300 mM, inhibition above 500 mM
NaCl
P9WMP9
optimal concentration: 50 mM
NaCl
Q89270
optimal concentration is 50-100 mM, higher concentrations inhibit helicase activity
Ni2+
P9WMP9
supports ATPase activity with 3fold lower efficiency compared to Mg2+
Ni2+
-
activity 3-5-fold lower when magnesium ions are replaced by
Zn2+
-
BcMCM amino-terminus can bind single-stranded DNA and harbors a zinc atom, BcMCM contains 0.11 zinc atoms per mole
Zn2+
-
activity 3-5-fold lower when magnesium ions are replaced by
additional information
-
Ca2+, Zn2+, Cd2+, Cu2+, Ni2+, Ag2+ and Co2+ are unable to support the activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2Z)-4-[2-(benzyloxy)phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
low inhibitory activities
(2Z)-4-[2-[(4-chlorobenzyl)oxy]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
no or marginal inhibition activities towards ATPase activity or duplex DNA-unwinding activity
(2Z)-4-[3-(benzylamino)phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity
(2Z)-4-[3-(benzyloxy)phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
low inhibitory activities
(2Z)-4-[3-[(4-chlorobenzyl)amino]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity
(2Z)-4-[3-[(4-chlorobenzyl)oxy]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity
(2Z)-4-[4-(benzyloxy)phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
low inhibitory activities, para-relationship between the diketoacid moiety and the OCH2Ar group do not show antiviral activities
(2Z)-4-[4-[(4-chlorobenzyl)oxy]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
low inhibitory activities, para-relationship between the diketoacid moiety and the OCH2Ar group do not show antiviral activities
(5'R)-8,5'-cyclo-2'-deoxyguanosine
-
the enzyme is strongly inhibited by (5'R)-8,5'-cyclo-2'-deoxyguanosine in the non-translocating strand
-
(5'S)-8,5'-cyclo-2'-deoxyguanosine
-
the enzyme is strongly inhibited by (5'S)-8,5'-cyclo-2'-deoxyguanosine in the non-translocating strand. At 40 nM enzyme, less than 10% of the forked duplex with (5'S)-8,5'-cyclo-2'-deoxyguanosine in the nontranslocating strand is unwound compared to 60% of the control forked duplex or the substrate with (5'S)-8,5'-cyclo-2'-deoxyguanosine in the translocating strand
-
(NH4)2SO4
-
45 mM
2',3'-ddATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2',3'-ddGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2',3'-ddTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-deoxythymidine 5'-phosphoryl-beta,gamma-hypophosphate
-
i.e. ppopT, dTTP analogue, most efficient inhibitor of NTPase activity among nucleotide derivaties, inhibits the ATP-dependent helicase reaction and also the ATP-independent duplex unwinding, structure of nucleic base and ribose fragment of NTP molecule have a slight effects on inhibitory properties
2'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
2'-dTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
3'-dUTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
5-fluoro-2-selenocytosine
-
reduces ATPase activity, no effect on helicase activity
Aclarubicin
-
-
actinomycin
-
-
actinomycin C1
-
-
-
ADP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
ammonium sulfate
-
45 mM, complete inhibition
AMP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
ATP
-
10 mM
ATP
-
the optimum concentration of ATP for DNA helicase activity is 1.0 mM. At 8 mM ATP the DNA unwinding activity of PDH120 is inhibited
ATP
A8D930
above 8 mM
ATP
-
substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed
ATPgammaS
-
-
beta,gamma-methylene-ATP
-
efficient inhibitor, like the N1-oxides N1-oxoadenosine 5'-triphosphate and N1-hydroxyinosine 5'-triphosphate
Cdc6-1 protein
-
inhibits the DNA unwinding activity, although it strongly stimulates the interaction of the enzyme with bubble containing synthetic oligonucleotides
-
Cdc6-3 protein
-
inhibits the DNA unwinding activity, although it strongly stimulates the interaction of the enzyme with bubble containing synthetic oligonucleotides
-
dATP
-
inhibits unwinding
dATP
-
substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed
daunorubicin
-
0.01 mM, completely inhibits DNA helicase reaction
daunorubicin
-
-
daunorubicin
-
-
daunorubicin
-
less efficient inhibition of DNA helicase activity, but no inhibition of ATPase activity
DnaG primase
-
SsoDnaG primase concentrations less than 0.001mM show little or no inhibition of SsoMCM helicase unwinding activity. Unwinding inhibition is strongest at or above 0.002 mM where the SsoMCM:SsoDnaG ratio is 2:1
-
double-strand DNA binding protein
-
-
-
Doxorubicin
-
-
Doxorubicin
-
less efficient inhibition of DNA helicase activity, but no inhibition of ATPase activity
dsDNA
-
0.01 mM
-
EDTA
-
5 mM
EDTA
-
5 mM, complete inhibition
EDTA
P0C6X7
-
EDTA
-
5 mM, complete inhibition
Ethidium bromide
-
-
GTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
histone H1
-
0.001 mg/ml, inhibits of the DNA helicase activity
-
Imidodiphosphate
-
maximal inhibitory activity among diphosphate analogues, non-catalytic and catalytic conditions, inhibits the ATP-dependent helicase reaction but no effect on the ATP-independent duplex unwinding, structure of nucleic base and ribose fragment of NTP molecule have a slight effects on inhibitory properties
K+
-
activation at 100-300 mM, inhibition above 500 mM
KCl
-
400 mM
KCl
-
optimum concentration: 250 mM. Completely inhibited at 400 mM
KCl
P40562
30% inhibition occurs when KCl concentration is increased from 15 to 200 mM
KCl
A8D930
helicase activity is inhibited at 200 mM
KCl
-
optimal concentration: 100 mM. Inhibition at 200 mM
KCl
-
200 mM, inhibits
KCl
-
slight decrease of activity in presence of
M13 dsDNA
-
0.03 mM, complete inhibition
-
M13 ssDNA
-
0.03 mM, complete inhibition
-
M13mp19 ssDNA
Q81JI8
ATPase activity is slightly stimulated by ssDNA, and only M13mp19 ssDNA stimulates it significantly (increase in Vmax)
-
Mg2+
-
absolute requirement for divalent cations. Mg2+ at 2.0 mM concentration optimally fulfills this requirement. At 8.0 mM MgCl2 the activity is totally inhibited
N1-hydroxyinosine 5'-triphosphate
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
N1-O-ATP
-
-
N1-OH-ITP
-
-
N1-oxoadenosine 5'-triphosphate
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
Na+
-
activation at 100-300 mM, inhibition above 500 mM
NaCl
-
57% inhibition at 0.2 M, 81% inhibition at 0.4 M
NaCl
-
ATPase activity is inhibited by salt (NaCl) above 50 mM with a half-maximal inhibition at about 110 mM
NaCl
Q89270
optimal concentration is 50-100 mM, higher concentrations inhibit helicase activity
NaCl
-
above 10 mM
NaCl
-
200 mM, inhibits
NaCl
-
above 200 mmol/l
NaCl
-
above 100 mM
Nogalamycin
-
0.01 mM, completely inhibits DNA helicase reaction
Nogalamycin
-
-
Nogalamycin
-
-
O6-benzyl-N7-chloroethylguanine
-
weak inhibitor of the ATPase and helicase activity
O6-benzylguanine
-
weak inhibitor of the ATPase and helicase activity
Poly(A)
Q06218
moderately inhibits ATPase activity
poly(C)
Q06218
moderately inhibits ATPase activity
Poly(U)
Q06218
moderately inhibits ATPase activity
potassium phosphate
-
-
potassium phosphate
-
100 mM, complete inhibition
replication protein A
-
inhibits unwinding and annealing activities
-
ribavirin 5'-triphosphate
-
competitive inhibitor with regard to ATP
RNA
-
0.01 mM
single-strand DNA binding protein
-
-
-
Single-stranded DNA
O24736
-
single-stranded DNA-binding proteins
P51979
-
-
ssDNA
-
0.01 mM
-
ssDNA
Q81JI8
ATPase activity is slightly stimulated by ssDNA, and only M13mp19 ssDNA stimulats it significantly
-
SsoCdc6-1 protein
-
significantly inhibits the loading activity of the helicase, and this inhibitive effects can not be reversed by the stimulation of SsoCdc6-2 protein
-
SsoCdc6-1 protein
-
inhibits the DNA-binding activity of SsoMCM
-
SsoCdc6-1 protein
-
strongly inhibits the ATPase and DNA helicase activity of the Sulfolobus solfataricus MCM protein
-
SsoCdc6-2 protein
-
i.e. Cdc6 (cell-division control)-like factor from Sulfolobus solfataricus. The Cdc6 WH-domain is responsible for DNA-binding and inhibition of MCM DNA helicase. Residues 298-400 of Cdc6 (cell-division control)-like factor also bind DNA molecules and inhibit the DNA helicase activity of the SsoMCM mini-chromosome maintenance complex, although with lesser efficiency with respect to the full-sized SsoCdc6-2
-
SsoCdc6-3 protein
-
significantly inhibits the loading activity of the helicase, and this inhibitive effects can not be reversed by the stimulation of SsoCdc6-2 protein
-
Streptavidin
-
the enzyme is completely blocked by streptavidin bound to the 3'-ssDNA tail 6 nucleotides upstream of the single-stranded/double-stranded DNA junction. The enzyme efficiently unwinds the forked duplex with streptavidin bound just upstream of the junction, suggesting that the enzyme recognizes elements of the fork structure to initiate unwinding
-
TaGins51 protein
-
inhibits the ATPase activity, but not the helicase activity
-
tetrabromobenzotriazole
-
inhibits unwinding, no inhibition of ATP hydrolysis
Trypsin
-
-
-
UTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
yeast total RNA
Q06218
severly inhibits ATPase activity
-
Mg2+
-
required, optimal concentration: 0.8 mM. Inhibition at 4 mM
additional information
-
Hel E is inhibited by replication fork structures
-
additional information
-
inhibitory potential of peptides deduced from amino acid sequence of motif VI tested, NTP-binding and hydrolyzing site not involved, 4.7 pM DNA substrate used for determination of helicase activity
-
additional information
-
domain 2 of wild-type NS3 protein and domain 2 devoid of the loop structure used for inhibition studies on functions of protein kinase C (PKC), inhibitory potential towards the majority of protein kinase C isoforms shown
-
additional information
Q974S1
the Holliday junction-specific endonuclease from Sulfolobus tokodaii (StoHjc) inhibits in vitro
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
catalytic DNA helicase activity coupled with NTPase stimulated by
DNA
Q06218
ATPase activity is stimulated by yeast genomic DNA and salmon sperm DNA
DnaG primase
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA.The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
Double-stranded DNA
-
the enzyme is strongly stimulated by either single- or double-stranded DNA
Double-stranded DNA
P51979
MER3 ATPase activity is stimulated by either single- or double-stranded DNA
dsDNA
Q96YR7
ATPase activity of StoHerA is stimulated by ssDNA and dsDNA
-
GINS complex
-
stimulates both the ATPase and DNA helicase activities of mini-chromosome maintenance helicase; the DNA helicase activity of Pyrococcus furiosus MCM is stimulated by the addition of the Pyrococcus furiosus GINS complex of Gins23 and Gins51
-
heterotrimeric single-stranded DNA binding protein replication protein A
P40562
enhances DNA helicase activity of Mph1
-
homopolynucleotides
P0C6X7
significantly stimulate the ATPase activity (15-25fold) with the exception of poly(G) and poly(dG), which are non-stimulatory. dT24 binds over 10 times more strongly than dA24
-
N7-chloroethylguanine
-
; 2.2fold activation at 200-250 mM
N9-chloroethylguanine
-
8.5fold activation at 200-250 mM
O6-benzyl-N9-chloroethylguanine
-
stimulator of NTPase activity, with a maximum effect of 350% of control at 650 mM
poly(C)
P0C6X1
strong stimulation
poly(dA)
-
170-180% activation at 1.7-3.3 mM, no activation by other polynucleotides
poly(dA)
P0C6X1
strong stimulation
poly(dI*C)
-
weakly supports ATPase activity
-
Poly(dT)
P0C6X1
strong stimulation
Poly(dT)
-
weakly supports ATPase activity
Poly(U)
P0C6X1
strong stimulation
polyadenylate
-
doubling of ATPase activity in the presence of
-
polyuridylate
-
doubling of ATPase activity in the presence of, lowers Km for the ATP substrate
-
repair proteins Mre11
Q96YR7
stimulates helicase activity
-
replication protein A
Q19546
from Caenorhabditis elegans, stimulates helicase activity
-
replication protein A
-
stimulates helicase activity
-
replication protein A
-
stimulates activity
-
replication protein A
P38935
from yeast or human
-
ribavirin
-
activates ATPase activity, no effect on helicase activity
Single-stranded DNA
-
stimulates activity
Single-stranded DNA
-
required
Single-stranded DNA
P07271
stimulates
Single-stranded DNA
Q6I4A9
stimulates
Single-stranded DNA
-
the enzyme is strongly stimulated by either single- or double-stranded DNA
Single-stranded DNA
P51979
MER3 ATPase activity is stimulated by either single- or double-stranded DNA
Single-stranded DNA
P40562
the enzyme requires single-stranded DNA for activation
Single-stranded DNA
A8D930
the ATPase activity of AvDH1 is stimulated more by single-stranded DNA than by double-stranded DNA or RNA. Significantly stimulated by the presence of M13 ssDNA
Single-stranded DNA
P38935
more than 5fold stimulation of ATPase activity
Single-stranded DNA
-
nonstructural single-stranded DNA greatly stimulates ATPase activity due to a high affinity for PIF1, even though PIF1 preferentially unwinds forked substrates. The N-terminal portion oF PIF1 helicase, named the PIF1 N-terminal (PINT) domain, contributes to enhancing the interaction with single-stranded DNA through intrinsic binding activity
Single-stranded DNA
-
stimulates activity
single-stranded DNA binding protein
-
of Escherichia coli (SSB), stimulates to a lower extent
-
single-stranded DNA binding protein
-
stimulates activity and forms a protein/protein complex with the mini-chromosome maintenance protein helicase
-
single-stranded DNA binding protein dRP-A
-
stimulates the activity on substrates with more than 300 nucleotides double-stranded region
-
single-stranded DNA-binding protein
-
from Escherichia coli, strongly stimulates when long partial duplex substrates are used
-
single-stranded DNA-binding protein
P35187
of Escherichia coli, stimulates activity
-
single-stranded DNA-binding protein
P51979
single-stranded DNA-binding proteins stimulate
-
ssDNA
-
the effect of single-stranded DNA on the kinetics of NTP hydrolysis depends on the type of nucleotide cofactor and the base composition of the DNA and is centered at the hydrolysis step. Homoadenosine ssDNA oligomers are particularly effective in increasing the hydrolysis rate
-
ssDNA
Q8DPU8
stimulates ATPase activity
-
ssDNA
Q96YR7
ATPase activity of StoHerA is stimulated by ssDNA and dsDNA
-
SsoCdc6-2 protein
-
stimulates the binding of the helicase onto the forked DNA
-
SsoCdc6-2 protein
-
stimulates the DNA-binding activity of the enzyme
-
yeast replication protein A
-
stimulates significantly
-
mitochondrial single-stranded DNA-binding protein
-
stimultes the enzyme
-
additional information
P0C6X1
no stimulation by poly(G)
-
additional information
-
synthetic RNA poly(U) does not support ATP hydrolysis at all. Unlike DNA helicase I, DNA helicase II is not stimulated by SpRPA or Escherichia coli SSB at low ATP concentrations
-
additional information
P38935
no significant stimulation by Escherichia coli ssDNA-binding protein
-
additional information
-
in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
2'(3')-O-(N-methylanthraniloyl)ATP
P56255
pH 7.5, 20C, in presence of DNA
0.006
2'(3')-O-(N-methylanthraniloyl)ATP
P56255
pH 7.5, 20C, without DNA
0.00006
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A
0.00009
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A/D327A
0.0001
ATP
-
pH and temperature not specified in the publication, mutant enzyme D327A
0.00012
ATP
-
pH and temperature not specified in the publication, mutant enzyme V324A
0.00014
ATP
-
pH and temperature not specified in the publication, mutant enzyme K323A
0.00017
ATP
-
pH and temperature not specified in the publication, mutant enzyme R329A; pH and temperature not specified in the publication, wild-type enzyme
0.00022
ATP
-
pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G
0.00023
ATP
-
pH and temperature not specified in the publication, mutant enzyme V324A/L325A
0.00027
ATP
-
pH and temperature not specified in the publication, mutant enzyme L325A
0.00028
ATP
-
pH and temperature not specified in the publication, wild-type enzyme
0.0004
ATP
-
pH and temperature not specified in the publication, mutant enzyme T550G/P551G/D552G/S553G/P554G
0.0012
ATP
-
pH and temperature not specified in the publication, mutant enzyme L189D/D191R
0.0016
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G
0.0019
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, wild-type enzyme
0.0025
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, mutant enzyme T550G/P551G/D552G/S553G/P554G
0.0035
ATP
P56255
pH 7.5, 20C, in presence of DNA
0.0038
ATP
-
pH 8.0, 30C, with saturating concentration of M13 mp18 ssDNA
0.0044
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A/D327A/R329A
0.005
ATP
P56255
pH 7.5, 20C, without DNA
0.0095
ATP
-
pH 7.5, 30C, in presence of 2 mM Mg2+
0.013
ATP
-
recombinant protein including C-terminal portion the ATPase/helicase domain encompassing residues 181-619, ATP concentration 1 mM ATP, ATPase but not DNA helicase activity
0.013
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, mutant enzyme L189D/D191R
0.0553
ATP
P9WMP9
pH 7.5, in presence of 1 mM Co2+
0.061
ATP
P38935
-
0.07
ATP
-
helicase-catalyzed DNA unwinding activity mediated by recombinant nonstructural protein 3, reactions with 1 mM ATP contain 1.25 mM total MgCl2, data are globally fit to a model for substrate inhibition
0.08
ATP
P9WMP9
pH 7.5, in presence of 1 mM Mg2+
0.086
ATP
P9WMP9
pH 7.5, in presence of 1 mM Mn2+
0.09
ATP
-
pH 7.5, 30C
0.1
ATP
P46063
mutant (RECQ1(T1))Y564A, a construct encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa
0.115
ATP
P46063
full-length RECQ1 helicase
0.128
ATP
P9WMP9
pH 7.5, in presence of 1 mM Ni2+
0.135
ATP
P46063
(RECQ1(T1)), a construct encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa
0.15
ATP
-
pH 8.0, 30C, in presence of ssDNA
0.15
ATP
Q12039
pH 7.5, 30C
0.152
ATP
Q81JI8
pH 7.5, 37C, addition of 60-mer oligonucleotide
0.163
ATP
-
addition of polyuridylate lowers Km for the ATP substrate
0.2
ATP
-
pH 7.8, 30C
0.22
ATP
Q81JI8
pH 7.5, 37C, addition of M13mp19 ssDNA
0.256
ATP
-
wild-type
0.33
ATP
P0C6X7
pH 6.6, 25C
0.47
ATP
P51979
pH 7.6, 30C, in presence of poly(dA)
0.58
ATP
P51979
pH 7.6, 30C, in presence of M13mp18 single-stranded circular DNA
0.65
ATP
-
pH 7.8, 37C
0.84
ATP
-
mutant A318T, pH 7.5, 37C, in the presence of calf thymus DNA
0.89
ATP
Q9BX63
wild-type, pH 7.4, 30C, in the presence of M13 ssDNA
1
ATP
-
mutant W315L, pH 7.5, 37C, in the presence of calf thymus DNA
1.02
ATP
-
mutant K319T, pH 7.5, 37C, in the presence of calf thymus DNA
1.03
ATP
-
mutant R354P, pH 7.5, 37C, in the presence of calf thymus DNA
1.04
ATP
-
mutant R334Q, pH 7.5, 37C, in the presence of calf thymus DNA
1.08
ATP
-
mutant T457I, pH 7.5, 37C, in the presence of calf thymus DNA
1.1
ATP
-
mutant W474C, pH 7.5, 37C, in the presence of calf thymus DNA
1.17
ATP
-
mutant S369Y pH 7.5, 37C, in the presence of calf thymus DNA
1.22
ATP
-
mutant A475P, pH 7.5, 37C, in the presence of calf thymus DNA; wild-type wit His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
1.24
ATP
-
mutant R357P, pH 7.5, 37C, in the presence of calf thymus DNA
1.3
ATP
-
mutant A359T, pH 7.5, 37C, in the presence of calf thymus DNA
1.32
ATP
-
mutant P335L, pH 7.5, 37C, in the presence of calf thymus DNA
1.4
ATP
Q9BX63
mutant DELTA Q25, pH 7.4, 30C, in the presence of M13 ssDNA
1.43
ATP
-
wild-type without His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
1.44
ATP
-
mutant F485L, pH 7.5, 37C, in the presence of calf thymus DNA
1.5
ATP
Q9BX63
mutant Q25A, pH 7.4, 30C, in the presence of M13 ssDNA
1.6
ATP
Q9BX63
wild-type, pH 7.4, 30C, in the absence of DNA
1.8
ATP
Q9BX63
mutant Q25A, pH 7.4, 30C, in the absence of DNA
1.81
ATP
-
mutant R303W, pH 7.5, 37C, in the presence of calf thymus DNA
1.82
ATP
-
mutant K319E, pH 7.5, 37C, in the presence of calf thymus DNA
1.89
ATP
-
mutant S369P, pH 7.5, 37C, in the presence of calf thymus DNA
1.9
ATP
Q9BX63
mutant DELTA Q25, pH 7.4, 30C, in the absence of DNA
1.96
ATP
-
mutant Y508C, pH 7.5, 37C, in the presence of calf thymus DNA
2.23
ATP
-
mutant I367T, pH 7.5, 37C, in the presence of calf thymus DNA
2.48
ATP
-
mutant R374Q , pH 7.5, 37C, in the presence of calf thymus DNA
4.55
ATP
-
mutant L381P, pH 7.5, 37C, in the presence of calf thymus DNA
0.47
CTP
P0C6X7
pH 6.6, 25C
0.2
dATP
P0C6X7
pH 6.6, 25C
0.25
dATP
-
pH 7.8, 30C
0.25
dATP
-
pH 8.0, 30C, in presence of ssDNA
0.22
dCTP
P0C6X7
pH 6.6, 25C
0.35
dGTP
P0C6X7
pH 6.6, 25C
0.3
dTTP
-
helicase-catalyzed DNA unwinding activity mediated by recombinant nonstructural protein 3, reactions with 0.2 mM ATP contain 0.45 mM total MgCl2, data are globally fit to a model for substrate inhibition
0.93
dUTP
P0C6X7
pH 6.6, 25C
0.2
GTP
P0C6X7
pH 6.6, 25C
0.55
UTP
P0C6X7
pH 6.6, 25C
1.4
UTP
-
pH 7.5, 30, in the presence of forked DNA
1.6
UTP
-
pH 7.5, 30, in the presence of ssDNA
1.7
UTP
-
pH 7.5, 30, in the presence of ssM13mp18
3.4
UTP
-
pH 7.5, 30, in the absence DNA
0.41
GTP
-
helicase-catalyzed DNA unwinding activity mediated by recombinant nonstructural protein 3, data for reactions performed at or below 1 mM NTP, data are globally fit to a model for substrate inhibition
additional information
additional information
P56255
KM-values for cleavage of dTn DNA (dT10, dT20, dT30, dT40)
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
2'(3')-O-(N-methylanthraniloyl)ATP
P56255
pH 7.5, 20C, without DNA
17.2
2'(3')-O-(N-methylanthraniloyl)ATP
P56255
pH 7.5, 20C, in presence of DNA
0.03
ATP
-
pH and temperature not specified in the publication, mutant enzyme K323A; pH and temperature not specified in the publication, mutant enzyme R329A
0.03
ATP
-
pH and temperature not specified in the publication, mutant enzyme L189D/D191R
0.033
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A/D327A
0.038
ATP
-
pH and temperature not specified in the publication, mutant enzyme D327A
0.04
ATP
-
pH and temperature not specified in the publication, mutant enzyme V324A
0.043
ATP
-
pH 8.0, 30C, without ssDNA
0.045
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A/D327A/R329A
0.047
ATP
-
pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G; + Y-DNA, pH and temperature not specified in the publication, mutant enzyme I555D/L556S/I557D
0.048
ATP
-
pH and temperature not specified in the publication, mutant enzyme E326A
0.052
ATP
-
pH and temperature not specified in the publication, mutant enzyme T550G/P551G/D552G/S553G/P554G; pH and temperature not specified in the publication, wild-type enzyme
0.055
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G
0.065
ATP
-
pH and temperature not specified in the publication, mutant enzyme V324A/L325A
0.067
ATP
-
pH and temperature not specified in the publication, wild-type enzyme
0.068
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, wild-type enzyme
0.07
ATP
Q9BX63
mutant DELTA Q25, pH 7.4, 30C, in the absence of DNA
0.075
ATP
Q9BX63
mutant K52R, pH 7.4, 30C, in the presence of M13 ssDNA
0.08
ATP
-
pH and temperature not specified in the publication, mutant enzyme L325A
0.085
ATP
Q9BX63
mutant K52R, pH 7.4, 30C, in the presence of M13 ssDNA
0.09
ATP
-
+ Y-DNA, pH and temperature not specified in the publication, mutant enzyme L189D/D191R
0.155
ATP
Q9BX63
mutant Q25A, pH 7.4, 30C, in the absence of DNA
0.2
ATP
Q9BX63
wild-type, pH 7.4, 30C, in the absence of DNA
0.3
ATP
P56255
pH 7.5, 20C, without DNA
0.66
ATP
-
mutant A475P, pH 7.5, 37C, in the presence of calf thymus DNA
0.7
ATP
-
mutant W474C, pH 7.5, 37C, in the presence of calf thymus DNA
0.88
ATP
-
mutant T457I, pH 7.5, 37C, in the presence of calf thymus DNA
0.98
ATP
-
mutant K319T, pH 7.5, 37C, in the presence of calf thymus DNA
1.01
ATP
-
mutant R334Q, pH 7.5, 37C, in the presence of calf thymus DNA
1.06
ATP
-
mutant A359T, pH 7.5, 37C, in the presence of calf thymus DNA
1.08
ATP
-
mutant P335L, pH 7.5, 37C, in the presence of calf thymus DNA
1.13
ATP
-
mutant W315L, pH 7.5, 37C, in the presence of calf thymus DNA
1.15
ATP
-
mutant F485L, pH 7.5, 37C, in the presence of calf thymus DNA
1.18
ATP
-
mutant R354P, pH 7.5, 37C, in the presence of calf thymus DNA
1.19
ATP
-
mutant A318T, pH 7.5, 37C, in the presence of calf thymus DNA
1.2
ATP
Q12039
pH 7.5, 30C
1.5
ATP
P46063
full-length RECQ1 helicase
1.52
ATP
-
mutant R357P, pH 7.5, 37C, in the presence of calf thymus DNA
1.68
ATP
Q9BX63
mutant DELTA Q25, pH 7.4, 30C, in the presence of M13 ssDNA
1.9
ATP
-
wild-type wit His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
1.94
ATP
-
mutant S369Y pH 7.5, 37C, in the presence of calf thymus DNA
2.04
ATP
-
mutant Y508C, pH 7.5, 37C, in the presence of calf thymus DNA
2.09
ATP
-
mutant S369P, pH 7.5, 37C, in the presence of calf thymus DNA
2.17
ATP
-
mutant R374Q , pH 7.5, 37C, in the presence of calf thymus DNA
2.18
ATP
-
wild-type without His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
2.24
ATP
-
mutant K319E, pH 7.5, 37C, in the presence of calf thymus DNA
2.29
ATP
-
mutant R303W, pH 7.5, 37C, in the presence of calf thymus DNA
2.89
ATP
-
mutant I367T, pH 7.5, 37C, in the presence of calf thymus DNA
3.6
ATP
Q9BX63
mutant Q25A, pH 7.4, 30C, in the presence of M13 ssDNA
7.41
ATP
P46063
mutant (RECQ1(T1))Y564A, a construct encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa
8.31
ATP
-
mutant L381P, pH 7.5, 37C, in the presence of calf thymus DNA
8.8
ATP
P51979
pH 7.6, 30C, in presence of M13mp18 single-stranded circular DNA
9.2
ATP
P51979
pH 7.6, 30C, in presence of poly(dA)
11.25
ATP
P46063
(RECQ1(T1)), a construct encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa
13.1
ATP
P9WMP9
pH 7.5, in presence of 1 mM Ni2+
15
ATP
-
pH 8.0, 30C, in presence of ssDNA
16.9
ATP
P56255
pH 7.5, 20C, in presence of DNA
19.1
ATP
P0C6X7
pH 6.6, 25C
19.8
ATP
P9WMP9
pH 7.5, in presence of 1 mM Mn2+
22.2
ATP
P9WMP9
pH 7.5, in presence of 1 mM Co2+
29.8
ATP
P9WMP9
pH 7.5, in presence of 1 mM Mg2+
43.3
ATP
Q9BX63
wild-type, pH 7.4, 30C, in the presence of M13 ssDNA
7980
ATP
-
pH 7.5, 30C, in presence of 2 mM Mg2+
13.9
CTP
P0C6X7
pH 6.6, 25C
0.25
dATP
-
pH 8.0, 30C, without ssDNA
14.8
dATP
P0C6X7
pH 6.6, 25C
23
dATP
-
pH 8.0, 30C, in presence of ssDNA
14.3
dCTP
P0C6X7
pH 6.6, 25C
7.5
dGTP
P0C6X7
pH 6.6, 25C
14.8
dUTP
P0C6X7
pH 6.6, 25C
10.5
UTP
P0C6X7
pH 6.6, 25C
5.4
GTP
P0C6X7
pH 6.6, 25C
additional information
additional information
P56255
turnover numbers for cleavage of dTn DNA (dT10, dT20, dT30, dT40)
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.54
ATP
-
mutant A475P, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.64
ATP
-
mutant W474C, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.8
ATP
-
mutant F485L, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.81
ATP
-
mutant A359T, pH 7.5, 37C, in the presence of calf thymus DNA; mutant T457I, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.82
ATP
-
mutant P335L, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.88
ATP
-
mutant R374Q , pH 7.5, 37C, in the presence of calf thymus DNA
4
0.96
ATP
-
mutant K319T, pH 7.5, 37C, in the presence of calf thymus DNA
4
0.97
ATP
-
mutant R334Q, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.04
ATP
-
mutant Y508C, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.11
ATP
-
mutant S369P, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.13
ATP
-
mutant W315L, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.15
ATP
-
mutant R354P, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.23
ATP
-
mutant K319E, pH 7.5, 37C, in the presence of calf thymus DNA; mutant R357P, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.27
ATP
-
mutant R303W, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.3
ATP
-
mutant I367T, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.42
ATP
-
mutant A318T, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.53
ATP
-
wild-type without His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.55
ATP
-
wild-type wit His-tag, pH 7.5, 37C, in the presence of calf thymus DNA
4
1.67
ATP
-
mutant S369Y pH 7.5, 37C, in the presence of calf thymus DNA
4
1.83
ATP
-
mutant L381P, pH 7.5, 37C, in the presence of calf thymus DNA
4
25
ATP
-
pH and temperature not specified in the publication, mutant enzyme L189D/D191R
4
185.7
ATP
-
pH and temperature not specified in the publication, wild-type enzyme
4
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.116
2',3'-ddATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.721
2',3'-ddGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.298
2',3'-ddTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.291
2'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.097
2'-deoxythymidine 5'-phosphoryl-beta,gamma-hypophosphate
-
i.e. ppopT, dTTP analogue, inhibition of NTPase activity of NS3 protein by NTP derivatives
0.277
2'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.116
2'-dTTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.141
3'-dATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.443
3'-dGTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.26
3'-dUTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.01
actinomycin
-
pH 8.0, 37C, inhibition of DNA helicase activity
0.1
actinomycin
-
pH 8.0, 37C, inhibition of ATPase activity
0.0056
actinomycin C1
-
pH 8.0, 37C
-
1.3
ADP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
5
AMP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.69
ATP
-
recombinant nonstructural protein 3 analyzed for DNA unwinding rates, 22C, 2 mM Mg2+, 25 nM enzyme, and 5 nM substrate, pH 6.5, initiation by adding each NTP to 0.5 mM
0.145
beta,gamma-methylene-ATP
-
efficient inhibitor, like the N1-oxides N1-oxoadenosine 5'-triphosphate and N1-hydroxyinosine 5'-triphosphate
0.004
daunorubicin
-
pH 8.0, 37C
0.0052
Ethidium bromide
-
pH 8.0, 37C
0.09
GTP
-
recombinant nonstructural protein 3 analyzed for DNA unwinding rates, acts as a noncompetitive inhibitor, 22C, 2 mM MgCl2, 25 nM enzyme, and 5 nM substrate, pH 6.5, initiation by adding each NTP to 0.5 mM
0.576
GTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.205
N1-O-ATP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.109
N1-OH-ITP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
0.00071
Nogalamycin
-
pH 8.0, 37C
0.001
Nogalamycin
-
pH 8.0, 37C, inhibition of DNA helicase activity
0.017
Nogalamycin
-
pH 8.0, 37C, inhibition of ATPase activity
0.09
NTP
-
recombinant nonstructural protein 3 analyzed for DNA unwinding rates, data globally fit to a model for substrate inhibition, 22C, 2 mM MgCl2, 25 nM enzyme, and 5 nM substrate, pH 6.5, initiation by adding each NTP to 0.5 mM
1.46
UTP
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0054
(2Z)-4-[3-(benzylamino)phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity
0.012
(2Z)-4-[3-[(4-chlorobenzyl)amino]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity
0.013
(2Z)-4-[3-[(4-chlorobenzyl)oxy]phenyl]-2-hydroxy-4-oxobut-2-enoic acid
-
inhibition of duplex DNA-unwinding activity, moderate inhibition activities against helicase ATPase
0.075
5-fluoro-2-selenocytosine
-
pH 7.5, 30C
0.009
Aclarubicin
-
pH 9.0, 37C
0.002
daunorubicin
-
pH 9.0, 37C
0.005
Nogalamycin
-
pH 9.0, 37C
0.12
ribavirin 5'-triphosphate
-
pH 7.5, 30C, inhibition of helicase activity
0.4
ribavirin 5'-triphosphate
-
pH 7.5, 30C, inhibition of ATPase activity
0.06
tetrabromobenzotriazole
-
-
0.009
Doxorubicin
-
pH 9.0, 37C
additional information
additional information
-
inhibitory potential of peptides deduced from amino acid sequence of motif VI tested, 4.7 pM DNA substrate used for determination of helicase activity, HCV(1487-1500) peptide most potent enzyme inhibitor, shortening or lengthening the peptide reduces significantly the inhibitory potential of the derivatives, NTPase activity not affected
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
P27395
structural characterization of catalytic domain, mutation analysis of residue substitution in the Walker A motif (Gly199, Lys200 and Thr201), within the NTP-binding pocket (Gln457, Arg461 and Arg464) and of Arg458 in the outside of the pocket in the motif IV, residues crucial for ATPase and DNA helicase activities and virus replication, Lys200 cannot be substituted by other residues to establish sufficient activities, structure of the NTP-binding pocket well conserved among the viruses of the Flaviviridae
additional information
-
highest specific activity among plant helicases
additional information
-
molecular beacon-based helicase assay (MBHA) developed, unwinding of DNA mediated by recombinant nonstructural protein 3 occurs at different rates depending on the nature and concentration of NTPs in solution, presence of an intact NS3 protease domain makes HCV helicase somewhat less specific than truncated NS3 bearing only its helicase region specificity determined by the nature of the Watson-Crick base-pairing region of the NTP base and the nature of the functional groups attached to the 2' and 3' carbons of the NTP sugar
additional information
-
overview of sequences of NTPase/helicase motifs VI derived peptides and their deleted derivatives, kinetic analyses reveals that binding of the peptides do not interfere with the NTPase activity of the enzymes, peptides do not interact with the ATP binding site
additional information
-
DNA helicase reaction can proceed in two modes depending on the ratio between enzyme and substrate concentration, non-catalytic in the case of enzyme excess and catalytic in the case of tenfold substrate excess, structure of nucleic base and ribose fragment of NTP molecule has a slight effect on inhibitory properties, duplex DNA oligonucleotides used for determination of DNA helicase activity
additional information
-
surface of domain 2 of the NS3 NTPase/helicase in direct vicinity to a flexible loop that is localized between Val1458 and Thr1476, accessibility of the Arg-rich amino acid motif by this loop for protein kinase C inhibition analyzed, two variants of domain 2 generated, in vitro protein kinase C (PKC) phosphorylation studies, binding and competition assays, modelling of ribbon diagrams, presence of the intact loop abolishes the binding of domain 2 to a tailed duplex RNA, binding of dsDNA not affected, loop structure reduces the extent of inhibition of protein kinase C (PKC) by domain 2 and regulates the binding of dsRNA, various mechanisms by which the NS3 protein perturb signal transduction in infected cells
additional information
-
eight analogues of anti-HCV aryl diketoacide (ADK) investigated for inhibitory capacity, phosphate release assay and FRET-based assay
additional information
Q9WPH5
ambiguous helicase activity, also DNA unwinding
additional information
-
structural characterization of the C-terminal portion containing the ATPase/helicase domain, encompasses residues 181-619, monomer structure determined by analytical centrifugation and gel filtration, SDS-PAGE and immunoblotting, structure determined by circular dichroism and fluorescence spectroscopy, ATPase activity stimulated by RNA and ssDNA, DNA helicase activity assayed with different salt concentrations from 5 to 150 mM and ATP concentrations at 40, 80, 100, 250 and 500 microM, respectively, no DNA helicase activity at protein concentrations up to 500 nM, linker region between the protease and the helicase domains predicted as a prerequisite for protein-protein interactions leading to the formation of the active oligomer
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
D0KN27
assay at
6.5
-
assay at; helicase-catalyzed DNA unwinding activity at
6.6 - 8.4
P40562
-
7
-
assay at
7.4
-
activity assay at
7.4
Q9BX63
assay at
7.5
-
unwinding reaction
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.6
-
assay at
7.6
Q9UUA2
assay at
7.8
-
assay at
8
Q19546
assay at
8
A8D930
ATPase activity, DNA-unwinding activity
8
-
assay at
8
P95949
assay at
8
Q96YR7
assay at
8.8
P95479
assay at
8.9
O24736
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 35% of maximal activity, pH 9.0: about 65% of maximal activity
6.5 - 8.5
A8D930
pH 6.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity, ATPase activity
6.5 - 8.9
-
the enzyme functions efficiently over wide ranges of pH from 6.5 to 8.9
7.5 - 9
-
significant unwinding activity is observed in the broad pH range (pH 7.59.0)
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21
-
assay at room temperature
22
-
helicase-catalyzed DNA unwinding activity at
25
P0C6X7
assay at
25
P95479
assay at
29
A8D930
ATPase activity
30
-
assay at
30
P51979
assay at
30
O14867
assay at
30
Q12039
assay at
30
-
assay at
30
-
assay at
30
Q9BX63
assay at
37
P27395
assay at
37
Q19546
assay at
37
P07271
assay at
37
P9WMP9
assay at
37
-
assay at
37
P35187
assay at
37
-
assay at
37
-
assay at
37
Q9UUA2
assay at
37
-
assay at
37
-
assay at
37
-
activity assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
45
D0KN27
the assay is carried out at either 60C or 45C
60
D0KN27
the assay is carried out at either 60C or 45C
60
P95949
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 37
Q19546
similar active at 20C, 30C and 37C
25 - 34
A8D930
25C: about 55% of maximal activity, 34C: about 40% of maximal activity, ATPase activity
30 - 60
O24736
30C: about 65% of maximal activity, 60C: about 75% of maximal activity
40 - 80
-
the enzyme is active at temperatures between 40C and 80C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
A8D930
calculated from sequence
8
Q8I3W6
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
P38935
maximal level of expression is observed in late G1/early S phase
Manually annotated by BRENDA team
-
GRTH is a negative regulator of apoptosis in spermatocytes and promotes the progress of spermatogenesis
Manually annotated by BRENDA team
Q9QY16
GRTH is a negative regulator of apoptosis in spermatocytes and promotes the progress of spermatogenesis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q12039
mitochondrial localization of Hmi1p is essential for its role in mtDNA metabolism
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Adeno-associated virus 2
Adeno-associated virus 2
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50480
A8D930
calculated from sequence
693421
54000
P27395
molecular mass of the helicase/NTPase domain, SDS-PAGE
690191
63000
-
-
721107
65000
-
gel filtration, glycerol gradient analysis
690795
65000
P95949
gel filtration, monomeric form
724217
66000
-
recombinant protein of C-terminal portion the ATPase/helicase domain, residues 181-619, SDS-PAGE, gel filtration
701395
72000
-
SDS-PAGE
719883
85000
P9WMP9
sedimentation equilibrium ultracentrifugation
692829
93000
-
single subunit
720774
120000
-
gel filtration, glycerol gradient centrifugation
692155
120000
P95479
sucrose gradient centrifugation, N-terminal microsequencing
722494
128000
-
gel filtration
694413
136000
-
gel filtration
692150
137000
O57849
calculated from sequence
722629
140000
P95949
gel filtration, dimeric form
724217
170000
Q8I3W6
calculated from sequence
692470
200000
-
gel filtration, glycerol gradient centrifugation
694414
462000
-
calculated from sequence
726360
470000
-
gel filtration
725348
500000
-
gel filtration
690869
560000
-
homohexamer
720774
600000
P38935
gel filtration
694417
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
A8D930
x * 54000, SDS-PAGE
?
-
x * 90000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
P0C6X7
x * 70000, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
Q81JI8
x * 50000, SDS-PAGE
?
-
x * 180000, SDS-PAGE
?
-
x * 12000, SDS-PAGE
?
A8D930
x * 50478, calculated from sequence
?
-
x * 54000, small isoform of RECQ5 helicase, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
dimer
Q9BX63
FANCJ exists as molecular weight species corresponding to a monomer and a dimer, and the dimeric form displays a higher specific activity for ATPase and helicase, as well as greater DNA binding
dimer
P95949
2 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence, forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability
dimer
-
2 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence, forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability
-
heptamer
-
structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings
heterodimer
-
1 * 54000 + 1 * 66000, SDS-PAGE
hexamer
-
-
hexamer
-
6 * 90000, SDS-PAGE
hexamer
P38935
6 * 116000, SDS-PAGE
hexamer
-
structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings
hexamer
-
homohexamer, 6 * 93000
hexamer
-
recombinant TWINKLE assembles into hexamers and higher oligomers, and addition of MgUTP stabilizes hexamers over higher oligomers
hexamer
-
6 * 75000, 77428, calculated from sequence
hexamer
-
6 * 77428, calculated from sequence, wild-type enzyme, critical roles for hexamerization and helicase function is demonstated
hexamer
-
the enzyme has an unusual mode of ATP usage where localized cooperativity exists between pairs of subunits within the hexameric assembly. The allosteric communication loop mediates intersubunit communication
hexamer
-
6 * 75000, 77428, calculated from sequence, 6 * 77428, calculated from sequence, wild-type enzyme, critical roles for hexamerization and helicase function is demonstated
-
homohexamer
P20356
6 * 30000
homohexamer
-
critical roles for hexamerization and helicase function
homohexamer
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
homohexamer
-
the mini-chromosome maintenance complex binds as a hexamer and slides on the end of a 3'-extended single-stranded DNA tail of a Y-shaped substrate. Binding is oriented so that the motor domain of the protein faces duplex DNA
homohexamer
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity, the mini-chromosome maintenance complex binds as a hexamer and slides on the end of a 3'-extended single-stranded DNA tail of a Y-shaped substrate. Binding is oriented so that the motor domain of the protein faces duplex DNA, critical roles for hexamerization and helicase function
-
monomer
-
1 * 128000, SDS-PAGE
monomer
-
1 * 63000, SDS-PAGE
monomer
-
1 * 71000, SDS-PAGE
monomer
-
1 * 135000, SDS-PAGE
monomer
P9WMP9
1 * 85000, the lack of cooperativity observed for both the ATPase and helicase activities lends support to the view that UvrD monomers are the functional unit
monomer
-
BcMCM is a monomer in solution but likely forms the functional oligomer in vivo
monomer
-
alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration
monomer
Q9BX63
FANCJ exists as molecular weight species corresponding to a monomer and a dimer, and the dimeric form displays a higher specific activity for ATPase and helicase, as well as greater DNA binding
monomer
P95479
the monmomeric protein contains a helicase-like module and a type I topoisomerase module
monomer
P95949
1 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence, forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability
monomer
-
1 * 85000, the lack of cooperativity observed for both the ATPase and helicase activities lends support to the view that UvrD monomers are the functional unit
-
monomer
-
1 * 100393, the enzyme possesses two different oligomeric states, calculated from sequence, forms monomers and dimers in solution. Only the monomeric form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability
-
octamer
-
structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings
oligomer
-
recombinant TWINKLE assembles into hexamers and higher oligomers, and addition of MgUTP stabilizes hexamers over higher oligomers
oligomer
-
the enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP). Both N-terminal and C-terminal portions of ORF735 (87 and 160 amino acid residues, respectively, in size) are required for protein dimerization but dispensable for the formation of the higher-order oligomer. The protein unwinds DNA only as a large oligomer
oligomer
-
the enzyme exists in solution as a salt-stable dimer and is capable of assembling into a salt-sensitive oligomer that is significantly larger than a hexamer in the presence of a divalent cation (Mg2+) and an adenine nucleotide (ATP, dATP, or ADP) or its analog (ATPgammaS or AMPPNP). Both N-terminal and C-terminal portions of ORF735 (87 and 160 amino acid residues, respectively, in size) are required for protein dimerization but dispensable for the formation of the higher-order oligomer. The protein unwinds DNA only as a large oligomer
-
monomer
West Nile virus WNV
-
alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration
-
additional information
Q89270
posttranslational modifications lacking in in vitro- or bacterially synthesized Rep52 may be required for efficient Rep52 multimerization
additional information
-
in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex. The complex is composed of a HerA hexamer bound to a NurA dimer
additional information
-
in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex. The complex is composed of a HerA hexamer bound to a NurA dimer
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of the helicase domain of bacteriophage T7 gene 4 protein
-
1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to ATPgammaS
P15043
hanging-drop vapour-diffusion method with polyethyleneglycol monomethyl ether as precipitating agent
P20356
purified RECQ1T1 protein is crystallized in the presence of ATP-gammaS and oligonucleotides by vapor diffusion from sitting drops equilibrated against 0.2 M sodium bromide, 20% PEG 3350, 10% ethylene glycol, 0.1 M bis-Tris propane (pH 7.5). Crystal structure of a truncated form (RECQ1(T1)) of the human RECQ1 protein with MgADP2-
P46063
enzymatically active fragment of the JEV NTPase/helicase catalytic domain, recombinant protein, crystal structure determined at 1.8 A resolution, data collection and refinement statistics
P27395
crystallization of the Hef helicase domain (HefN546, residues 1546)
-
hanging drop method at pH 7.6, crystal structure of a nearly full-length MCM hexamer that is helicase-active and thus has all features essential for unwinding DNA. The structure is a chimera of Sulfolobus solfataricus N-terminal domain and Pyrococcus furiosus ATPase domain. The chimera protein construct consists of SsoMCMN, (SsoMCM aa 1269) fused to PfMCMAAA (PfMCM aa 257361/729966 = aa 257966 with its intein, aa 362728, removed)
-
hanging drop vapor diffusion technique, high-resolution crystal structures of the enzyme in two apo-states and two nucleotide bound forms, at resolutions of 2.02.7 A
O73946
all solved XPD structures contain two Rad51/RecQ-like domains (HD1 and HD2) with two additional domains, the Fe-S and Arch domains, inserted between adjacent beta-strands of the central beta-sheet of HD1
-
2.8 A crystal structure of the N-terminal domain (residues 1-268), sitting drop vapor diffusion technique at room temperature
-
4.35 A crystal structure of the near-full-length enzyme; 4.35 A crystal structure of the near-full-length enzyme. The structure shows an elongated fold, with 5 subdomains that are organized into 2 large N- and C-terminal domains; 4.35 A crystal structure of the near-full-length ssoMCM. The structure shows an elongated fold, with 5 subdomains that are organized into two large N- and C-terminal domains
-
crystals are grown from hanging-drops
D0KN27
hanging drop method at pH 7.6, crystal structure of a nearly full-length MCM hexamer that is helicase-active and thus has all features essential for unwinding DNA. The structure is a chimera of Sulfolobus solfataricus N-terminal domain and Pyrococcus furiosus ATPase domain. The chimera protein construct consists of SsoMCMN, (SsoMCM aa 1269) fused to PfMCMAAA (PfMCM aa 257361/729966 = aa 257966 with its intein, aa 362728, removed)
-
sitting-drop vapor diffusion at 20C, 2.25 A crystal structure
Q971R4
crystal structure in complex with a short DNA fragment is reported
-
vapor diffusion in hanging drop method
-
hanging-drop vapour diffusion at room temperature
Q9WY48
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 95
-
no unfolding in the temperature range 3095C, indicating that its Tm is greater than 95C
726073
42
-
wild-type protein has a half-liife if 7.9 min at 42C
719883
56
-
1 min, inactivated
692150
56
-
1 min, loss of activity
692155
60
A8D930
enzyme is heat labile and loses its activity upon heating at 60C for 1 min
693421
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is destroyed if trypsin is included in the reaction
-
trypsin destroys activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, DNA helicase VI loses 90% of its activity in 24 h
-
4C, inactivation after prolonged storage
-
-70C, loses 25% of its activity following storage for 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme recombinantly expressed in Escherichia coli
-
gel filtration
Q9WPH5
gel filtration, recombinant nonstructural protein 3
-
gel filtration, recombinant protein
-
gel filtration, SDS-PAGE
-
truncated and full-length complexes between nonstructural protein 3 (NS3) and nonstructural protein 4A (NS4), NS3-4A complex purifies as two separable proteins, gel filtration, SDS-PAGE
-
a construct (RECQ1(T1)) encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa is produced in Escherichia coli and purified to more than 95% homogeneity
P46063
full-length PIF1 with a 6* histidine tag at the N-terminus, a C-terminal truncated form (PIF1N) and a N-terminal truncated form (PIF1C)
-
generation of recombinant baculovirus encoding the human TWINKLE gene, expression in insect cells
-
recombinant
-
streamlined purification for the production of near-homogeneous and high yield recombinant forms of the human mitochondrial DNA helicase, minimizing the number of steps and the time elapsed for purification
-
using Ni-NTA chromatography
-
one-step column purification of helicaseprimase subcomplex (helicase-primase enzyme complex consisting of UL5 and UL52 gene functions) using C-terminally His-tagged UL5 subunit
-
gel filtration, recombinant protein
P27395
recombinant histidine-tagged form of the protein
P9WMP9
recombinant
Q12039
recombinant enzyme
Q06218
recombinant Sgs1 fragment (amino acids 4001268 of the 1447-amino acid full-length protein)
P35187
gel filtration, recombinant protein, soluble form
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
A8D930
PcrA protein is overexpressed with a His6 fusion at its amino-terminal end
Q6I4A9
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3), recombinant protein, NS3d2wt variant corresponding to wild-type domain 2, NS3d2D construct comprises the complete domain, HCV(1361-1503) without loop, pET21b andpET16b vectors
-
expressed in Escherichia coli, strain Rosetta (DE3), recombinant nonstructural protein 3
-
expressed in Escherichia coli, strains XL-1 Blue, Rosetta (DE3), M15 (pREP4), vector pET-21-2c, kinetics of NS3 protein accumulation upon its expression in Escherichia coli at 25C for 1-5 h shown
-
NS3-plus and NS3/4a-plus genes expressed in Escherichia coli, composition of NS3-4A expression product using the pet-SUMO vector
Q9WPH5
NS3-plus and NS3/4a-plus genes expressed in Escherichia coli, generation of NS3-4A expression product, pET15b and pet-SUMO vector
-
a construct (RECQ1(T1)) encompassing amino acids 49616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa is produced in Escherichia coli
P46063
expressed in Hi5 insect cells
-
expressed in insect cells using the baculovirus expression system
Q9BX63
expressed in SF9 cells as His-tagged fusion proteins lacking the N-terminal mitochondrial targeting signal using the baculovirus expression system
-
expression in Escherichia coli
P38935
human hPif1 (nuclear form amino acids 1641) and the hPif helicase domain (hPifHD, amino acid residues 206620) are cloned as a fusion protein with glutathione S-transferase in pET11c. GST-hPifHD is expressed in Escherichia coli BL21(DE3) cells
-
overexpressed in Escherichia coli as His-tagged fusion proteins
-
overexpression of an oligohistidine-tagged version of the BLM gene product in Saccharomyces cerevisiae
-
baculovirus expression system
P0C6X1
His6-tagged DNA helicase expressed via recombinant baculovirus
-
expressed in Escherichia coli BL21 (DE3), recombinant protein, pET21b vector
P27395
-
Q8VID5
expressed in Escherichia coli
-
histidine-tagged form of the protein is expressed
P9WMP9
expression in Escherichia coli
-
a recombinant Sgs1 fragment (amino acids 4001268 of the 1447-amino acid full-length protein) is overexpressed in yeast
P35187
expression in Escherichia coli
-
expression of a recombinant Dbp9p in Escherichia coli
Q06218
expression of a truncated version of Rrm3p as a GST fusion protein in Saccharomyces cerevisiae. This polypeptide (Rrm3pDELTAN), contains amino acids 194 to 723 of the 723-amino-acid protein, including all seven helicase motifs as well as 56 amino acids amino-terminal of the first helicase motif. Rrm3pDELTAN is expressed under the control of a galactose-inducible promoter
P07271
the carboxyl-terminal His6 epitope is attached to the MPH1-coding sequence and the tagged gene is placed under the galactose inducible GAL1 promoter in the vector pYES
P40562
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli
Q4JC68
construction of an overexpression cassette of an HMG-CoA reductase gene and its application as a selectable marker for shuttle vectors of Sulfolobus islandicus. High-level expression of the His6-tagged HerA helicase is obtained with the cells harboring pSSRAherA. The establishment of two efficient selectable markers (pyrEF and hmg) is subsequently exploited for genetic analysis. A herA merodiploid strain of Sulfolobus islandicus is constructed using pyrEF marker and used as the host to obtain pSSRNherA transformant with simvastatin selection. While the gene knockout (herA) cells generated from the herA merodiploid cells fail to form colonies in the presence of 5-fluoroorotic acid, the mutant cells could be rescued by expression of the gene from a plasmid (pSSRNherA), because their transformants form colonies on a solid medium containing 5-fluoroorotic acid and simvastatin
F0NFK8
expressed in Escherichia coli in soluble form; expression in Escherichia coli
P95949
expression in Escherichia coli
-
expression in Escherichia coli, wild-type and site-directed mutants
D0KN27
expressed in Escherichia coli
-
expressed in Escherichia coli, C-terminal portion with the ATPase/helicase domain, plasmid pET-30a
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MCM6 promoter contains cis-elements which are related to salt, drought, ABA cold and wound stresses
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K116H
Q89270
an MBP-Rep52 chimera bearing K116H mutation within a consensus helicase- and ATPase-associated motif (motif I or Walker A site) is deficient for both DNA helicase and ATPase activities
K340H
Q89270
in a Rep78 A-site mutant protein bearing mutation K340H, the MBP-Rep52 A-site mutant protein fails to exhibit a trans-dominant negative effect when it is mixed with wild-type MBP-Rep52 or MBP-Rep78 in vitro
C261A
-
mutant with a disrupted zinc-binding site. One mol of the C261A mutant contains 0.03 atoms
K653A
-
mutation of the ATP-binding site reduces activity to about 30% of wild-type. This drop in ATPase activity corresponds to an abrogation of helicase activity observed in the same mutant
D470A
-
mutant supports growth of T7DELTA4 phage lacking gene 4 similar to wild-type, hydrolysis of dTTP similar to wild-type, stimulation in ssDNA-dependent hydrolysis catalyzed is about 15-45% of that observed with wild-type helicase, mutant shows 2fold lower affinity for the ssDNA compared to wild-type. Compared to wild-type mutant retains 30% DNA unwinding using a short duplex DNA
H465A
-
mutant does not support growth of T7DELTA4 phage lacking gene 4, hydrolysis of dTTP is not stimulated by the presence of ssDNA, mutant shows 2fold lower affinity for the ssDNA compared to wild-type. Mutant does not exhibit any significant level of DNA unwinding using a short duplex DNA
K467A
-
mutant supports growth of T7DELTA4 phage lacking gene 4 similar to wild-type, hydrolysis of dTTP similar to wild-type, stimulation in ssDNA-dependent hydrolysis catalyzed is about 15-45% of that observed with wild-type helicase, mutant shows 10fold lower affinity for the ssDNA compared to wild-type. Mutant unwinds DNA poorly and exhibits less than 5% of the wild-type activity. Mutant forms more heptamers than hexamers as compared to the wild-type gp4
K471A
-
mutant supports growth of T7DELTA4 phage lacking gene 4 similar to wild-type, hydrolysis of dTTP similar to wild-type, stimulation in ssDNA-dependent hydrolysis catalyzed is about 15-45% of that observed with wild-type helicase, mutant shows 2fold lower affinity for the ssDNA compared to wild-type. Compared to wild-type mutant retains 30% DNA unwinding using a short duplex DNA. Mutant forms more heptamers than hexamers as compared to the wild-type gp4
K473A
-
mutant supports growth of T7DELTA4 phage lacking gene 4 similar to wild-type, hydrolysis of dTTP similar to wild-type, stimulation in ssDNA-dependent hydrolysis catalyzed is about 15-45% of that observed with wild-type helicase, mutant shows 2fold lower affinity for the ssDNA compared to wild-type. Compared to wild-type mutant retains 30% DNA unwinding using a short duplex DNA. Mutant forms more heptamers than hexamers as compared to the wild-type gp4
L466A
-
mutant does not support growth of T7DELTA4 phage lacking gene 4, hydrolysis of dTTP is not stimulated by the presence of ssDNA, mutant shows much lower affinity for the ssDNA compared to wild-type. Mutant does not exhibit any significant level of DNA unwinding using a short duplex DNA
N468A
-
mutant does not support growth of T7DELTA4 phage lacking gene 4, hydrolysis of dTTP is not stimulated by the presence of ssDNA, mutant shows much lower affinity for the ssDNA compared to wild-type. Mutant does not exhibit any significant level of DNA unwinding using a short duplex DNA
H293A
-
mutation results in a protein with a significantly higher level of ATPase in the absence of RNA. The mutant protein still unwinds RNA. In the presence of RNA, the H293A mutant hydrolyzes ATP slower than wild-type
A318T
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type
A349P
Q9BX63
expression of a FANCJ mutant protein with a pathogenic A349P amino acid substitution in a wild-type background exerts a dominant negative effect on resistance to DNA cross-linking agents or TMS
A359T
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
A475P
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows lowest kcat (ATP) value
DELTAQ25
Q9BX63
mutant bearing a deletion of Q25 shows a similar phenotype as Q25A
F485L
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
I367T
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type, mutant shows a higher Km (ATP) and kcat value compared to wild-type
K319E
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type
K319T
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
K421A
-
the Walker A mutant K421A of TWINKLE fails to unwind dsDNA
K52R
Q9BX63
mutant is seriously compromised in its ATPase activity, kcat (ATP) highly decreased compared to wild-type
P335L
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
Q25A
Q9BX63
Q25A mutation of the invariant glutamine in the Q motif abolishes its ability to complement cisplatin or telomestatin sensitivity of a fancj null cell line and exerts a dominant negative effect. Mutant shows impaired FANCJ helicase activity and ATPase activity but displays ATP binding and temperature-induced unfolding transition similar to wild-type. Mutant exists only as a monomer. Km (ATP) increased compared to wild-type, kcat 10fold decreased compared to wild-type
R112H
-
most common mutations in TTD patients, amino acid substitution R112H, is localized in the Fe-S domain of XPD just before the first conserved cysteine residue. Missense mutation results in a complete loss of XPD helicase activity and a reduced basal transcription activity of the TFIIH complex
R303W
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type, mutant is much more sensitive to heat inactivation than wild-type
R334Q
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
R354P
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
R357P
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type
R374Q
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a higher Km (ATP) value compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) and a 2fold increase in Kd (ssDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
S369P
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
S369Y
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) increased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
T457I
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
W315L
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
W474C
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
Y508C
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type
D523N
P04014
DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity
D542N
P04014
DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity
K484E
P04014
mutant enzyme binds the immunoaffinity column poorly, the heparin purified E1/K484E is tested for the above activities. The protein that is recovered shows no activity
K337A
Q9UUA2
K337A and the K337R alleles are unable to supply the essential function of Pfh1p
K337R
Q9UUA2
K337A and the K337R alleles are unable to supply the essential function of Pfh1p
A349P
Q4JC68
mutation destabilizes the Fe-S cluster and abolishes helicase activity
C105S
Q4JC68
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
C137S
Q4JC68
mutant enzyme contains no Fe-S cluster
R112H
Q4JC68
mutation destabilizes the Fe-S cluster and abolishes helicase activity
A349P
-
mutation destabilizes the Fe-S cluster and abolishes helicase activity
-
C105S
-
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
-
C137S
-
mutant enzyme contains no Fe-S cluster
-
C88S
-
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
-
R112H
-
mutation destabilizes the Fe-S cluster and abolishes helicase activity
-
A416R/A420R
-
mutant shows no helicase activity, near abrogation of helicase activity, no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
D327A
-
about 75% of wild-type helicase activity
D488A
-
mutant has an apparent increase in helicase activity but a reduction in ATPase activity to approximately one third of wild-type levels. This mutant has a gel filtration profile compatible with a dimer or trimer. All other proteins appear hexameric
delE199R211
-
replacement of the loop residues E199R211 with the tripeptide serineasparagineglyine. The mutant with a deletion in ACL (allosteric communication loop) has no detectable helicase activity even at high protein concentrations. The ATPase activity of the mutant is severely reduced and shows no DNA stimulation
E202A/E203A/Q207A
-
mutant has severely impaired DNA helicase activity. The mutant shows lower ATPase activity than wild type, and the ATPase activity is stimulated to a lesser extent by DNA
E202G/E203G/V204G
-
mutant shows no helicase activity
E307A
-
inactive in DNA unwinding and partially active in the ATPase assay
E326A
-
about 95% of wild-type helicase activity
E326A/D327A
-
about 85% of wild-type helicase activity
E326A/D327A/R329A
-
mutant shows no helicase activity
E422A
-
up to 2fold higher affinity for the DNA substrate than the wild-type enzyme. ATPase activity and helicase activity are similar to wild-type enzyme
E422R
-
has the same affinity as the wild-type enzyme. No ability to hydrolyse ATP, no helicase activity
E422R/R329E
-
mutant lacks detectable ATPase and helicase activities
H146A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity, the purified mutant enzyme retains full ATPase activity
I555D/L556S/I557D
-
mutant shows no helicase activity
K129A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity, the purified mutant enzyme retains full ATPase activity
K134A
-
mutation affects binding to duplex DNA molecules, whereas it has no effect on binding to single-stranded DNA and on the DNA unwinding activity, the purified mutant enzyme retains full ATPase activity
K194A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity, the purified mutant enzyme retains full ATPase activity
K246A/R247A
-
indistinguishable from wild-type protein with respect to heat stability. ATPase activity of the mutated protein does not increase in the presence of DNA. Mutation reduces DNA binding
K246A/R247A/K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
K265A/E307A
-
completely abolished ATPase activity
K265A/R372I
-
completely abolished ATPase activity
K323A
-
about 40% of wild-type helicase activity
K323A
-
reduced helicase activity
K323A/R440A
-
reduced helicase activity
K346A
-
ATPase activity of the mutant is noticeably reduced, although not completely abolished, it is almost completely devoid of helicase activity
K346A
-
no ATPase activity, no helicase activity
K366E
-
severely compromised helicase activity but only a modest reduction in ATPase activity
K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
K52A
D0KN27
mutant is unable to function as a helicase
K646stop
D0KN27
mutant lacking domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
L189D/D191R
-
mutant shows no helicase activity, near abrogation of helicase activity, no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
L325A
-
about 40% of wild-type helicase activity
L565D
-
has the same affinity as the wild-type enzyme. ATPase properties similar to wild-type enzyme, significant stimulation of helicase activity
R255A
D0KN27
mutant shows significantly reduced helicase activity
R320A
D0KN27
mutant shows significantly reduced helicase activity
R329A
-
about 50% of wild-type helicase activity
R329E
-
up to 2fold lower affinity for the DNA substrate than the wild-type enzyme. Low and non-DNA-stimulated ATPase activity. Helicase activity is similar to wild-type enzyme
R331A
-
no ATPase activity, no helicase activity
R331I
-
has the same affinity as the wild-type enzyme. No ability to hydrolyse ATP, no helicase activity
R331K
-
up to 2fold higher affinity for the DNA substrate than the wild-type enzyme. ATPase properties similar to wild-type enzyme. Helicase activity at approximately half the level of wild-type enzyme
R359A
-
severely compromised helicase activity but only a modest reduction in ATPase activity
R372I
-
very low levels of ATPase activity and no helicase activity
R440A
-
reduced helicase activity
R662A
D0KN27
mutant lacking the first arginine of the RAR motif in domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
T374A
-
reduced but detectable helicase activity with an increase in ATPase activity
T550G/P551G/D552G/S553G/P554G
-
mutant shows no helicase activity
V324A
-
about 90% of wild-type helicase activity
V324A/L325A
-
about 80% of wild-type helicase activity
K52A
-
mutant is unable to function as a helicase
-
K646stop
-
mutant lacking domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
-
R255A
-
mutant shows significantly reduced helicase activity
-
R320A
-
mutant shows significantly reduced helicase activity
-
R662A
-
mutant lacking the first arginine of the RAR motif in domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
-
A416R/A420R
-
mutant shows no helicase activity, near abrogation of helicase activity
-
D327A
-
about 75% of wild-type helicase activity
-
D488A
-
mutant has an apparent increase in helicase activity but a reduction in ATPase activity to approximately one third of wild-type levels. This mutant has a gel filtration profile compatible with a dimer or trimer. All other proteins appear hexameric
-
E307A
-
inactive in DNA unwinding and partially active in the ATPase assay
-
E326A
-
about 95% of wild-type helicase activity
-
H146A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity, the purified mutant enzyme retains full ATPase activity
-
K129A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity, the purified mutant enzyme retains full ATPase activity
-
K134A
-
mutation affects binding to duplex DNA molecules, whereas it has no effect on binding to single-stranded DNA and on the DNA unwinding activity
-
K246A/R247A
-
indistinguishable from wild-type protein with respect to heat stability. ATPase activity of the mutated protein does not increase in the presence of DNA. Mutation reduces DNA binding
-
K246A/R247A/K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
-
K265A/E307A
-
completely abolished ATPase activity
-
K265A/R372I
-
completely abolished ATPase activity
-
K323A
-
about 40% of wild-type helicase activity
-
K346A
-
ATPase activity of the mutant is noticeably reduced, although not completely abolished, it is almost completely devoid of helicase activity, no ATPase activity, no helicase activity
-
K366E
-
severely compromised helicase activity but only a modest reduction in ATPase activity
-
K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
-
R331A
-
no ATPase activity, no helicase activity
-
R359A
-
severely compromised helicase activity but only a modest reduction in ATPase activity
-
R372I
-
very low levels of ATPase activity and no helicase activity
-
T374A
-
reduced but detectable helicase activity with an increase in ATPase activity
-
E355A
Q96YR7
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
E355A
Sulfolobus tokodaii 7
-
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
-
P469A
-
mutant supports growth of T7DELTA4 phage lacking gene 4 similar to wild-type, hydrolysis of dTTP similar to wild-type, stimulation in ssDNA-dependent hydrolysis catalyzed is about 15-45% of that observed with wild-type helicase
additional information
-
site-directed mutagenesis of the four conserved cysteines of the Fe-S cluster in the Rad3 (XPD) helicase from Ferroplasma acidarmanus (FacXPD) revealed that the integrity of the domain is required for the proper folding and structural stability of the auxiliary domain and is important for coupling ATP hydrolysis to unidirectional translocation of helicase
L381P
-
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) increased compared to wild-type, mutant shows a higher Km (ATP) and kcat value compared to wild-type
additional information
-
His-tagged HDHB fragments incubated with glutathione beads bind to GST-RPA70N. HDHB residues 394-958 and 459-811 bind specifically to GST-RPA70N beads, demonstrating a specific interaction between HDHB 459-811 and RPA70N
P479S
P04014
DNA binding and ATPase activity is comparable to wild-type enzyme, 50% of in vitro replication activity compared to wild-type enzyme
additional information
-
a mutation of the zinc finger motif of the MCM protein reduces single-stranded and double-stranded DNA binding and abolishes helicase activity. Removal of the HTH domain from the MCM protein results in an enzyme with increased ATPase and helicase activity. A mutation of the MCM N-terminal beta-hairpin completely abolishes DNA binding and helicase activity
C88S
Q4JC68
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
additional information
-
mutations of the Fe-S domain, including the conserved cysteines, abolishes SaXPD helicase activity and destabilizes tertiary structure, attesting to the structural importance of the Fe-S domain
L565K
-
up to 2fold lower affinity for the DNA substrate than the wild-type enzyme. ATPase properties similar to wild-type enzyme, significant stimulation of helicase activity
additional information
-
a mutation of the MCM N-terminal beta-hairpin reduces but does not abolish DNA binding and helicase activity
additional information
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
L189D/D191R
-
mutant shows no helicase activity, near abrogation of helicase activity, no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
-
additional information
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
peptide inhibitors reproducing the structure of the autoregulatory motif as possibility to develop effective antivirals
pharmacology
P27395
conservation of the NTP-binding pocket among viruses of the family Flaviviridae as potential for development of therapeutics
medicine
Q8I3W6
UvrD helicase is a potential drug targets for chemotherapy of malaria. As Plasmodium falciparum contains only one homologue of UvrD helicase and human lacks this helicase, detailed studies including cloning and characterization of UvrD helicase of malaria parasite may be helpful in identifying a compound that has no effect on the cellular machinery of the host and consequently could be used as the potential drug for the treatment of malaria