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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; 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; 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; 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
-
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
-
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, 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
-
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
-
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
-
FEN1, a key participant in DNA replication and repair, is the major human flap endonuclease that recognizes and cleaves flap DNA structures
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; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death; plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
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
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
additional information
specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease
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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
-
-
?
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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
flap DNA + H2O
?
-
-
-
-
?
RNA + H2O
?
-
hydrolysis of nucleic acids
-
-
?
additional information
?
-
DNA + H2O

?
Q8I9M9
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
?
P13717
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

?
-
F4JJL0
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
?
-
F4JJL3
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
?
-
Q9C9G4
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
?
-
Q9SXA6
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
?
-
F4JJL0
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
-
additional information
?
-
F4JJL3
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
-
additional information
?
-
Q9C9G4
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
-
additional information
?
-
Q9SXA6
isozyme ENDO4 shows quite strong DNase activity, but relatively weak RNase activity
-
-
-
additional information
?
-
F4JJL0
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
-
additional information
?
-
F4JJL3
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
-
additional information
?
-
Q9C9G4
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
-
additional information
?
-
Q9SXA6
no activity by isozyme ENDO5 on ssDNA or dsDNA
-
-
-
additional information
?
-
F4JJL0
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
?
-
F4JJL3
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
?
-
Q9C9G4
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
?
-
Q9SXA6
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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Ca2+
activates at pH 8.0; activates at pH 8.0; activates at pH 8.0, preferred divalent cation
[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
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
Mn2+

activates; activates; activates, highly activating divalent cation
Mn2+
-
can replace Mg2+, more effective than Mg2+
Zn2+

dependent on; 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+; metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+; 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+; metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+; 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+; metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+; 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+; metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+; the enzyme activity is not affected by Mg2+ or Fe2+; 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+
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-
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-
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Vigna radiata
-
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-
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