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5'-CCTGGCAGTT + H2O
?
-
synthetic labeled deoxydecanucleotide, cleavage of 5'-Ap*G bond and with lower activity of Gp*T, Cp*A, and Gp*G bonds
-
-
?
B-form DNA + H2O
?
-
B form of herring testis DNA
-
-
?
B-Z-hybrid form DNA + H2O
?
-
hybrid B-Z form of herring testis DNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
ds-oligoDNA + H2O
?
-
-
-
-
?
flap DNA + H2O
?
-
-
-
-
?
highly polymerized DNA + H2O
?
-
-
-
-
?
lambda DNA + H2O
?
-
-
size of linear DNA fragments decreases with prolonged incubation time
-
?
lambda phage DNA + H2O
?
-
-
-
-
?
M13 flap DNA + H2O
?
-
-
small fragment of 5-10 nucleotides
-
?
M13 mp19 (+) DNA + H2O
?
-
-
small fragment of 5-8 nucleotides
-
?
poly(A) + H2O
?
-
more rapidly degraded than native DNA
-
-
?
poly(C) + H2O
?
-
more rapidly degraded than native DNA
-
-
?
poly(dA) + H2O
?
-
more rapidly degraded than native DNA
-
-
?
poly(dA)poly(dT) + H2O
?
-
more rapidly degraded than native DNA
-
-
?
poly(dC) + H2O
?
-
-
-
-
?
poly(dT) + H2O
?
-
-
-
-
?
poly(G) + H2O
?
-
-
-
-
?
polyA + H2O
?
-
synthetic homopolyribonucleotide
-
-
?
polyC + H2O
?
-
synthetic homopolyribonucleotide
-
-
?
polyG + H2O
?
-
synthetic homopolyribonucleotide
-
-
?
polyU + H2O
?
-
synthetic homopolyribonucleotide
-
-
?
pUC18 DNA + H2O
?
-
covalently closed circular plasmid DNA
substrate converted into relaxed circular form and than to the linear form
-
?
pUC19 DNA + H2O
?
-
relaxation of the supercoiled DNA and cutting of the open circular DNA to a linear form
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
ss-oligoDNA + H2O
?
-
-
-
-
?
supercoiled plasmid DNA + H2O
?
-
-
-
-
?
additional information
?
-
3'-nucleotides + H2O
?
-
e.g. 3'-AMP
-
-
?
3'-nucleotides + H2O
?
-
e.g. 3'-AMP
-
-
?
3'-nucleotides + H2O
?
-
e.g. 3'-AMP
-
-
?
3'-nucleotides + H2O
?
-
e.g. 3'-AMP
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
Azotobacter agilis
-
-
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
heat denatured
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
native double-stranded
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
partially degraded DNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
hydrolysis rate about 3 times more slowly than compared to RNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
single-stranded DNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
heat denatured
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
native double-stranded
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
cleaves supercoiled DNA only at specific sites
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
single-stranded DNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
cleaves supercoiled DNA only at specific sites
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
DNA is slightly preferred as a substrate than RNA
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
cleaves supercoiled DNA only at specific sites
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
cleaves supercoiled DNA only at specific sites
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
native double-stranded
-
-
?
DNA + H2O
5'-phosphonucleotides + 5'-phosphomononucleotides
-
single-stranded DNA
-
-
?
DNA + H2O
?
-
tritium labeled DNA from Escherichia coli, fragmented by limited sonication
random DNA cleavage with respect to all possible phosphodiester bonds
-
?
DNA + H2O
?
dsDNA to ssDNA preference ratio for Par_DSN-t4 is equal to 10, corresponding ratio for intact Par_DSN is equal to 1000
-
-
?
DNA + H2O
?
protein and DNA are held together by a mix of salt-bridges, water-mediated and direct hydrogen bond interactions between the protein and DNA backbone, almost no DNA bases are directly involved in the contacts
-
-
?
DNA + H2O
?
in absence of Mg2+ the enzyme shows a preference for DNA as compared to RNA
-
-
?
DNA + H2O
?
Serratia marcescens nuclease is highly effective on sputum
-
-
?
dsDNA + H2O
?
-
primarily responsible for internucleosomal DNA cleavage during the terminal stages of apoptosis, preference for cleaving the internucleosomal linker regions in chromatin
fragments possessing ends with 5-phosphate and 3-hydroxyl groups, exclusively double strand breaks (primarily blunt ends)
-
?
dsDNA + H2O
?
-
-
DNA fragments carrying phosphate groups at 5' ends and hydroxyl group at the 3' ends
-
?
dsDNA + H2O
?
-
physiological function currently unknown
DNA fragments carrying phosphate groups at 5' ends and hydroxyl group at the 3' ends, random DNA cleavage with respect to all possible phosphodiester bonds
-
?
dsDNA + H2O
?
-
hydrolysis of nucleic acids
-
-
?
poly(I) + H2O
?
-
-
-
-
?
poly(I) + H2O
?
-
synthetic homopolyribonucleotide
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
Azotobacter agilis
-
polyuridylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
Azotobacter agilis
-
polycytidylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
Azotobacter agilis
-
e.g.: polyadenylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
Azotobacter agilis
-
not polyguanylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
polyguanylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
rRNA
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
tRNA
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
rRNA
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
polyuridylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
polycytidylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
e.g.: polyadenylic acid
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
highest activity against poly(U)
-
-
?
RNA + H2O
5'-phosphooligonucleotides + 5'-phosphomononucleotides
-
poly(dC)
-
-
?
RNA + H2O
?
-
-
-
-
?
RNA + H2O
?
in absence of Mg2+ the enzyme shows a preference for DNA as compared to RNA
-
-
?
RNA + H2O
?
-
hydrolysis of nucleic acids
-
-
?
ssDNA + H2O
?
-
more rapidly degraded than native DNA
-
-
?
ssDNA + H2O
?
-
-
small fragment of 8-20 nucleotides
-
?
ssDNA + H2O
?
-
hydrolysis of nucleic acids, preference for ssDNA
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
Azotobacter agilis
-
hydrolysis of shorter chains much slower than of longer chains
-
-
?
additional information
?
-
-
enzyme also shows 3'-nucleotidase activity
-
-
?
additional information
?
-
-
single-stranded DNA, single-stranded RNA, double-stranded RNA nor RNA-DNA heteroduplexes are not substrates for the enzyme
-
-
?
additional information
?
-
-
inactive towards 3'-phosphoester linkage of nucleoside cyclic 2',3'- and 3',5'-monophosphates
-
-
?
additional information
?
-
-
enzyme also shows 3'-nucleotidase activity
-
-
?
additional information
?
-
-
3'-nucleotidase activity is greater for purine than for pyrimidine ribonucleotides
-
-
?
additional information
?
-
-
little activity towards ribonucleoside 2'- and 5'-monophosphates and deoxyribonucleoside 3'- and 5'-monophosphates
-
-
?
additional information
?
-
-
poly(dC)poly(dG) is not substrate for the enzyme
-
-
?
additional information
?
-
-
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
-
-
?
additional information
?
-
-
linear flap structures with tails of more than 20 nucleotides and shorter duplex regions are not hydrolyzed
-
-
?
additional information
?
-
-
the subunits of the dimer function independently as monomers, molecular dynamic simulations involving Mg2+, modelling of complex building with DNA
-
-
?
additional information
?
-
-
the enzyme potently degrades both DNA and RNA and is a nuclease with broad specificity, but it shows some sensitivity to the secondary structure of the substrate
-
-
?
additional information
?
-
-
substrate is highly polymerized herring testis DNA of the random nucleotide sequence. Hydrolysis of the B-form and hybrid B-Z form DNA by the enzyme. The hybrid B-Z form is formed upon addition of MgSO4 and Co(NH3)6Cl3
-
-
?
additional information
?
-
-
substrate specificity in descending order is ssDNA, dsDNA, RNA
-
-
?
additional information
?
-
-
substrate specificity, no activity with dinucleoside monophosphates, overview
-
-
?
additional information
?
-
-
mung bean nuclease is an endonuclease specific to single-stranded DNA or RNA
-
-
?
additional information
?
-
-
human DNA samples are used as substrates
-
-
?
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flap DNA + H2O
?
-
-
-
-
?
RNA + H2O
?
-
hydrolysis of nucleic acids
-
-
?
additional information
?
-
DNA + H2O
?
dsDNA to ssDNA preference ratio for Par_DSN-t4 is equal to 10, corresponding ratio for intact Par_DSN is equal to 1000
-
-
?
DNA + H2O
?
protein and DNA are held together by a mix of salt-bridges, water-mediated and direct hydrogen bond interactions between the protein and DNA backbone, almost no DNA bases are directly involved in the contacts
-
-
?
dsDNA + H2O
?
-
primarily responsible for internucleosomal DNA cleavage during the terminal stages of apoptosis, preference for cleaving the internucleosomal linker regions in chromatin
fragments possessing ends with 5-phosphate and 3-hydroxyl groups, exclusively double strand breaks (primarily blunt ends)
-
?
dsDNA + H2O
?
-
-
DNA fragments carrying phosphate groups at 5' ends and hydroxyl group at the 3' ends
-
?
dsDNA + H2O
?
-
physiological function currently unknown
DNA fragments carrying phosphate groups at 5' ends and hydroxyl group at the 3' ends, random DNA cleavage with respect to all possible phosphodiester bonds
-
?
dsDNA + H2O
?
-
hydrolysis of nucleic acids
-
-
?
ssDNA + H2O
?
-
-
-
-
?
ssDNA + H2O
?
-
hydrolysis of nucleic acids, preference for ssDNA
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO2 digests ssDNA over dsDNA, it achieves strong DNase activity under two completely different conditions, but it exerts its nuclease activity towards dsDNA only in acidic buffer as a Ca2+/Zn2+-dependent enzyme
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
the isozyme ENDO1 is defined as bifunctional enzymes due to its ability to digest both DNA and RNA substrates, showing a quite strong DNase activity and weak RNase activity, it digests ssDNA over dsDNA
-
-
?
additional information
?
-
-
single-stranded DNA, single-stranded RNA, double-stranded RNA nor RNA-DNA heteroduplexes are not substrates for the enzyme
-
-
?
additional information
?
-
-
recombinant protein is active on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand
-
-
?
additional information
?
-
-
the enzyme potently degrades both DNA and RNA and is a nuclease with broad specificity, but it shows some sensitivity to the secondary structure of the substrate
-
-
?
additional information
?
-
-
substrate specificity in descending order is ssDNA, dsDNA, RNA
-
-
?
additional information
?
-
-
mung bean nuclease is an endonuclease specific to single-stranded DNA or RNA
-
-
?
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NaCl
the enzyme is capable to hydrolyze DNA in the presence of 0.9% NaCl containing 0.002 M calcium cations
[Co(NH3)6]3+
-
binding to the DNA substrate induces changes in the secondary structure of the enzyme, followed by a decrease of the enzyme activity
Ca2+
activates at pH 8.0
Ca2+
activates at pH 8.0, preferred divalent cation
Ca2+
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+
Mg2+
Azotobacter agilis
-
increases hydrolysis rate of EDTA-dialyzed RNA, no effect on hydrolysis of undialyzed RNA, inhibition at high concentrations
Mg2+
-
no reactivation after EDTA treatment
Mg2+
-
optimum activity in the presence of 2.5 mM
Mg2+
-
optimum concentration 10 mM, inhibitory at higher concentrations
Mg2+
-
coordinates 5 water molecules that participate in the enzyme-controlled reaction
Mg2+
-
molecular dynamic simulations, interaction with enzyme monomer-DNA complex via 6 ligands, which are changing during the reaction simulation, e.g. Asn119 loses its coordination while Glu127 becomes a ligand, overview
Mg2+
in the presence of 0.58 mM Mg2+, the digestive activity of the enzyme is approximately fourfold increased as compared with the activity in the absence of Mg2+ taken as 100%. Further fivefold increase in Mg2+ concentration causes near 1.5fold enhancement in the enzyme activity. Subsequent two- and fourfold increases in Mg2+ concentration have only a minor impact on the enzyme activity within the experimental error range. 6.0-11.6 mM of Mg2+ corresponding to 20-40 Mg2+ per 1 phosphate in RNA is optimal for the hydrolysis of RNA. Optimal Mg2+ amount is linked with the changing secondary structure of RNA substrates within A-helix. Addition of Mg2+ affects both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that is supported by strong increase in the Kcat values and change in the Km values
Mg2+
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+
Mn2+
activates
Mn2+
activates, highly activating divalent cation
Mn2+
-
can replace Mg2+, more effective than Mg2+
Zn2+
dependent on
Zn2+
dependent on, Zn2+-dependent activity of the enzyme can be strongly enhanced by the Ca2+
Zn2+
-
reactivates after EDTA treatment
Zn2+
-
reactivates after EDTA treatment
Zn2+
-
the enzyme is a zinc metalloprotein, three zinc ions interact with the DNA substrate and have different roles in catalysis, e.g. stabilization of the transition state and as reaction nucleophile, binding structures and kinetics, overview
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
-
no reactivation after EDTA treatment by Cd2+, Cu2+
additional information
-
no requirement for added divalent cation
additional information
-
no effect by Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
Azotobacter agilis
-
-
additional information
-
-
additional information
-
-
additional information
G133V mutant, dsDNA, not detectable (inactive protein)
additional information
-
G133V mutant, dsDNA, not detectable (inactive protein)
additional information
G139V mutant, dsDNA, not detectable (inactive protein)
additional information
-
G139V mutant, dsDNA, not detectable (inactive protein)
additional information
H168A mutant, dsDNA, not detectable (inactive protein)
additional information
-
H168A mutant, dsDNA, not detectable (inactive protein)
additional information
H171A mutant, dsDNA, not detectable (inactive protein)
additional information
-
H171A mutant, dsDNA, not detectable (inactive protein)
additional information
H237A mutant, dsDNA, not detectable
additional information
-
H237A mutant, dsDNA, not detectable
additional information
K235A mutant, dsDNA, 110 Kunitz units
additional information
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K235A mutant, dsDNA, 110 Kunitz units
additional information
K235R mutant, dsDNA, 5980 Kunitz units
additional information
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K235R mutant, dsDNA, 5980 Kunitz units
additional information
Par_DSN-t1 lacks DNAse activity
additional information
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Par_DSN-t1 lacks DNAse activity
additional information
Par_DSN-t2 lacks DNase activity
additional information
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Par_DSN-t2 lacks DNase activity
additional information
Par_DSN-t3 lacks DNAse activity
additional information
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Par_DSN-t3 lacks DNAse activity
additional information
Par_DSN-t4 has low specific activity (6 Kunitz-units compared to 6070 Kunitz units for intact Par_DSN), dsDNA
additional information
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Par_DSN-t4 has low specific activity (6 Kunitz-units compared to 6070 Kunitz units for intact Par_DSN), dsDNA
additional information
R121/122A mutant, dsDNA, not detectable (inactive protein)
additional information
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R121/122A mutant, dsDNA, not detectable (inactive protein)
additional information
R121A mutant, dsDNA, 5960 Kunitz units
additional information
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R121A mutant, dsDNA, 5960 Kunitz units
additional information
R121K mutant, dsDNA, 5990 Kunitz units
additional information
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R121K mutant, dsDNA, 5990 Kunitz units
additional information
R122A mutant, dsDNA, 6030 Kunitz units
additional information
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R122A mutant, dsDNA, 6030 Kunitz units
additional information
R122K mutant, dsDNA, 6050 Kunitz units
additional information
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R122K mutant, dsDNA, 6050 Kunitz units
additional information
R184A mutant, dsDNA, 1810 Kunitz units
additional information
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R184A mutant, dsDNA, 1810 Kunitz units
additional information
R184K mutant, dsDNA, 6100 Kunitz units
additional information
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R184K mutant, dsDNA, 6100 Kunitz units
additional information
wild-type, dsDNA, 6070 Kunitz units
additional information
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wild-type, dsDNA, 6070 Kunitz units
additional information
-
-
additional information
-
-
additional information
-
cells transformed with plasmid pDS (carrying 2 copies of Serratia marcescens nuclease) are more effective in stopping cell division than those transformed with plasmid pSS (carrying 1 copy of Serratia marcescens nuclease), OD600 analysis, colony test on plates. Cells cotransformed grow more slowly before induction of Serratia marcescens nuclease, OD600 analysis, florescence, colony test on plates
additional information
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purified enzyme
additional information
-
-
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evolution
the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview
malfunction
-
Deficiencies in FEN1 function or deletion of the fen1 gene have profound biological effects, including the suppression of repair of DNA damage incurred from the action of various genotoxic agents
physiological function
enzyme is able to ablate cells in culture
physiological function
-
FEN1, a key participant in DNA replication and repair, is the major human flap endonuclease that recognizes and cleaves flap DNA structures
physiological function
-
flap endonuclease 1 is a key enzyme in DNA repair and DNA replication. It is a structure-specific nuclease that removes 5'-overhanging flaps and the RNA/DNA primer during maturation of the Okazaki fragment
physiological function
-
Flap endonuclease 1 plays critical roles in both DNA replication and repair. Human FEN1 endonuclease, an enzyme involved in excising single-stranded DNA flaps that arise during Okazaki fragment processing and base excision repair, cleaves model flap substrates assembled into nucleosomes. Orienting the flap substrate toward the histone octamer does not significantly alter the rotational orientation of two different nucleosome positioning sequences on the surface of the histone octamer but does cause minor perturbation of nucleosome structure. In contrast, neither flaps oriented toward nor away from the nucleosome surface are cleaved by the enzyme in nucleosomes containing the high-affinity 601 nucleosome positioning sequence. Sequence-dependent motility of DNA on the nucleosome is a major determinant of FEN1 activity
physiological function
-
Flap endonuclease, FEN1, is essential for DNA replication and repair, and removes RNA and DNA 5' flaps. Structural and functional analyses of human FEN1:DNA complexes show structure-specific, sequence-independent recognition for nicked dsDNA bent 100° with unpaired 3' and 5' flaps. dsDNA binding and bending, the ssDNA gateway, and double-base unpairing flanking the scissile phosphate control precise flap incision by the two-metal-ion active site
physiological function
-
role of FEN1 in replication, recombination, DNA repair and maintenance of telomeres. FEN1 exhibits distinct activity on G4 DNA substrates representative of intermediates in immunoglobulin class switch recombination. hFEN1 but not hEXO1 cleaves substrates bearing telomeric G4 DNA 5'-flaps, consistent with the requirement for FEN1 in telomeric lagging strand replication. FEN1 can create ssDNA at uncapped telomere ends thereby contributing to recombination
physiological function
-
the Dna2 enzyme is at the center of both DNA replication and DNA damage repair, acting in conjunction with flap endonuclease 1 and replication protein A in DNA lagging strand replication and with BLM/Sgs1 and MRN/X in double strand break repair. Dna2 shows helicase and flap endo/exonuclease activities requiring an unblocked 5' single-stranded DNA end to unwind or cleave DNA, but Dna2 in fact can create 5' single-stranded DNA ends. Both endonuclease and flap endo/exonuclease are abolished by the Dna2-K677R mutation, implicating the same active site in catalysis. ATP-dependent flap endo/exonuclease activity is observed only in the presence of Mn2+. The endonuclease is blocked by ATP and is thus experimentally distinguishable from the flap endo/exonuclease function. Mechanism of action of Dna2 in multiprotein complexes, overview
physiological function
any mononucleotide produced by Sma nuc during hydrolysis of DNA or RNA may regulate the enzyme activity affecting the RNase activity without pronounced influence on the activity towards DNA. The type of carbohydrate residue in mononucleotides does not affect the regulation. In contrast, the effects depend on the type of bases in nucleotides
physiological function
involvement of isozyme ENDO1 in endosperm senescence. Plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
physiological function
plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
additional information
specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease
additional information
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specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease
additional information
-
treatment of enriched DNA with the mung bean nuclease, an endonuclease specific to single-stranded DNA or RNA, can dramatically reduce genomic DNA carry over of single-stranded template genomic DNA from microdroplet-PCR and increase on-target efficiency of the resultant library. Nuclease treatment of enrichment products shall be incorporated in the workflow of targeted sequencing using microdroplet-PCR for enrichment
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Brown, P.H.; Ho, T.D.
Biochemical properties and hormonal regulation of barley nuclease
Eur. J. Biochem.
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1987
Hordeum vulgare
brenda
Imagawa, H.; Toryu, H.; Ozawa, T.; Takino, Y.
Purification and characterization of nucleases from tea leaves
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46
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Camellia sinensis
-
brenda
Pietrzak, M.; Cudny, H.; Maluszynski, M.
Purification and properties of two ribonucleases and a nuclease from barley seeds
Biochim. Biophys. Acta
614
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Hordeum vulgare
brenda
Stevens, A.; Hilmoe, R.J.
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Azotobacter agilis
-
brenda
Stevens, A.; Hilmoe, R.J.
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Azotobacter agilis
-
brenda
Sasakuma, M.; Oleson, A.
Partial purification and properties of nuclease I from barley malt
Phytochemistry
18
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1979
Hordeum vulgare
-
brenda
Sawicka, T.
Membrane-bound nucleolytic activity of corn root cells
Phytochemistry
26
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1987
Zea mays
-
brenda
Oleson, A.E.; Janski, A.M.; Clark, E.T.
An extracellular nuclease from suspension cultures of tobacco
Biochim. Biophys. Acta
366
89-100
1974
Nicotiana tabacum
brenda
Varlamov, V.P.; Lopatin, S.A.; Bannikova, G.E.; Andrushina, I.A.; Rogozhin, S.V.
Ligand-exchange chromatography of nucleases
J. Chromatogr.
364
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1986
Serratia marcescens
brenda
Grafi, G.; Meller, E.; Sher, N.; Sela, I.
Characterization of S1/mung-bean-type nuclease activity in plant cell suspensions
Plant Sci.
74
107-114
1991
Solanum lycopersicum, Nicotiana tabacum, Petunia x hybrida, Triticum monococcum
-
brenda
Franke, I.; Meiss, G.; Blecher, D.; Gimadutdinow, O.; Urbanke, C.; Pingoud, A.
Genetic engineering, production and characterization of monomeric variants of the dimeric Serratia marcescens endonuclease
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425
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1998
Serratia marcescens
brenda
Shlyapnikov, S.V.; Lunin, V.V.; Perbandt, M.; Polyakov, K.M.; Lunin, V.Y.; Levdikov, V.M.; Betzel, C.; Mikhailov, A.M.
Atomic structure of the Serratia marcescens endonuclease at 1.1 A resolution and the enzyme reaction mechanism
Acta Crystallogr. Sect. D
56
567-572
2000
Serratia marcescens
brenda
Friedhoff, P.; Gimadutdinow, O.; Rueter, T.; Wende, W.; Urbanke, C.; Thole, H.; Pingoud, A.
A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli
Protein Expr. Purif.
5
37-43
1994
Serratia marcescens
brenda
Kobayashi, H.; Inokuchi, N.; Koyama, T.; Tomita, M.; Irie, M.
Purification and characterization of the 2nd 5'-nucleotide-forming nuclease from Lentinus edodes
Biosci. Biotechnol. Biochem.
59
1169-1171
1995
Lentinula edodes
brenda
Bannikova, G.E.; Blagova, E.V.; Dementiev, A.A.; Morgunova, E.Y.; Mikchailov, A.M.; Shlyapnikov, S.V.; Verlamov, V.P.; Vainstein, B.K.
Two isoforms of Serratia marcescens nuclease. Crystallization and preliminary X-ray investigation of the enzyme
Biochem. Int.
24
813-822
1991
Serratia marcescens
brenda
Filimonova, M.N.; Krause, K.L.; Benedik, M.J.
Kinetic studies of the Serratia marcescens extracellular nuclease isoforms
Biochem. Mol. Biol. Int.
33
1229-1236
1994
Serratia marcescens
brenda
Pedersen, J.; Filimonova, M.; Roepstorff, P.; Biedermann, K.
Characterization of Serratia marcescens nuclease isoforms by plasma desorption mass spectrometry
Biochim. Biophys. Acta
1202
13-21
1993
Serratia marcescens
brenda
Lunin, V.Y.; Blagova, E.V.; Levdikov, V.M.; Lunin, V.V.; Shlypnikov, S.V.; Perbandt, M.; Raishankar, K.S.; Betzel, H.; Mikhailov, A.M.
Extracellular endonuclease of Serratia marcescens. 1. Three-dimensional structure of crystalline protein at 1.7 A resolution
Mol. Biol.
33
180-187
1999
Serratia marcescens
-
brenda
Filimonova, M.; Gubskaya, V.; Nuretdinov, I.; Leshchinskaya, I.
Action of hexaamminecobalt on the activity of Serratia marcescens nuclease
BioMetals
16
447-453
2003
Serratia marcescens
brenda
Koziolkiewicz, M.; Owczarek, A.; Domanski, K.; Nowak, M.; Guga, P.; Stec, W.J.
Stereochemistry of cleavage of internucleotide bonds by Serratia marcescens endonuclease
Bioorg. Med. Chem.
9
2403-2409
2001
Serratia marcescens
brenda
Berkmen, M.; Benedik, M.J.
Multi-copy repression of Serratia marcescens nuclease expression by dinI
Curr. Microbiol.
44
44-48
2002
Serratia marcescens
brenda
Marchetti, S.; Zaina, G.; Chiaba, C.; Pappalardo, C.; Pitotti, A.
Isolation and characterization of an endonuclease synthesized by barley (Hordeum vulgare L.) uninucleate microspores
Planta
213
199-206
2001
Hordeum vulgare
brenda
Shlyapnikov, S.V.; Lunin, V.V.; Blagova, E.V.; Abaturov, L.V.; Perbandt, M.; Betzel, C.; Mikhailov, A.M.
A comparative structure-function analysis and molecular mechanism of action of endonucleases from Serratia marcescens and Physarum polycephalum
Russ. J. Bioorg. Chem.
28
20-27
2002
Serratia marcescens
-
brenda
Pires de Castro, C.S.; Rodrigues SouzaDe, J.; Bloch, C.
Mechanism of DNA cleavage catalyzed by mung bean nuclease
Inorg. Chim. Acta
357
2579-2592
2004
Vigna radiata
-
brenda
Yupsanis, T.; Symeonidis, L.; Kalemi, T.; Moustaka, H.; Yupsani, A.
Purification, properties and specificity of an endonuclease from Agropyron elongatum seedlings
Plant Physiol. Biochem.
42
795-802
2004
Thinopyrum elongatum
brenda
Chen, C.; Beck, B.W.; Krause, K.; Pettitt, B.M.
Solvent participation in Serratia marcescens endonuclease complexes
Proteins
62
982-995
2006
Serratia marcescens
brenda
Hanus, J.; Kalinowska-Herok, M.; Widlak, P.
The major apoptotic endonuclease DFF40/CAD is a deoxyribose-specific and double-strand-specific enzyme
Apoptosis
13
377-382
2008
Homo sapiens
brenda
Laquel-Robert, P.; Sellem, C.H.; Sainsard-Chanet, A.; Castroviejo, M.
Identification and biochemical analysis of a mitochondrial endonuclease of Podospora anserina related to curved-DNA binding proteins
Biochim. Biophys. Acta
1770
527-542
2007
Podospora anserina
brenda
Mandal, P.; Chakraborty, P.; Sau, S.; Mandal, N.C.
Purification and characterization of a deoxyriboendonuclease from Mycobacterium smegmatis
J. Biochem. Mol. Biol.
39
140-144
2006
Mycolicibacterium smegmatis
brenda
Li, Q.; Wu, Y.J.
A fluorescent, genetically engineered microorganism that degrades organophosphates and commits suicide when required
Appl. Microbiol. Biotechnol.
82
749-756
2009
Serratia marcescens
brenda
Anisimova, V.E.; Shcheglov, A.S.; Bogdanova, E.A.; Rebrikov, D.V.; Nekrasov, A.N.; Barsova, E.V.; Shagin, D.A.; Lukyanov, S.A.
Is crab duplex-specific nuclease a member of the Serratia family of non-specific nucleases?
Gene
418
41-48
2008
Paralithodes camtschaticus (Q8I9M9), Paralithodes camtschaticus
brenda
Chen, C.; Krause, K.; Pettitt, B.M.
Advantage of being a dimer for Serratia marcescens endonuclease
J. Phys. Chem. B
113
511-521
2009
Serratia marcescens (P13717), Serratia marcescens
brenda
Caballero, I.; Piedrahita, J.A.
Evaluation of the Serratia marcescens nuclease (NucA) as a transgenic cell ablation system in porcine
Anim. Biotechnol.
20
177-185
2009
Serratia marcescens (P13717), Serratia marcescens
brenda
Filimonova, M.; Gubskaya, V.; Nuretdinov, I.
Some features of hydrolysis of the hybrid B-Z-form dna by Serratia marcescens nuclease
OnLine J. Biol. Sci.
14
179-185
2014
Serratia marcescens
-
brenda
Lesniewicz, K.; Karlowski, W.M.; Pienkowska, J.R.; Krzywkowski, P.; Poreba, E.
The plant S1-like nuclease family has evolved a highly diverse range of catalytic capabilities
Plant Cell Physiol.
54
1064-1078
2013
Arabidopsis thaliana (F4JJL0), Arabidopsis thaliana (F4JJL3), Arabidopsis thaliana (Q9C9G4), Arabidopsis thaliana (Q9SXA6)
brenda
Yu, Z.; Cao, K.; Tischler, T.; Stolle, C.A.; Santani, A.B.
Mung bean nuclease treatment increases capture specificity of microdroplet-PCR based targeted DNA enrichment
PLoS ONE
9
e103491
2014
Vigna radiata
brenda
Romanova, J.; Filimonova, M.
The effects of addition of mononucleotides on Sma nuc endonuclease activity
ScientificWorldJournal
2012
454176
2012
Serratia marcescens (P13717), Serratia marcescens
brenda
Vafina, G.; Bulatov, E.; Zaynutdinova, E.; Filimonova, M.
A one-step protocol for chromatographic purification of non-recombinant exogenous bacterial enzyme nuclease of Serratia marcescens
BioNanoSci.
6
335-337
2016
Serratia marcescens (P13717)
-
brenda
Romanova, J.; Gubskaya, V.; Nuretdinov, I.; Zainutdinova, E.; Filimonova, M.
Analysis of the mechanism of Mg2+ action on the RNase activity of Serratia marcescens endonuclease
BioNanoSci.
7
276-283
2017
Serratia marcescens (P13717)
-
brenda
Vafina, G.; Zainutdinova, E.; Bulatov, E.; Filimonova, M.N.
Endonuclease from Gram-negative bacteria Serratia marcescens is as effective as pulmozyme in the hydrolysis of DNA in sputum
Front. Pharmacol.
9
114
2018
Serratia marcescens (P13717)
brenda
Khamidullina, R.; Fazleeva, I.; Trushin, M.; Gimadutdinov, O.
Reactivation of Serratia marcescens mutant endonuclease by hydroxilamine
J. Pharm. Sci. Res.
10
2341-2345
2018
Serratia marcescens (P13717)
-
brenda