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Information on EC 3.1.22.1 - deoxyribonuclease II
for references in articles please use BRENDA:EC3.1.22.1
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.22 Endodeoxyribonucleases producing 3'-phosphomonoesters
3.1.22.1 deoxyribonuclease II
IUBMB Comments
Preference for double-stranded DNA.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.1.22.1
- chromatin
- endonuclease
- nuclei
- spleen
- nucleases
- nucleosome
- cathepsins
-
micrococcal
-
engulf
-
caspase-independent
- spiralis
- medicine
- trichinella
-
caspase-activated
- dnaase
-
ii-like
-
internucleosomal
-
undigested
-
endonucleolytic
-
nonhistone
-
corpses
-
cation-independent
- analysis
Reaction Schemes
showendonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
Synonyms
dnase ii, nuc-1, acid dnase, deoxyribonuclease ii, l-dnase ii, acid deoxyribonuclease, lei/l-dnase ii, dnase iialpha, dnase iibeta, dnase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid deoxyribonuclease
acid DNase
deoxyribonuclease II
deoxyribonuclease IIalpha
deoxyribonucleate 3'-nucleotidohydrolase
-
-
-
-
DNase 2
DNase 2a
DNase II
DNase II homolog
DNase IIalpha
DNase IIbeta
DNase2
EC 3.1.4.6
-
-
formerly
-
L-DNase II
LEI
LEI-derived DNase II
LEI/L-DNase II
leukocyte elastase inhibitor-derived DNase II
lysosomal DNase II
-
-
-
-
Nuc-1
pancreatic DNase II
-
-
-
-
R31240_2
-
-
-
-
acid deoxyribonuclease
-
-
-
-
acid DNase
-
-
-
-
DNase II
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
preference for double-stranded DNA. Similar enzymes: crab testis DNase, snail DNase, salmon testis DNase, liver acid-DNase, human acid-DNases of gastric mucosa and cervix
-
-
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
deoxyribonuclease IIbeta is a protein with considerably homology to DNase II
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
deoxyribonuclease IIbeta is a protein with considerably homology to DNase II
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
the signal-peptide leader sequence is required for correct glycosylation and the N-glycosylation is important for formation of the active enzyme
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
The protein is a single, contiguous polypeptide chain, featuring N-linked sugar moieties and at least one disulfide bridge
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
The pathway for DNA degradation involves three distinct steps. The second step is mediated by the NUC-1.
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-64-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bis(p-nitrophenyl) phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate:
-
Substrates: slow hydrolysis at optimal pH from 5.6 to 5.9
Products: -
Products: -
?
calf thymus DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
Substrates: -
Products: -
Products: -
?
deoxyribonucleoside 5'-phosphates p-nitrophenyl esters + H2O
p-nitrophenol + deoxyribonucleoside 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
dsDNA + H2O
oligonucleotides + ?
-
Substrates: velocity of DNA degradtion is four times higher four dsDNA than for ssDNA
Products: -
Products: -
?
duplex-oligonucleotide + H2O
?
-
Substrates: 20- and 16mers with specific sequences and structures like hairpin and duplex DNA, can cut bonds in a loop at nearly the same rate as in duplex DNA, doesn't require phosphate exposure or a double-stranded track
Products: -
Products: -
?
d[ApAp(S)ApA] + H2O
d[Ap(S)ApA] + 3'-dAMP
-
Substrates: digestion of Rp- and Sp-isomers
Products: after 2 h incubation, prolonged incubation leads to d[Ap(S)Ap]-Rp-isomer, dA and d[Ap(S)Ap]-Sp-isomer. Does not hydrolyse phosphorothioate internucleotidic linkage of either configuration
Products: after 2 h incubation, prolonged incubation leads to d[Ap(S)Ap]-Rp-isomer, dA and d[Ap(S)Ap]-Sp-isomer. Does not hydrolyse phosphorothioate internucleotidic linkage of either configuration
?
d[ApApApA] + H2O
d[ApApA] + 3'-dAMP
-
Substrates: -
Products: after 60 min of incubation, prolonged incubation leads to 3'-dAMP and dA end products in a 3 : 1 ratio
Products: after 60 min of incubation, prolonged incubation leads to 3'-dAMP and dA end products in a 3 : 1 ratio
?
linearized plasmid DNA + H2O
oligonucleotides + ?
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
Substrates: -
Products: -
Products: -
?
ssDNA + H2O
oligonucleotides + ?
-
Substrates: velocity of DNA degradtion is four times higher four dsDNA than for ssDNA
Products: -
Products: -
?
supercoiled plasmid DNA + H2O
linearized plasmid DNA + ?
-
Substrates: -
Products: -
Products: -
?
chromatin + H2O
oligonucleotides + ?
-
Substrates: chicken erythrocyte and yeast nuclei
Products: 100 bp cleavage-pattern in the condensed form and 200 bp cleavage-pattern in the extended form
Products: 100 bp cleavage-pattern in the condensed form and 200 bp cleavage-pattern in the extended form
?
chromatin + H2O
oligonucleotides + ?
-
Substrates: SDS and proteinase K treated substrate
Products: single-stranded regions in oligonucleotides are formed, not detected in untreated chromatin
Products: single-stranded regions in oligonucleotides are formed, not detected in untreated chromatin
?
chromatin + H2O
oligonucleotides + ?
-
Substrates: mouse liver chromatin
Products: 100 bp cleavage-pattern of H1-reconstituted chromatin, 200 bp cleavage-pattern at the internucleosomal cleavage site of H1-free chromatin
Products: 100 bp cleavage-pattern of H1-reconstituted chromatin, 200 bp cleavage-pattern at the internucleosomal cleavage site of H1-free chromatin
?
DNA + H2O
3'-phosphooligonucleotide
-
Substrates: degradation of the DNA of apoptotic cells
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotide
-
Substrates: using TdT-mediated dUTP-nicked-end labelling, TUNEL, is followed DNA fragmentation that occurs in vivo during programmed cell death, Nuc-1 functions in the elimination of TUNEL-reactive DNA ends to a TUNEL nonreactive state
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: fragments longer than 10 nucleotides
Products: fragments longer than 10 nucleotides
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: velocity of DNA degradation is four times higher for dsDNA than for ssDNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: the 3'-phosphate terminal position contains 78% deoxyadenosine, less than 1% deoxycytidine, 6% deoxyguanosine, 16% thymidine, the 5'-hydroxy position contains 38% thymidine, 24% deoxyguanosine, 21% deoxyadenosine and 17% deoxycytidine
Products: the 3'-phosphate terminal position contains 78% deoxyadenosine, less than 1% deoxycytidine, 6% deoxyguanosine, 16% thymidine, the 5'-hydroxy position contains 38% thymidine, 24% deoxyguanosine, 21% deoxyadenosine and 17% deoxycytidine
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: double-strand and single-strand DNA, but the enzyme acts preferentially on double-strand DNA
Products: this endonuclease makes double-strand breaks in the DNA substrate
Products: this endonuclease makes double-strand breaks in the DNA substrate
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: double-strand and single-strand DNA, but the enzyme acts preferentially on double-strand DNA
Products: this endonuclease makes double-strand breaks in the DNA substrate
Products: this endonuclease makes double-strand breaks in the DNA substrate
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: native DNA degraded 3-4 times faster than denatured DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: native DNA degraded 5-15 times faster than denatured DNA
Products: average chain length 11 to 15mers
Products: average chain length 11 to 15mers
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: preference for double-stranded DNA, terminal four 3'-nucleotides resistant to cleavage
Products: prominent fragments longer than eight nucleotides
Products: prominent fragments longer than eight nucleotides
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: double-strand DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: ethanol stress on ARPE-19 cells can induce a pathway which is a form of programmed cell death with characteristics of both apoptosis and necrosis, possibly by triggering conversion of leukocyte elastase inhibitor LEI to L-DNase II
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: DNase II exhibits a catalytic domain common to phospholipase D superfamily
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: the enzyme in macrophages appears to be responsible for destroying the nuclear DNA expelled from erythroid precursor cells
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: it is proposed that DNase II together with the Chk2, p53, and p21 pathway forms a genetic barrier blocking the replication of potentially harmful DNA introduced via apoptotic bodies, thereby preventing transformation and malignant development
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: limited digest yields fragments larger than tetranucleotides, exhaustive digestion yields mono-, di- and trinucleotides, where at the 3'-terminus G predominates
Products: limited digest yields fragments larger than tetranucleotides, exhaustive digestion yields mono-, di- and trinucleotides, where at the 3'-terminus G predominates
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: The LEI/L-DNase II pathway is activated in light-induced retinal degeneration
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: The LEI/L-DNase II pathway is activated in light-induced retinal degeneration
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: native DNA degraded 2.5 times faster than heat-denatured DNA
Products: oligonucleotides with an average chain length of about seven
Products: oligonucleotides with an average chain length of about seven
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA, micrococcus luteus DNA and poly[d(A-T)d(A-T)]
Products: formation of dinucleotides to 8 nucleotide chain length
Products: formation of dinucleotides to 8 nucleotide chain length
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: average chain length of oligonucleotides 10-12
Products: average chain length of oligonucleotides 10-12
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: calf thymus DNA
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: double-strand and single-strand scission
Products: formation of oligonucleotides of an average chain length from 14 to 100 in the middle activity phase, purine nucleotides form about 75% of the 3'-terminals, formation of oligonucleotides of an average chain length from 6 to 14 in the terminal activity phase
Products: formation of oligonucleotides of an average chain length from 14 to 100 in the middle activity phase, purine nucleotides form about 75% of the 3'-terminals, formation of oligonucleotides of an average chain length from 6 to 14 in the terminal activity phase
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: independence to double-strand and single-strand break mechanism
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
?
Substrates: method of ToLFP (topoisomerase ligation fluorescence probes) is used for directly visualizing DNA fragments generated by DNase II in Caenorhabditis elegans embryos. The ratio of non-autonomous and autonomous modes of DNase II is about 3-7. ToLFP method can be used to differentiate the locations of blastomeres where DNase II acts autonomously or non-autonomously in degrading apoptotic DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme could be one of the factors in the late block to polyspermy in the cytoplasm of avian eggs, the enzyme activity might also be responsible for poor efficiency in obtaining transgenic birds by microinjection of exogenous DNA into the fertilised chick ovum
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme acts on both dsDNA and ssDNA, dsDNA is preferred, the enzyme causes double-strand breaks in DNA substrates and generates 3-phosphate and 5-OH termini
Products: -
Products: -
?
DNA + H2O
?
Substrates: the enzyme possesses a typical divalent iron-independent DNA catalytic activity
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: cleaves DNA in co-ordination with other nucleases to produce internucleosomal degradation
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: salmon sperm DNA
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: involved in nuclear DNA metabolism
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: SV40 minichromosome and naked SV40 DNA, preferentially cleaves the SV40 minichromosome at a distinct 72 bp modulator element, near the replication origin, near the T-ag binding site II and near the BamHI site, where termination of replication and late transcription occurs
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: nearest cuts are staggered by 4 nucleotides, 3'end extending, staggered cuts are symmetrically located about a dyad axis in the nucleosome core
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: prefers to cut purine-rich steps in duplex-DNA, will also attack heat-denatured and single-stranded substrates
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: involvement in recombination, replication and degradation of DNA
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: transformation from leukocyte elastase inhibitor to L-DNase II acts as a switch of protease and nuclease pathways
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: involved in DNA replication
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: convertes genomic DNA into fragments of less than 2 kbp
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: the 6.5 kbp EcoRI fragment containing the beta-globin gene region shows a 6fold increased sensitivity to DNase II
Products: -
Products: -
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
Substrates: IgGs from rabbit immunized with DNase II effectively hydrolyze DNA
Products: -
Products: -
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
Substrates: no sequence specificity
Products: primary reaction product, "nicking" mechanism
Products: primary reaction product, "nicking" mechanism
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
Substrates: plasmid pBR322
Products: primary reaction product, "nicking" mechanism
Products: primary reaction product, "nicking" mechanism
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
Substrates: introduces a strong excess of single-strand nicks relative to double-strand breaks, more than 50% converted to nicked circular DNA
Products: -
Products: -
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
Substrates: plasmid pBR322
Products: primary reaction product, "nicking" mechanism
Products: primary reaction product, "nicking" mechanism
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
-
Substrates: The enzyme plays a role in the degradation of exogenous DNA encountered by phagocytosis and is important for DNA fragmentation and degradation during cell death
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
-
Substrates: The enzyme plays a role in the degradation of exogenous DNA encountered by phagocytosis and is important for DNA fragmentation and degradation during cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is essential to maintaining proper immune function in Drosophila
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is required for degrading DNA of dying cells and this function is necessary for the proper removal of apoptotic nuclei during fetal development
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme precursor Leukocyte Elastase Inhibitor is cleaved by elastase at its reactive center loop. Cleavage abolishes the antiprotease activity and leads to a conformational modification that exposes an endonuclease active site and a nuclear localization signal. Both endonuclease activity and nuclear translocation are needed to induce cell death
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
3'-phosphooligonucleotide
-
Substrates: using TdT-mediated dUTP-nicked-end labelling, TUNEL, is followed DNA fragmentation that occurs in vivo during programmed cell death, Nuc-1 functions in the elimination of TUNEL-reactive DNA ends to a TUNEL nonreactive state
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme could be one of the factors in the late block to polyspermy in the cytoplasm of avian eggs, the enzyme activity might also be responsible for poor efficiency in obtaining transgenic birds by microinjection of exogenous DNA into the fertilised chick ovum
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: ethanol stress on ARPE-19 cells can induce a pathway which is a form of programmed cell death with characteristics of both apoptosis and necrosis, possibly by triggering conversion of leukocyte elastase inhibitor LEI to L-DNase II
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: the enzyme in macrophages appears to be responsible for destroying the nuclear DNA expelled from erythroid precursor cells
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: it is proposed that DNase II together with the Chk2, p53, and p21 pathway forms a genetic barrier blocking the replication of potentially harmful DNA introduced via apoptotic bodies, thereby preventing transformation and malignant development
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: The LEI/L-DNase II pathway is activated in light-induced retinal degeneration
Products: -
Products: -
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
Substrates: The LEI/L-DNase II pathway is activated in light-induced retinal degeneration
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: cleaves DNA in co-ordination with other nucleases to produce internucleosomal degradation
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: involved in nuclear DNA metabolism
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: prefers to cut purine-rich steps in duplex-DNA, will also attack heat-denatured and single-stranded substrates
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: induces DNA digestion during apoptosis
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: involvement in recombination, replication and degradation of DNA
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: directed into the secretory pathway
Products: -
Products: -
?
DNA + H2O
oligonucleotides + ?
-
Substrates: transformation from leukocyte elastase inhibitor to L-DNase II acts as a switch of protease and nuclease pathways
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: involved in DNA replication
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: convertes genomic DNA into fragments of less than 2 kbp
Products: -
Products: -
?
nuclei + H2O
oligonucleotides + ?
-
Substrates: the 6.5 kbp EcoRI fragment containing the beta-globin gene region shows a 6fold increased sensitivity to DNase II
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
Products: -
Products: -
?
additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
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additional information
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Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
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additional information
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-
-
Substrates: The enzyme plays a role in the degradation of exogenous DNA encountered by phagocytosis and is important for DNA fragmentation and degradation during cell death
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additional information
?
-
Substrates: The enzyme is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability.
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additional information
?
-
-
Substrates: The enzyme plays a role in the degradation of exogenous DNA encountered by phagocytosis and is important for DNA fragmentation and degradation during cell death
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additional information
?
-
-
Substrates: enzyme is essential to maintaining proper immune function in Drosophila
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additional information
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-
-
Substrates: the enzyme is required for degrading DNA of dying cells and this function is necessary for the proper removal of apoptotic nuclei during fetal development
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additional information
?
-
-
Substrates: enzyme precursor Leukocyte Elastase Inhibitor is cleaved by elastase at its reactive center loop. Cleavage abolishes the antiprotease activity and leads to a conformational modification that exposes an endonuclease active site and a nuclear localization signal. Both endonuclease activity and nuclear translocation are needed to induce cell death
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CuCl2
-
high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo
CuSO4
-
high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo
Mg2+
additional information
Mg2+
-
in the presence of external 5 mM Mg2+ ions, the IgGs are 17 to 25fold more active than the same IgG preparations containing intrinsic metal ions before their dialysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
dialysis of IgGs from rabbits immunized with DNase II against a buffer containing EDTA or addition of EDTA to the reaction mixture leads to a complete disappearance of DNase activity
growth hormone
-
in mice fed a 20% protein diet, growth hormone treatment decreases elevated activites of DNase II and RNase
-
human growth hormone
-
treatment of post-weaning mice results in 63% inhibition in gastrocnemius muscle
-
RNAi
-
expression of a DNase IIRNAi construct in flies results in a significant decrease in total hemocyte numbers
-
bovine serum albumin
-
90% inhibition at 0.015 mg/ml, addition of inhibitor changes pH-activity curve, optimal pH shifted to the alkaline side, DNA substrate compete with inhibitor and reverses inhibitor action
-
bovine serum albumin
-
90% inhibition at 0.015 mg/ml, addition of inhibitor changes pH-activity curve, optimal pH shifted to the alkaline side, DNA substrate compete with inhibitor and reverses inhibitor action
-
Cu2+
inhibited by copper ions and to a lesser extent manganese ions, but not inhibited by calcium, magnesium or zinc ions
Mg2+
-
addition of Mg2+ ions to the dialyzed preparations of IgGs leads to a reduction of the IgG DNase activity
Mg2+
-
slightly inhibitory at 10 mM and pH 4.5, inhibitory effects depending on enzyme purity
Mn2+
inhibited by copper ions and to a lesser extent manganese ions, but not inhibited by calcium, magnesium or zinc ions
tunicamycin
inhibits the N-linked glycosylation and virtually abolishes the enzyme activity
additional information
-
caspases inhibitors have no effect on acid endonucleases, and no effect on apoptosis
-
additional information
-
despite having putative poly(ADP-ribose)-acceptor sites, LEI/L-DNase II is neither significantly poly(ADP-ribosyl)ated nor inhibited by PARP-1 during caspase-independent apoptosis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AP-24
-
apoptotic protease of 24 kDa, is activated during apoptosis and is able to activate L-DNase II
-
bromobenzene
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
chlorobenzene
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
gasoline
-
increases enzyme activity in the digestive gland and in hemocytes
-
intracellular elastase
-
a neutral protease, can transform LEI into L-DNase II
-
iodobenzene
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
phenol
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
additional information
-
catalytic center of the human DNase II involves His113 and His295, as well as Lys115 and Lys295. The histidine at position 295 of the human sequence is critical for DNase II activity. The human DNase II is active as a contiguous polypeptide chain and has four potential glycosylated sites
-
additional information
-
activation is favoured at pH 4 but is increased by a tissue extract
-
additional information
-
His115, His132, and His297 play crucial roles in the function of porcine DNase II. His115 and His297 residues in porcine DNase II act as a general acid-base pair during catalysis, whereas residue His132 appears to be involved in proper protein folding. The porcine DNase II is processed into two non-covalently linked peptides of 35 and 10 kDa and has six potential glycosylated sites
-
additional information
-
proteolytic processing of recombinant DNase II occurs in the lysosome, which is not involved in the activation of DNase II. The processed enzyme is relatively stable after it is formed
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000005
supercoiled plasmid DNA
-
pH 2.6, 3.0% IgG relative content, 18.6% relative DNase activity
-
0.0000008
supercoiled plasmid DNA
-
3 M NaCl, 2.0% IgG relative content, 22.3% relative DNase activity
-
0.0000135
supercoiled plasmid DNA
-
0.51 M NaCl, 28.3% IgG relative content, 27.8% relative DNase activity
-
0.0000158
supercoiled plasmid DNA
-
non-fractioned elution, 100% IgG relative content, 100% relative DNase activity
-
0.0000183
supercoiled plasmid DNA
-
0.1 M NaCl, 11.1% IgG relative content, 25.7% relative DNase activity
-
0.0000608
supercoiled plasmid DNA
-
0.0 M NaCl, 55.6 IgG relative content, 5.5% relative DNase activity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000183
supercoiled plasmid DNA
-
pH 2.6, 3.0% IgG relative content, 18.6% relative DNase activity
-
0.000000367
supercoiled plasmid DNA
-
0.1 M NaCl, 11.1% IgG relative content, 25.7% relative DNase activity
-
0.00000065
supercoiled plasmid DNA
-
3 M NaCl, 2.0% IgG relative content, 22.3% relative DNase activity
-
0.000000883
supercoiled plasmid DNA
-
0.0 M NaCl, 55.6 IgG relative content, 5.5% relative DNase activity
-
0.00000145
supercoiled plasmid DNA
-
0.51 M NaCl, 28.3% IgG relative content, 27.8% relative DNase activity
-
0.00000167
supercoiled plasmid DNA
-
non-fractioned elution, 100% IgG relative content, 100% relative DNase activity
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
1 unit defined as absorbance of digestion products at 260 nm/min/mg
additional information
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotynilated forward and fluorescein-labeled reverse primers
additional information
-
1 unit defined as absorbance of digestion products at 260 nm/min/mg
additional information
Ovis aries aries
-
1 unit defined as absorbance of digestion products at 260 nm/min/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
4.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
-
pH 4.0: about 30% of maximal activity, pH 7.5: about 45% of maximal activity
5 - 6.8
-
pH 5.0: about 40% of maximal activity, pH 6.8: about 15% of maximal activity
7 - 8
pH 7.0: about 65% of maximal activity, pH 8.0: about 40% of maximnal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
-
40°C: about 70% of maximal activity, 70°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme activity is reported in all of the human cell lines examined
SwissProt
brenda
extensive database search to find sequence homology, which may allow a better analysis of critical residues
SwissProt
brenda
polymorphisms associated with risk of renal disorder among systemic lupus erythematosus patients
-
-
brenda
fed a diet containing 20% or 12% protein. Acid RNase and DNASE II activity increase according to the dietary protein content. In mice fed a 20% protein diet, growth hormone treatment decreases both activites
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is mainly located at the cuticle and stichosome of the nematode
brenda
-
isoform DNase II and acid RNase directly participate in muscle DNA and RNA degradation. Treatment with recombinant human growth hormone leads to 63% inhibition of DNase and 48% inhibition of RNase activity
brenda
higher enzyme activity in the gills observed in the autumn/winter period can be associated with feeding and cellular adaptation to low seawater temperatures
brenda
-
specific activity of acid DNase of unexposed, control mussels is higher in the hemocytes than in the digestive gland
brenda
the enzyme is mainly located at the cuticle and stichosome of the nematode
brenda
the enzyme is mainly expressed on the teguments of female adult parasites
brenda
additional information
-
in Pnuc-1(4xNLS)::GFP transgenic larvae and adults, and in Pcrn-7(4xNLS)::GFP larvae
brenda
-
in Pnuc-1(4xNLS)::GFP transgenic larvae and adults, and in Pcrn-7(4xNLS)::GFP larvae
-
brenda
-
specific activity of acid DNase of unexposed, control mussels is higher in the hemocytes than in the digestive gland
brenda
in the digestive gland, high DNase activity is observed in relation to food availability and spawning
brenda
-
isoform DNase IIbeta accounts for about 50% of the acid nuclease activity in cortical fiber cell. Activity is strongest in early differentiation and associated with the lysosomal fraction. Later, an increasing portion of enzyme is found in cytosol
brenda
-
in Pnuc-1(4xNLS)::GFP transgenic embryos, in the head region of comma and 1.5fold stage embryos and 3fold or 4fold stage embryos, and in Pnuc-1(4xNLS)::GFP transgenic larvae and adults
brenda
-
in Pnuc-1(4xNLS)::GFP transgenic embryos, in the head region of comma and 1.5fold stage embryos and 3fold or 4fold stage embryos, and in Pnuc-1(4xNLS)::GFP transgenic larvae and adults
-
brenda
-
in posterior intestinal cells of Pnuc-1(4xNLS)::GFP transgenic larvae and adults. In anterior intestinal cells of 3fold or 4fold stage Pnuc-1(4xNLS)::GFP transgenic embryos and in Pnuc-1(4xNLS)::GFP transgenic larvae and adults. In intestinal cells of Pcrn-6(4xNLS)::GFP transgenic embryos, larvae or adults
brenda
-
in posterior intestinal cells of Pnuc-1(4xNLS)::GFP transgenic larvae and adults. In anterior intestinal cells of 3fold or 4fold stage Pnuc-1(4xNLS)::GFP transgenic embryos and in Pnuc-1(4xNLS)::GFP transgenic larvae and adults. In intestinal cells of Pcrn-6(4xNLS)::GFP transgenic embryos, larvae or adults
-
brenda
-
isoforms DN2-1 and DN2-2 are mainly expressed in intestine
brenda
-
the enzyme gene is expressed in the fetal liver of the wild-type and DNase II+/- embryos, but not in the DNase II-/- liver
brenda
DNase II is mainly expressed in the salivary gland
brenda
additional information
-
is present in intestinal precursor cells of Pcrn-6(4xNLS)::GFP transgenic embryos. Is absent from Pcrn-7(4xNLS)::GFP transgenic embryos. Except for a few anterior intestinal cells in 4fold stage embryos, the embryonic expression patterns of the three DNase II genes do not seem to overlap
brenda
additional information
-
is present in intestinal precursor cells of Pcrn-6(4xNLS)::GFP transgenic embryos. Is absent from Pcrn-7(4xNLS)::GFP transgenic embryos. Except for a few anterior intestinal cells in 4fold stage embryos, the embryonic expression patterns of the three DNase II genes do not seem to overlap
-
brenda
additional information
-
DNase2 isoforms are mainly expressed in immune organs
brenda
additional information
-
no enzymic activity detected in blood plasma samples
brenda
additional information
-
in vitro physical interaction between LEI/L-DNase II and PARP-1. positive effect of LEI (and, to a lesser extent, of L-DNase II) on PARP-1 activity
brenda
additional information
-
muscle larvae stage, newborn stage and adult stage
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during early differentiation, localization to lysosome. Later, an increasing portion of enzyme is found in cytosol
brenda
-
fraction of procaspase-8 and LEI colocalise in the mitochondria. After etoposide treatment, cathepsin D is released from lysosomes and part of it colocalises with caspase-8 and LEI
brenda
additional information
-
putative leucine-rich nuclear export signal on LEI/L-DNase II sequence, a mandatory condition for binding exportin molecules. The exportin Crm1 interacts with LEI/L-DNase II
-
brenda
-
LEI is concentrated around the nucleus. LEI/L-DNase II nuclear export is leptomycin B sensitive. The export is mediated by Crm1 receptor
brenda
-
secretion into the culture medium from COS-7 cell culture
-
brenda
-
DNase IIbeta resides in the lysosomes of cortical fiber cells, close to the organelle-free zone
brenda
-
and heterophagolysosome of macrophages and mononuclear cells, two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa
brenda
the enzyme is localized in the lysosomal vacuolar system of both gill and digestive gland tissues
brenda
-
post-translational processing of the DNase II to produce the alpha1, beta and alpha2 subunits occurs in the lysosome
brenda
-
L-DNase II is translocated to the nucleus to meet its new substrate, DNA
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
presence of DNase II is found in 90 bacteria species belonging to 54 different genera and seven phyla. The majority of the significant hits (85%) come from Bacteroidetes and Proteobacteria phyla. Bacterial DNase II-like proteins possess a signature catalytic motif of eukaryotic DNase II. Both N- and C-terminus specific HKD motifs are well conserved in bacterial DNase II-like proteins, and histidine residues in both motifs are conserved in all bacterial DNase II-like sequences. Bacterial DNase II-like proteins are divided into two distinct clades
malfunction
physiological function
malfunction
-
loss of all three DNase II genes (nuc-1, crn-6 or crn-7) does not affect the activation or progression of cell death. Removal or disruption of NUC-1 secretion signal eliminates NUC-1's ability to mediate DNA degradation across its expression border
malfunction
loss of NUC-1 leads to up-regulation of antimicrobial genes
malfunction
loss of CRN-7 leads to up-regulation of antimicrobial genes
malfunction
-
loss of all three DNase II genes (nuc-1, crn-6 or crn-7) does not affect the activation or progression of cell death. Removal or disruption of NUC-1 secretion signal eliminates NUC-1's ability to mediate DNA degradation across its expression border
-
physiological function
DNase II gene shows relatively low genetic diversity with regard to the non-synonymous single nucleotide polymorphisms, suggesting that the enzyme has been well conserved
physiological function
-
three DNase II genes: nuc-1 plays a major role, crn-6 plays an auxiliary role, and crn-7 plays a negligible role in resolving 3' OH DNA breaks generated in apoptotic cells. NUC-1 constitutes the major DNase II activity and CRN-6 provides the minor DNase II activity in the organism. Nuc-1, crn-6 and crn-7 affect apoptotic DNA degradation but do not affect the activation or the kinetics of apoptosis. The crn-6 gene but not crn-7 can partially substitute for nuc-1 in mediating apoptotic DNA degradation and both fail to replace nuc-1 in degrading bacterial DNA in intestine. Despite of their restricted and largely non-overlapping expression patterns, both CRN-6 and NUC-1 can mediate apoptotic DNA degradation in many cells, suggesting that they are likely secreted nucleases that are retaken up by other cells to exert DNA degradation functions. NUC-1, but not CRN-6 or CRN-7, mediates degradation of chromosome DNA in ventral cord apoptotic cells and bacterial DNA in intestine. Neither CRN-6 nor CRN-7 can substitute for NUC-1 in digesting bacterial DNA in intestine. Nuc-1 can still promote apoptotic DNA degradation in both embryos and larvae when its expression is restricted to intestine cells. NUC-1 expressed in the head can mediate apoptotic DNA degradation in the posterior ventral cord
physiological function
-
fundamental role in the degradation of DNA from both apoptotic cells, and nuclei extruded from red blood cells during erythropoiesis; mice lacking DNase II die late in embryogenesis
physiological function
-
upon cleavage by its cognate protease, leukocyte elastase inhibitor LEI is transformed into L-DNase II, a protein with a pro-apoptotic activity. LEI/L-DNase II can interact with BCL-2 and BAX in apoptotic and non-apoptotic conditions. These proteins both inhibit the L-DNase II pro-apoptotic activity
physiological function
the enzyme induces early humoral immune responses in infected mice. It may play an important role in the host-parasite interaction
physiological function
NUC-1 is the major DNase II for degrading apoptotic DNA
physiological function
key role of DNase II in DNA sensing by the DNA sensor Toll-like receptor 9 (TLR9). DNase II is required for TLR9 activation by bacterial genomic DNA. TLR9 responds to DNA fragments generated by DNase II
physiological function
the enzyme plays a role in degrading apoptotic DNA in distinct sites of the gonad, and acts as negative regulators of innate immunity
physiological function
deoxyribonuclease II has a major role in cellular DNA degradation
physiological function
lack of DNase II in hepatocytes induces RIP1-dependent non-apoptotic cell death with necrotic phenotype through the mitochondrial DNA-driven activation of TLR9/IFN-beta signaling pathway upon activation of the mitochondrial apoptotic pathway
physiological function
DNase II is responsible for DNA-degrading activity of saliva. DNase II is indispensable for SBPH survival on rice. DNase II secretion decreases H2O2 accumulation and callose deposition in rice. The presence of DNase II in the saliva helps degrade extracellular DNA, and prevents the surrounding plant cells from triggering plant defence responses
physiological function
-
during embryonic development, DNase II is involved in death of primordial germ cells. DNase II has to be translocated from cytoplasm, and primordial germ cell death is associated with DNase II-dependent DNA breaks. Mitochondrial protein AIF cooperates with DNase II to promote PGC death and mediates its nuclear translocation. DNA double-strand breaks activate the DNA damage-sensing enzyme, PARP-1 and the ATR/Chk1 branch of the DNA damage response. PARP-1 and DNase II engage in a positive feedback amplification loop resulting in primordial germ cell death
physiological function
-
knockdown of DNase2 isoforms leads to the slower repair of wounds. Isoform DN2-2 has no obvious effect on the clearance of biofilm of Staphylococcus aureus, an effect is found on clearance of the young biofilm of Pseudomonas aeruginosa
physiological function
DNASE2 knockdown inhibits proliferation and promotes apoptosis of hepatocellular carcinoma cells. DNASE2 overexpression shows the opposite results. miR-139-5p targets DNASE2 and suppresses its expression. Overexpression of miR-139-5p inhibits malignant phenotypes of hepatocellular carcinoma cells. Oncogene circ_0073228 is upregulated in hepatocellular carcinoma cells. Inhibition of miR-139-5p or overexpression of DNASE2 counteract the inhibitory effects of circ_0073228 knockdown on hepatocellular carcinoma cell progression
physiological function
-
three DNase II genes: nuc-1 plays a major role, crn-6 plays an auxiliary role, and crn-7 plays a negligible role in resolving 3' OH DNA breaks generated in apoptotic cells. NUC-1 constitutes the major DNase II activity and CRN-6 provides the minor DNase II activity in the organism. Nuc-1, crn-6 and crn-7 affect apoptotic DNA degradation but do not affect the activation or the kinetics of apoptosis. The crn-6 gene but not crn-7 can partially substitute for nuc-1 in mediating apoptotic DNA degradation and both fail to replace nuc-1 in degrading bacterial DNA in intestine. Despite of their restricted and largely non-overlapping expression patterns, both CRN-6 and NUC-1 can mediate apoptotic DNA degradation in many cells, suggesting that they are likely secreted nucleases that are retaken up by other cells to exert DNA degradation functions. NUC-1, but not CRN-6 or CRN-7, mediates degradation of chromosome DNA in ventral cord apoptotic cells and bacterial DNA in intestine. Neither CRN-6 nor CRN-7 can substitute for NUC-1 in digesting bacterial DNA in intestine. Nuc-1 can still promote apoptotic DNA degradation in both embryos and larvae when its expression is restricted to intestine cells. NUC-1 expressed in the head can mediate apoptotic DNA degradation in the posterior ventral cord
-
Show AA Sequence and Transmembrane Helices (1592 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
35000
36000
37000
38000
42000
43000
-
mutants N86Q, N212Q, N266Q, N290Q. It appears that the four sites each contribute to glycosylation and no additional glycosylation sites are responsible for the observed size
45000
46500
-
Western blot analysis or calculated (addition of the mass of sugar contents to the sequence-derived mass)
48000
two active DNase isoforms are detected in the digestive gland (48 and 37 kDa) and one in the gills (48 kDa)
35000
-
SDS-PAGE, derived from leukocyte elastase inhibitor protein after acidic treatment
37000
-
unglycosylated form of wild-type enzyme and N69Q mutant upon tunicamycin treatment
37000
two active DNase isoforms are detected in the digestive gland (48 and 37 kDa) and one in the gills (48 kDa)
45000
Western blot analysis, the incubation with tunicamycin results in a 37000 Da enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
alphabeta, 10000 + 27000, both subunits are bridged by a disulfide bond, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
Both enzymes alpha and beta contain four predicted N-glycosylation sites, including one site that is found in both proteins and one site found in enzyme beta for which the corresponding site in enzyme alpha does not fit the consensus. The N-glycosylation inhibitor tunicamycin diminishes the activity, but the deglycosylation with peptide N-glycosidase has no effect on protein activity
glycoprotein
glycosylation is apparently required for maximal enzyme activity
proteolytic modification
-
protein is synthesized as a precursor with a signal sequence
proteolytic modification
-
processing of DNase II in vivo is greatly altered in the liver of mice lacking cathepsin L. DNase II is extracellularly secreted from cells overexpressing DNase II and is detected as a pro-form, which is activated under acidic conditions. In transgenic COS1 cells, a band of 45 kDa colocalizeswith ER marker protein Bip and two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa in lysosomes
proteolytic modification
post-translational proteolytic processing (from a 48000 Da protein to a 37000 Da protein) is not an essential step for the activation of DNase.
proteolytic modification
-
epidermal growth factor triggers a cleavage of Leukocyte Elastase Inhibitor precursor into L-DNase II, its subsequent enzymatic activation and nuclear translocation
proteolytic modification
-
enzyme precursor Leukocyte Elastase Inhibitor is cleaved by elastase at its reactive center loop. Cleavage abolishes the antiprotease activity and leads to a conformational modification that exposes an endonuclease active site and a nuclear localization signal. Both endonuclease activity and nuclear translocation are needed to induce cell death
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of BthDNase II grown from a solution containing 0.0004 ml of protein at 26.5 mg/ml and 0.0004 ml of precipitant equilibrated against 0.080 ml of precipitant (100 mM BisTris pH 6.5, 28% (w/v) PEG MME 2000). A single crystal is cryo-protected with 15% (v/v) ethylene glycol and vitrified in liquid nitrogen. Crystal structure solved at 1.65 A resolution
structural model of protein. DNase IIalpha is a monomeric enzyme with pseudodimeric fold. It contains two requisite PLD-signature motifs in the N-terminal subdomains which together form a single active site
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A58del
in Japanese, African, Korean and Caucasian subjects, homozygous for the G292 allele. Shows almost no DNase II activity
D107N
-
although the mutant is capable of even greater glycosylation, this mutant results in some loss of activity
H188R
in Japanese, African, Korean and Caucasian subjects, homozygous for the A683 allele. DNase II activity is similar to that of the wild-type
H295A
N212Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N266Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N290Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N69Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N86Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
Q322Term
R23I
in Japanese, African, Korean and Caucasian subjects, homozygous for the G188 allele. DNase II activity is similar to that of the wild-type
R298L
in Japanese, African, Korean and Caucasian subjects, homozygous for the G1013 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
V190I
in Korean subjects,heterozygous for the G688 and A688 alleles. In Japanese, homozygous for the G688 allele. DNase II activity is similar to that of the wild-type
V284M
in Japanese, African, Korean and Caucasian subjects, homozygous for the G970 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
AP10T
-
point mutation in the hinge region of LEI, has decreased anti-protease activity. Cells overexpressing wild-type LEI or AP10T-LEI have the same survival rate under unstressed condition. Mutant retains its pro-apoptotic activity when transformed into L-DNase II by an apoptotic stimulus (e.g., hexa-methylene-amiloride treatment). When mutant cells are treated with etoposide they do not present the same survival rate than wild-type cells
H115
extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding
H132L
soluble, very little catalytic activity. Protein is improperly folded and degraded via the proteosomal pathway within 24 h
H297L
extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding
V295A
-
exhibits a significant cell death compared to the wild-type, highest rate of cells with nuclear retention of LEI
additional information
Q322Term
in Japanese, African, Korean and Caucasian subjects, homozygous for the C1084 allele. Shows almost no DNase II activity
additional information
-
Mutations in nuc-1 block the conversion of TUNEL-reactive DNA to a subsequent TUNEL-unreactive state.
additional information
-
knock-down of enzyme activity by RNAi results in a dramatic reduction in enzymic activity and a significant decrease in total hemocyte numbers. Infection of knock-down flies with Gram negative or positive bacteria results in a severe reduction in fly viability
additional information
-
mutation of the histidine moiety of His 368 completely abolishes endonuclease activity of L-DNase II
additional information
-
DNase IIdeficient mouse embryos accumulate undigested DNA in macrophages, which are present in all tissues, such as the thymus, kidney, interdigit, spleen, and liver. The accumulation of undegraded DNA also stimulates production of interferon-beta, and eventually causes death of the knockout mice. Peripheral blood of DNase II-/- embryos contain massive nucleated erythrocytes and no live DNase II-/- mice are born because of severe respiratory disturbance. Deficiency of the DNase II in adult mice is not lethal
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
polyethyleneglycol
-
activity remaines unchanged when stored at -40°C for 12 months
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 1 mM PMSF, 50% glycerol v/v, several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
commercially available DNase II further purified by chromatography steps to homogeneity
-
near homogeneity by chromatography steps
partial
to homogeneity by 6step chromatography techniques
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA of pDNase II cloned in the pcDNA3 vector and transfected into HEK 293T cells
-
DNA fragment containing the entire coding sequence of DNase II cDNA amplified and ligated into pcDNA3.1(+). Mutants corresponding to each single nucleotide polymorphism expressed in COS-7 cell
Escherichia coli BL21(DE3) pLysS strain transformed with a pET 23d(+) plasmid coding for LEI with a 6x His tag. PZeo-LEI wild-type transfected into HeLa cells, MEF cell lines or BHK-21 cells
-
expression in Chinese hamster ovary cells
expression in COS-7 cells
expression in human embryonic kidney 293 cells
LEI cDNA subcloned into pZeoSV2+, into pET23d+ in frame with the His-tag, and into pDsRed2-C1 plasmid in frame with the red fluorescent protein fused to its N-term. Expression in Escherichia coli strain BL21(DE3) pLysS. BHK cells transfected with a pZeo vector containing the wild-type or a punctually mutated LEI cDNA
-
MEF-/- cells null for enzyme expression and activity are transiently transfected with plasmid-expression constructs encoding wild-type human DNase IIalpha, pD2, or mutant forms
-
nuc-1, crn-7 or crn-6 coding sequence without a stop codon amplified and inserted into the pPD95.79 vector. Transcriptional reporter constructs containing the promoter of the DNase II gene fused to GFP with four tandem copies of the nuclear localization signal (NLS) injected into wild-type animals (embryos, larvae and adults)
-
Sp1 and Sp3 play a pivotal role in the transcriptional activation of DNase II in HL-60 cells during phorbol 12-myristate-13-acetate induced differentiation
-
the gene encoding DNase IIbeta has identical splice sites to DNase IIalpha
the subsequent targeted disruption of the DNase II gene confirms the requirement of DNase II activity within phagocytic cells
-
the wild-type and mutant enzyme cDNA plasmid are transiently transfected in HCT116 cells
wild-type or mutant LEI expressed in BHK-21 cells. 6xHis tagged wild-type and mutant LEI expressed from pET 23d(+) plasmid in Escherichia coli BL21(DE3)pLysS strain. Wild-type LEI expressed in HeLa cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated in varying degrees upon wounding and challenge with bacteria
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotinylated forward and fluorescein-labeled reverse primers
degradation
Caenorhabditis elegans effectively degrades approximately 99.999% of extracellular antibiotic resistance genes (tetM and kan) in 84 h and completely deactivates them within a few hours, primarily via deoxyribonuclease II present in the excretory and secretory products. C. elegans is effective in degrading extracellular antibiotic resistance genes under the effects of natural organic matter, cations, at 1, 20, and 30°C, and in surface water and wastewater samples
medicine
additional information
medicine
-
polymorphisms in the DNase II gene might play important roles in controlling renal disorder among patients with systemic lupus erythematosus
medicine
-
epidermal growth factor triggers a cleavage of Leukocyte Elastase Inhibitor precursor into L-DNase II, its subsequent enzymatic activation and nuclear translocation. Epidermal growth factor-induced cell death can be blocked by paraptosis inhibitor AIP-1/alix
medicine
-
incubation of retinal cells in the presence of corticoids induces a specific and dose-dependent reduction of cell viability. L-Dnase II is not involved
medicine
-
DNase II in Trichinella spiralis are secreted into circulation to cleave undigested DNA from apoptotic host cells, which reduces the innate immune response. The role played by DNase II in Trichinella spiralis may be a self-protective mechanism. DNase IIbeta or DNase II of Trichinella spiralis can be considered a candidate protein for therapy of autoimmune diseases, DNase IIdeficient diseases, or cancer
medicine
-
DNase II in macrophage lysosomes is responsible for definitive erythropoiesis in mouse fetal liver
medicine
-
immunization of healthy rabbits with DNase II produces IgGs with intrinsic DNase and RNase activities. 10% of the total IgG DNase and RNase activities belong to anti-idiotypic antibodies to DNase II (ca. 0.1% of total pIgGs), while 90% of the activities do not interact with Sepharose bearing antibodies against DNase II and might be antibodies to nucleic acids bound to DNase II. Fraction of abzymes hydrolyzing both DNA and RNA can contain subfraction of antibodies against DNase II
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
medicine
-
high expression of LEI in tumor cells may reduce the efficiency of etoposide as a chemotherapeutic agent. LEI inhibits cathepsin D, released from the lysosome during etoposide treatment. Cathepsin D enhances caspase activity in the cell by cleaving procaspase-8 and LEI overexpression slows down this cleavage, protecting cells from apoptosis
medicine
non-synonymous single nucleotide polymorphisms in the DNase II gene may have clinical implications in relation to the prevalence of autoimmune diseases
medicine
the enzymes DNase II-1 and DNase II-7 are the potential target molecules for anti-Trichinella vaccine for blocking both larval invasion and development
medicine
DNASE2 knockdown inhibits proliferation and promotes apoptosis of hepatocellular carcinoma cells. DNASE2 overexpression shows the opposite results. miR-139-5p targets DNASE2 and suppresses its expression. Overexpression of miR-139-5p inhibits malignant phenotypes of hepatocellular carcinoma cells. Oncogene circ_0073228 is upregulated in hepatocellular carcinoma cells. Inhibition of miR-139-5p or overexpression of DNASE2 counteract the inhibitory effects of circ_0073228 knockdown on hepatocellular carcinoma cell progression
additional information
-
DNase II enzyme and the ability to clear macromolecular DNA are essential for maintaining proper immune function in Drosophila
additional information
-
the DNase II from the crown-of-thorns starfish Acanthaster planci is toxic
additional information
-
potential of acid DNase response in mussels to serve as a biomarker of contaminant exposure, whereby the digestive gland is a suitable tissue for discrimination of polluted areas from maricultured area. Since acid DNase activity in mussel Mytilus galloprovincilais is tissue-specific and pollutant-specific the digestive gland/hemocyte (Hep/Hem) ratio reveals a pollutant effect that can not be detected by acid DNase measurement in single tissue only
additional information
-
caspase-independent apoptosis induced by hexamethylene amiloride, LEI/L-DNase II can activate PARP-1 and promote its auto-poly(ADP-ribosyl)ation, thus inhibiting PARP-1 activity. Overexpression of LEI blocks the pro-survival effect of PARP-1 in this model of cell death
additional information
-
a nuclear export signal on LEI involved in the control of LEI/L-DNase II nuclearization in healthy cells
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YEAR
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Molecular cloning and characterization of human and murine DNase II
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215
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The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis
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L-DNase II, a molecule that links proteases and endonucleases in apoptosis, derives from the ubiquitous serpin leukocyte elastase inhibitor
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Involvement of DNase II in nuclear degeneration during lens cell differentiation
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Barry, M.A.; Eastman, A.
Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
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300
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Cricetulus griseus
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Human urine deoxyribonuclease II (DNase II) isoenzymes: a novel immunoaffinity purification, biochemical multiplicity, genetic heterogeneity and broad distribution among tissues and body fluids
Biochim. Biophys. Acta
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Homo sapiens
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Mechanism of action of deoxyribonuclease II from human lymphoblasts
Eur. J. Biochem.
202
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1991
Homo sapiens
brenda
Liao, T.H.; Liao, W.C.; Chang, H.C.; Lu, K.S.
Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates
Biochim. Biophys. Acta
1007
15-22
1989
Sus scrofa
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Spitzer, S.; Eckstein, F.
Inhibition of deoxyribonucleases by phosphorothioate groups in oligonucleotides
Nucleic Acids Res.
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11691-11704
1988
Sus scrofa
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Galcheva-Gargova, Z.; Davidov, V.; Dessev, G.
Formation of single-stranded regions in the course of digestion of DNA with DNaseII and micrococcal nuclease
Arch. Biochem. Biophys.
240
464-469
1985
Mammalia
brenda
Drew, H.R.
Structural specificities of five commonly used DNA nucleases
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176
535-557
1984
Mammalia
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Anai, M.; Muta, A.; Umeno, M.; Sasaki, M.
Purification and properties of an acid deoxyribonuclease from rat small intestinal mucosa
J. Biochem.
94
339-344
1983
Rattus sp.
brenda
Eshima, N.; Muta, A.; Anai, M.
Inhibitory effect of bovine serum albumin on acid deoxyribonuclease from rat small intestinal mucosa
J. Biochem.
94
345-352
1983
Rattus sp., Cavia porcellus
brenda
Wood, W.I.; Felsenfeld, G.
Chromatin structure of the chicken beta-globin gene region
J. Biol. Chem.
257
7730-7736
1982
Gallus gallus
brenda
Shakhov, A.N.; Nedospasov, S.A.; Georgiev, G.P.
Deoxyribonuclease III as a probe to sequence-specific chromatin organisation: preferential cleavage in the 72 bp modulator sequence of SV40 minichromosome
Nucleic Acids Res.
10
3951-3965
1982
Mammalia
brenda
Keys, D.S.; Zbarsky, S.H.
Isolation of deoxyribonuclease II from bovine intestinal mucosa
Can. J. Biochem.
58
749-753
1980
Bos taurus
brenda
Horz, W.; Miller, F.; Klobeck, G.; Zachau, H.G.
Deoxyribonuclease II as a probe for chromatin structure. II. Mode of cleavage
J. Biol. Chem.
144
328-351
1980
Mammalia
-
brenda
Horz, W.; Zachau, H.G.
Deoxyribonuclease II as a probe for chromatin structure. I. Location of cleavage sites
J. Biol. Chem.
144
305-327
1980
Mammalia
brenda
Murai, K.; Yamanaka, M.; Akagi, K.; Anai, M.
Purification and properties of deoxyribonuclease II from human urine
J. Biochem.
87
1097-1103
1980
Homo sapiens
brenda
Sollner-Webb, B.; Melchior, W.; Felsenfeld jr., G.
DNase I, DNase II and staphylococcal nuclease cut at different, yet symmetrically located, sites in the nucleosome core
Cell
14
611-627
1978
Mammalia
brenda
Sieliwanowicz, B.; Yamamoto, M.; Stasuik, L.; Laskowski sr., M.
Studies of specificity of deoxyribonuclease from salmon testes
Biochemistry
14
39-46
1975
Oncorhynchus tshawytscha
brenda
Slor, H.
Purification of 14C-labelled deoxyribonuclease II from HeLa S3 lysosomes and its use as a marker for the study of nuclear deoxyribonuclease II
Biochem. J.
136
83-87
1973
Homo sapiens
brenda
Laval, J.; Thiery, J.P.; Ehrlich, S.D.; Paoletti, C.; Bernardi, G.
Studies on the specificity of an acid deoxyribonuclease from Helix aspersa (Mll.)
Eur. J. Biochem.
40
133-137
1973
Cornu aspersum
brenda
Schabort, J.C.
Affinity chromatography of bovine pancreatic and hog spleen deoxyribonucleases
J. Chromatogr.
73
253-256
1972
Sus scrofa
brenda
Dulaney, J.T.; Touster, O.
Isolation of deoxyribonuclease II of rat liver lysosomes
J. Biol. Chem.
247
1424-1432
1972
Rattus sp.
brenda
Yamamoto, M.; Bicknell, L.H.
Salmon testes deoxyribonuclease: large-scale purification and properties
Arch. Biochem. Biophys.
151
261-269
1972
Oncorhynchus tshawytscha
-
brenda
Sicard, P.J.; Obrenovich, A.; Sadron, A.
A new approach to the elucidation of the initial kinetics of neutral and acid deoxyribonucleases
Biochim. Biophys. Acta
268
468-479
1972
Sus scrofa
brenda
Bernarde, G.
Spleen acid deoxyribonuclease
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
271-287
1971
Sus scrofa
-
brenda
Slor, H.; Lev, T.
Acid deoxyribonuclease activity in purified calf thymus nuclei
Biochem. J.
123
993-995
1971
Bos taurus
brenda
Maly, A.
Deoxyribonuclease II from avian leukemic myeloblasts. II. Specificity of cleavage, electrophoresis of the enzyme and its subcellular localization
Collect. Czech. Chem. Commun.
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2980-2985
1971
Gallus gallus
-
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Slor, H.; Hodes, M.E.
Purification of deoxyribonuclease II from sheep spleen
Arch. Biochem. Biophys.
139
172-178
1970
Ovis aries aries
brenda
Schroeder, W.A.; Shelton, R.J.; Shelton, J.B.; Robberson, B.; Apell, G.
DNase II inhibitor in tissues and urine - pH and salt artifacts
Arch. Biochem. Biophys.
131
652-658
1969
Homo sapiens
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Nuske, R.; Venner, H.
Zur Reinigung von Deoxyribonuclease II
Hoppe-Seyler's Z. Physiol. Chem.
350
1472-1473
1969
Bos taurus
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Swenson, M.K.; Hodes, M.E.
The separation of the phosphodiesterase and deoxyribonuclease II activities of bovine spleen
J. Biol. Chem.
244
1803-1807
1969
Bos taurus
brenda
Carrara, M.; Bernardi, G.
Studies on acid deoxyribonuclease. V. The oligonucleotides obtained from deoxyribonucleic acid and their 3'-phosphate termini
Biochemistry
7
1121-1131
1968
Sus scrofa
brenda
Georgatsos, J.G.
Bond-cleaving specificity of a deoxyribonuclease II from mouse mammary tumors
Biochim. Biophys. Acta
142
128-132
1967
Mus musculus
brenda
Popov, A.P.; Konichev, A.S.; Tsvetkov, I.L.
Effect of toxic industrial pollutants on the activity and isoforms of acid DNase in the freshwater snail Viviparus viviparus L
Appl. Biochem. Microbiol.
39
454-458
2003
Viviparus viviparus
-
brenda
MacLea, K.S.; Krieser, R.J.; Eastman, A.
Revised structure of the active form of human deoxyribonuclease IIalpha
Biochem. Biophys. Res. Commun.
292
415-421
2002
Homo sapiens (Q8WZ79), Homo sapiens
brenda
MacLea, K.S.; Krieser, R.J.; Eastman, A.
Structural requirements of human DNase II alpha for formation of the active enzyme: the role of the signal peptide, N-glycosylation, and disulphide bridging
Biochem. J.
371
867-876
2003
Homo sapiens
brenda
Krieser, R.J.; MacLea, K.S.; Longnecker, D.S.; Fields, J.L.; Fiering, S.; Eastman, A.
Deoxyribonuclease IIalpha is required during the phagocytic phase of apoptosis and its loss causes perinatal lethality
Cell Death Differ.
9
956-962
2002
Mus musculus
brenda
Ikeda, S.; Takata, N.
Deoxyribonuclease II purified from Euglena gracilis SM-ZK, a chloroplast-lacking mutant: comparison with porcine spleen deoxyribonuclease II
Comp. Biochem. Physiol. B
131
519-525
2002
Euglena gracilis, Sus scrofa, Euglena gracilis SM-ZK
brenda
Chou, S.F.; Chen, H.L.; Lu, S.C.
Sp1 and Sp3 are involved in up-regulation of human deoxyribonuclease II transcription during differentiation of HL-60 cells
Eur. J. Biochem.
270
1855-1862
2003
Homo sapiens
brenda
Lyon, C.J.; Evans, C.J.; Bill, B.R.; Otsuka, A.J.; Aguilera, R.J.
The C. elegans apoptotic nuclease NUC-1 is related in sequence and activity to mammalian DNase II
Gene
252
147-154
2000
Caenorhabditis elegans
brenda
Krieser, R.J.; MacLea, K.S.; Park, J.P.; Eastman, A.
The cloning, genomic structure, localization, and expression of human deoxyribonuclease IIbeta
Gene
269
205-216
2001
Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus
brenda
MacLea, K.S.; Krieser, R.J.; Eastman, A.
A family history of deoxyribonuclease II: surprises from Trichinella spiralis and Burkholderia pseudomallei
Gene
305
1-12
2003
Homo sapiens (O00115), Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus (P56542), Mus musculus (Q9QY48), Rattus norvegicus (Q9QZK8), Rattus norvegicus (Q9QZK9), Bos taurus (P56541), Sus scrofa (O62855), Drosophila melanogaster (Q7JYM9), Caenorhabditis elegans (Q17778), Caenorhabditis elegans (P34508), Caenorhabditis elegans (P34387), Caenorhabditis elegans, Caenorhabditis elegans NUC-1 (Q17778), Caenorhabditis elegans K04H4.6 (P34508), Caenorhabditis elegans F09G8.2 (P34387)
brenda
Evans, C.J.; Aguilera, R.J.
DNase II: genes, enzymes and function
Gene
322
1-15
2003
Caenorhabditis elegans, Drosophila melanogaster, Mus musculus, Homo sapiens, Caenorhabditis elegans NUC-1
brenda
Wu, Y.C.; Stanfield, G.M.; Horvitz, H.R.
NUC-1, a caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis
Genes Dev.
14
536-548
2000
Caenorhabditis elegans
brenda
Kawane, K.; Fukuyama, H.; Kondoh, G.; Takeda, J.; Ohsawa, Y.; Uchiyama, Y.; Nagata, S.
Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver
Science
292
1546-1549
2001
Mus musculus
brenda
Stepinska, U.; Olszanska, B.
Detection of deoxyribonuclease I and II activities in Japanese quail oocytes
Zygote
9
1-7
2001
Coturnix japonica
brenda
Cymerman, I.A.; Meiss, G.; Bujnicki, J.M.
DNase II is a member of the phospholipase D superfamily
Bioinformatics
21
3959-3962
2005
Homo sapiens
brenda
Overbo, K.; Myrnes, B.
Deoxyribonuclease II from the Icelandic scallop (Chlamys islandica): isolation and partial characterization
Comp. Biochem. Physiol. B
143
315-318
2006
Chlamys islandica
brenda
Maclea, K.S.; Cheng, H.H.
Cloning and expression of deoxyribonuclease II from chicken
Gene
373
44-51
2006
Gallus gallus (Q2XP49), Gallus gallus
brenda
Ye, M.; Hu, Z.; Fan, Y.; He, L.; Xia, F.; Zou, G.
Purification and characterization of an acid deoxyribonuclease from the cultured mycelia of Cordyceps sinensis
J. Biochem. Mol. Biol.
37
466-473
2004
Ophiocordyceps sinensis
brenda
Shin, H.D.; Park, B.L.; Cheong, H.S.; Lee, H.S.; Jun, J.B.; Bae, S.C.
DNase II polymorphisms associated with risk of renal disorder among systemic lupus erythematosus patients
J. Hum. Genet.
50
107-111
2005
Homo sapiens
brenda
Bergsmedh, A.; Ehnfors, J.; Kawane, K.; Motoyama, N.; Nagata, S.; Holmgren, L.
DNase II and the Chk2 DNA damage pathway form a genetic barrier blocking replication of horizontally transferred DNA
Mol. Cancer Res.
4
187-195
2006
Mus musculus
brenda
Brossas, J.Y.; Tanguy, R.; Brignole-Baudouin, F.; Courtois, Y.; Torriglia, A.; Treton, J.
L-DNase II associated with active process during ethanol induced cell death in ARPE-19
Mol. Vis.
10
65-73
2004
Homo sapiens
brenda
Chahory, S.; Padron, L.; Courtois, Y.; Torriglia, A.
The LEI/L-DNase II pathway is activated in light-induced retinal degeneration in rats
Neurosci. Lett.
367
205-209
2004
Rattus norvegicus, Rattus norvegicus Fischer
brenda
Shiomi, K.; Midorikawa, S.; Ishida, M.; Nagashima, Y.; Nagai, H.
Plancitoxins, lethal factors from the crown-of-thorns starfish Acanthaster planci, are deoxyribonucleases II
Toxicon
44
499-506
2004
Acanthaster planci (Q75WF2)
brenda
Fombonne, J.; Padron, L.; Enjalbert, A.; Krantic, S.; Torriglia, A.
A novel paraptosis pathway involving LEI/L-DNaseII for EGF-induced cell death in somato-lactotrope pituitary cells
Apoptosis
11
367-375
2006
Rattus norvegicus
brenda
Cheng, Y.C.; Hsueh, C.C.; Lu, S.C.; Liao, T.H.
Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II
Biochem. J.
398
177-185
2006
Sus scrofa (O62855), Sus scrofa
brenda
Seong, C.S.; Varela-Ramirez, A.; Aguilera, R.J.
DNase II deficiency impairs innate immune function in Drosophila
Cell. Immunol.
240
5-13
2006
Drosophila melanogaster
brenda
Lopez-Oliva, M.E.; Agis-Torres, A.; Marquez, E.; Munoz-Martinez, E.
Growth hormone modulates the degradative capacity of muscle nucleases but not of cathepsin D in post-weaning mice
Comp. Biochem. Physiol. A
148A
159-167
2007
Mus musculus
-
brenda
Overbo, K.; Myrnes, B.
Deoxyribonuclease II from the Icelandic scallop (Chlamys islandica): Isolation and partial characterization
Comp. Biochem. Physiol. B
143B
315-318
2006
Chlamys islandica
-
brenda
Nakahara, M.; Nagasaka, A.; Koike, M.; Uchida, K.; Kawane, K.; Uchiyama, Y.; Nagata, S.
Degradation of nuclear DNA by DNase II-like acid DNase in cortical fiber cells of mouse eye lens
FEBS J.
274
3055-3064
2007
Mus musculus
brenda
Lopez-Oliva, M.E.; Agis-Torres, A.; Munoz-Martinez, E.
The modulator effect of GH on skeletal muscle lysosomal enzymes is dietary protein dependent
Growth Horm. IGF Res.
17
137-148
2007
Mus musculus
brenda
De Maria, A.; Bassnett, S.
DNase IIbeta distribution and activity in the mouse lens
Invest. Ophthalmol. Vis. Sci.
48
5638-5646
2007
Mus musculus
brenda
Cherepanova, A.; Tamkovich, S.; Pyshnyi, D.; Kharkova, M.; Vlassov, V.; Laktionov, P.
Immunochemical assay for deoxyribonuclease activity in body fluids
J. Immunol. Methods
325
96-103
2007
Homo sapiens
brenda
Padron-Barthe, L.; Lepretre, C.; Martin, E.; Counis, M.F.; Torriglia, A.
Conformational modification of serpins transforms leukocyte elastase inhibitor into an endonuclease involved in apoptosis
Mol. Cell. Biol.
27
4028-4036
2007
Sus scrofa
brenda
Valamanesh, F.; Torriglia, A.; Savoldelli, M.; Gandolphe, C.; Jeanny, J.C.; BenEzra, D.; Behar-Cohen, F.
Glucocorticoids induce retinal toxicity through mechanisms mainly associated with paraptosis
Mol. Vis.
13
1746-1757
2007
Rattus norvegicus
brenda
Schaefer, P.; Cymerman, I.A.; Bujnicki, J.M.; Meiss, G.
Human lysosomal DNase IIalpha contains two requisite PLD-signature (HxK) motifs: evidence for a pseudodimeric structure of the active enzyme species
Protein Sci.
16
82-91
2007
Homo sapiens
brenda
Fafandel, M.; Bihari, N.; Peric, L.; Cenov, A.
Effect of marine pollutants on the acid DNase activity in the hemocytes and digestive gland of the mussel Mytilus galloprovincialis
Aquat. Toxicol.
86
508-513
2008
Mytilus galloprovincialis
brenda
Torriglia, A.; Lepretre, C.; Padron-Barthe, L.; Chahory, S.; Martin, E.
Molecular mechanism of L-DNase II activation and function as a molecular switch in apoptosis
Biochem. Pharmacol.
76
1490-1502
2008
Homo sapiens, Cricetulus griseus, Gallus gallus, Rattus norvegicus, Mus musculus
brenda
Lepretre, C.; Fleurier, Y.; Martin, E.; Torriglia, A.
Nuclear export of LEI/L-DNase II by Crm1 is essential for cell survival
Biochim. Biophys. Acta
1783
1068-1075
2008
Homo sapiens, Sus scrofa, Cricetulus griseus
brenda
Padron-Barthe, L.; Courta, J.; Lepretre, C.; Nagbou, A.; Torriglia, A.
Leukocyte Elastase Inhibitor, the precursor of L-DNase II, inhibits apoptosis by interfering with caspase-8 activation
Biochim. Biophys. Acta
1783
1755-1766
2008
Sus scrofa
brenda
Liu, M.F.; Wu, X.P.; Wang, X.L.; Yu, Y.L.; Wang, W.F.; Chen, Q.J.; Boireau, P.; Liu, M.Y.
The functions of Deoxyribonuclease II in immunity and development
DNA Cell Biol.
27
223-228
2008
Trichinella spiralis, Homo sapiens, Sus scrofa, Mus musculus, Drosophila sp. (in: flies), Acanthaster planci, Haemonchus contortus
brenda
Huang, R.T.; Liao, T.H.; Lu, S.C.
Proteolytic processing of porcine deoxyribonuclease II occurs in lysosomes but is not required for enzyme activation
FEBS J.
276
1891-1899
2009
Sus scrofa
brenda
Krasnorutskii, M.A.; Buneva, V.N.; Nevinsky, G.A.
Immunization of rabbits with DNase II leads to formation of polyclonal antibodies with DNase and RNase activities
Int. Immunol.
21
349-360
2009
Bos taurus
brenda
Lepretre, C.; Scovassi, A.I.; Shah, G.M.; Torriglia, A.
Regulation of poly(ADP-ribose) polymerase-1 functions by leukocyte elastase inhibitor/LEI-derived DNase II during caspase-independent apoptosis
Int. J. Biochem. Cell Biol.
41
1046-1054
2009
Sus scrofa
brenda
Ueki, M.; Takeshita, H.; Fujihara, J.; Kimura-Kataoka, K.; Iida, R.; Yuasa, I.; Nakajima, T.; Kominato, Y.; Yasuda, T.
Genetic and expression analysis of all 7 non-synonymous single nucleotide polymorphisms in the human deoxyribonuclease II gene, with potential relevance to autoimmunity
Clin. Chim. Acta
411
92-98
2010
Homo sapiens (O00115), Homo sapiens
brenda
Lai, H.; Lo, S.; Kage-Nakadai, E.; Mitani, S.; Xue, D.
The roles and acting mechanism of Caenorhabditis elegans DNase II genes in apoptotic DNA degradation and development
PLoS ONE
4
e7348
2009
Caenorhabditis elegans, Caenorhabditis elegans N2 Bristol
brenda
Montero, J.A.; Lorda-Diez, C.I.; Certal, A.C.; Moreno, N.; Rodriguez-Leon, J.; Torriglia, A.; Hurle, J.M.
Coordinated and sequential activation of neutral and acidic DNases during interdigital cell death in the embryonic limb
Apoptosis
15
1197-1210
2010
Gallus gallus
brenda
Crow, Y.J.
The story of DNase II: a stifled death-wish leads to self-harm
Eur. J. Immunol.
40
2376-2378
2010
Mus musculus
brenda
Fischer, H.; Scherz, J.; Szabo, S.; Mildner, M.; Benarafa, C.; Torriglia, A.; Tschachler, E.; Eckhart, L.
DNase 2 is the main DNA-degrading enzyme of the stratum corneum
PLoS ONE
6
e17581
2011
Homo sapiens, Mus musculus
brenda
Jaadane, I.; Nagbou, A.; Behar-Cohen, F.; Torriglia, A.
Interaction of leukocyte elastase inhibitor/L-DNase II with BCL-2 and BAX
Biochim. Biophys. Acta
1843
2807-2815
2014
Homo sapiens
brenda
Ohkouchi, S.; Shibata, M.; Sasaki, M.; Koike, M.; Safig, P.; Peters, C.; Nagata, S.; Uchiyama, Y.
Biogenesis and proteolytic processing of lysosomal DNase II
PLoS ONE
8
e59148
2013
Mus musculus
brenda
Laine, L.M.; Biddau, M.; Byron, O.; Mueller, S.
Biochemical and structural characterization of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum
Biosci. Rep.
35
e00171
2015
Caenorhabditis elegans (Q17778)
brenda
Yu, H.; Lai, H.J.; Lin, T.W.; Chen, C.S.; Lo, S.J.
Loss of DNase II function in the gonad is associated with a higher expression of antimicrobial genes in Caenorhabditis elegans
Biochem. J.
470
145-154
2015
Caenorhabditis elegans (Q17778), Caenorhabditis elegans (P34387), Caenorhabditis elegans
brenda
Hou, N.; Piao, X.; Cai, P.; Wu, C.; Liu, S.; Xiao, Y.; Chen, Q.
A novel Schistosoma japonicum endonuclease homologous to DNase II
BMC Genomics
16
126
2015
Schistosoma japonicum (Q5DFP6), Schistosoma japonicum
brenda
Qi, X.; Yue, X.; Han, Y.; Jiang, P.; Yang, F.; Lei, J.J.; Liu, R.D.; Zhang, X.; Wang, Z.Q.; Cui, J.
Characterization of two Trichinella spiralis adult-specific DNase II and their capacity to induce protective immunity
Front. Microbiol.
9
2504
2018
Trichinella spiralis (Q32R75), Trichinella spiralis (Q32R69), Trichinella spiralis
brenda
Kovacic, I.; Fafandel, M.; Bihari, N.
Lysosomal deoxyribonuclease II from the mussel Mytilus galloprovincialis Characterization and seasonal activity
Mar. Biol. Res.
11
716-724
2015
Mytilus galloprovincialis (A0A3L5TW17)
-
brenda
Chan, M.P.; Onji, M.; Fukui, R.; Kawane, K.; Shibata, T.; Saitoh, S.; Ohto, U.; Shimizu, T.; Barber, G.N.; Miyake, K.
DNase II-dependent DNA digestion is required for DNA sensing by TLR9
Nat. Commun.
6
5853
2015
Mus musculus (P56542)
brenda
Varela-Ramirez, A.; Abendroth, J.; Mejia, A.A.; Phan, I.Q.; Lorimer, D.D.; Edwards, T.E.; Aguilera, R.J.
Structure of acid deoxyribonuclease
Nucleic Acids Res.
45
6217-6227
2017
Burkholderia thailandensis (Q2T8B0), Burkholderia thailandensis, Burkholderia thailandensis ATCC 700388 (Q2T8B0)
brenda
Saito, Y.; Hikita, H.; Nozaki, Y.; Kai, Y.; Makino, Y.; Nakabori, T.; Tanaka, S.; Yamada, R.; Shigekawa, M.; Kodama, T.; Sakamori, R.; Tatsumi, T.; Takehara, T.
DNase II activated by the mitochondrial apoptotic pathway regulates RIP1-dependent non-apoptotic hepatocyte death via the TLR9/IFN-beta signaling pathway
Cell Death Differ.
26
470-486
2019
Mus musculus (P56542)
brenda
Dong, W.; Liu, Y.; Hou, J.; Zhang, J.; Xu, J.; Yang, K.; Zhu, L.; Lin, D.
Nematodes degrade extracellular antibiotic resistance genes by secreting DNase II encoded by the nuc-1 gene
Environ. Sci. Technol.
57
12042-12052
2023
Caenorhabditis elegans (Q17778)
brenda
Sun, Z.; Yu, T.; Cao, X.; Gao, L.; Pang, Q.; Liu, B.; Deng, H.
Identification and characterization of deoxyribonuclease II in planarian Dugesia japonica
Gene
826
146464
2022
Dugesia japonica
brenda
Bai, L.; Yu, Z.; Li, Q.; Hu, X.; Liu, X.; Li, F.; Li, S.; Chen, Y.
Circ_0073228 serves as a competitive endogenous ribonucleic acid to facilitate proliferation and inhibit apoptosis of hepatocellular carcinoma cells by the miR-139-5p/deoxyribonuclease II axis
J. Gene Med.
25
e3507
2023
Homo sapiens (O00115)
brenda
Aslan, E.; Arslanyolu, M.
Discovery of deoxyribonuclease II-like proteins in bacteria
Mol. Phylogenet. Evol.
174
107554
2022
Bacteria
brenda
Tarayrah-Ibraheim, L.; Maurice, E.C.; Hadary, G.; Ben-Hur, S.; Kolpakova, A.; Braun, T.; Peleg, Y.; Yacobi-Sharon, K.; Arama, E.
DNase II mediates a parthanatos-like developmental cell death pathway in Drosophila primordial germ cells
Nat. Commun.
12
2285
2021
Drosophila melanogaster
brenda
Huang, H.J.; Cui, J.R.; Xia, X.; Chen, J.; Ye, Y.X.; Zhang, C.X.; Hong, X.Y.
Salivary DNase II from Laodelphax striatellus acts as an effector that suppresses plant defence
New Phytol.
224
860-874
2019
Laodelphax striatellus (A0A482XFQ4)
brenda
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