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2'(3')-O-(N-methylanthraniloyl)ATP + H2O
2'(3')-O-(N-methylanthraniloyl)ADP + phosphate
Substrates: the fluorescent ATP analogue is used throughout all experiments to provide a complete ATPase cycle for a single nucleotide species
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ATP + H2O
ADP + phosphate
CTP + H2O
CDP + phosphate
dATP + H2O
dADP + phosphate
dCTP + H2O
dCDP + phosphate
dGTP + H2O
dGDP + phosphate
dTTP + H2O
dTDP + phosphate
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Substrates: NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
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GTP + H2O
GDP + phosphate
single-stranded M13 viral form DNA annealed to a radiolabeled 91-mer oligonucleotide
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Substrates: the enzyme possesses an ATPase activity that is strongly stimulated by either single- or double-stranded DNA. Moreover, the enzyme exhibits ATP- and Mg2+-dependent DNA helicase activity that displays 3'-5' directionality
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UTP + H2O
UDP + phosphate
additional information
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ATP + H2O
ADP + phosphate
Substrates: DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: involved in DNA recombination, repair and genome stability maintenance
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ATP + H2O
ADP + phosphate
Substrates: AtMCM3 preferentially utilize ATP and dATP
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
-
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
Products: -
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ATP + H2O
ADP + phosphate
Substrates: an aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase
Products: -
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ATP + H2O
ADP + phosphate
Substrates: rates of DNA unwinding catalyzed by wild-type RecQ and truncated RecQ mutants are measured at the single molecule level using a 1.2 kb hairpin ssDNA substrate, method, overview
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: catalytic DNA helicase activity is coupled with NTPase and is stimulated by ATP
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 3'-5' helicase activity
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: the enzyme unwinds DNA in the 3'-5' direction with respect to the strand to which the enzyme is bound
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: radioactive enzyme activity assay with gamma-32P-ATP
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
-
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: the enzyme preferentially binds to fork-related Y-structured DNAs and unwinds their double-stranded regions
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: Arg329 is a key residue in the communication between the DNA-binding site of SsoMCM and the trans component of the ATPase active site
Products: -
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ATP + H2O
ADP + phosphate
Substrates: ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: ATP-dependent DNA helicase activity
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: dATP and ATP support DNA unwinding reaction
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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
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ATP + H2O
ADP + phosphate
Substrates: 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
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ATP + H2O
ADP + phosphate
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Substrates: 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 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
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ATP + H2O
ADP + phosphate
Substrates: the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
Products: -
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ATP + H2O
ADP + phosphate
Substrates: -
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: 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 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
Products: -
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ATP + H2O
ADP + phosphate
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Substrates: ATP-dependent DNA helicase activity
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate
Substrates: the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
Products: -
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ATP + H2O
ADP + phosphate
Substrates: ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail
Products: -
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ATP + H2O
ADP + phosphate
Substrates: dATP and ATP support DNA unwinding reaction
Products: -
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ATP + H2O
ADP + phosphate
Substrates: 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
Products: -
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ATP + H2O
ADP + phosphate