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190mer DNA fragment + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
3'AMP + H2O
adenosine + phosphate
-
phosphomonoesterase activity
-
?
calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
cosmid DNA + H2O
?
-
-
-
-
?
crab d(A-T) polymer + H2O
5'-hexanucleotides + ?
-
unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure
enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage
?
d(pA)10 + H2O
?
-
-
-
-
?
d(pApCpTpApCpApGpTpCpTpApCpA) + H2O
?
-
-
-
-
?
d(pGpGpCpApCpTpTpApC) + H2O
?
-
-
-
-
?
d(pT)10 + H2O
?
-
-
-
-
?
d(pTpApGpApApGpApTpCpApApA) + H2O
?
-
-
-
-
?
d-ApApTp + H2O
pTp + d-ApA
-
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
DNA + H2O
5'-phosphodinucleotides + 5'-phosphooligonucleotides
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
DNA + H2O
5'-phosphotrinucleotides + ?
double-stranded circular DNA + H2O
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
double-stranded DNA + H2O
?
double-stranded linear DNA + H2O
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
Fc-oligo-SH + H2O
?
-
degradation of a thiolated ferrocenyloligonucleotide, efficiency of DNase I reaction on the electrode is 48, 72, or 73% when treated with 1 microl of 2, 1, or 0.5 micromol ferrocenyloligonucleotide, respectively. DNase I can cleave the oligonucleotide on the gold surface and does not show a nonspecific surface absorption
-
-
?
H2AL2 nucleosome core particle + H2O
?
-
DNase I and hydroxyl radical footprinting as well as micrococcal and exonuclease III digestion show alterations in the structure of the histone variant H2AL2 nucleosome all over the nucleosomal DNA length
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
HMIP-2 + H2O
?
-
identifies three tissue-specific DNase I hypersensitive sites in the core intergenic interval
-
-
?
lambda phage DNA + H2O
?
-
-
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
NO2-Ph-pdTp-NO2-Ph + H2O
p-nitrophenol + ?
-
-
-
?
NO2-Ph-pdTp-NO2Ph + H2O
p-nitrophenol + NO2-Ph-pdT-3'-phosphate
-
rapidly hydrolyzed at a single bond
-
?
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
phage M13 DNA + H2O
?
-
endolytically cleavage generating single base nicks
-
?
poly(dA) + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
poly(dT) + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
pUC18 DNA + H2O
?
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
RNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
RNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
RNA + H2O
?
-
low activity
-
?
salmon sperm DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
single-stranded circular DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for single-stranded regions
-
?
single-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
single-stranded DNA + H2O
?
-
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
supercoiled DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
in presence of Mg2+ and Ca2+ under neutral conditions
production of 3'-OH and 5'-phosphate ends
?
supercoiled plasmid DNA + H2O
linear DNA + ?
supercoiled pUC18 DNA + H2O
?
-
endolytically cleavage generating single base nicks
-
?
Xenopus laevis DNA + H2O
5'-phosphooligonucleotides + ?
additional information
?
-
calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
chromatin + H2O
?
-
-
-
-
?
chromatin + H2O
?
recombinant DNase1 degrades chromatin effectively only in cooperation with serine proteases, such as plasmin or thrombin, which remove DNA-bound proteins. Recombinant DNase1/3 degrades chromatin without proteolytic help
-
-
?
chromatin + H2O
?
recombinant DNase1 degrades chromatin effectively only in cooperation with serine proteases, such as plasmin or thrombin, which remove DNA-bound proteins. Recombinant DNase1/3 degrades chromatin without proteolytic help
-
-
?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
lamdaDNA, HindIII
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for native DNA
produces nicks on one strand in preference to scission of both strands, autoretardation causes the continuous formation of products which are poorer substrates than those from which they are derived
?
DNA + H2O
5'-phosphooligonucleotides + ?
DNAse I converts 100% of 1 microg of supercoiled plasmid DNA to relaxed form in 1 h at 37°C. A 10fold higher concentration of DNAse I converts 98% of 1 microg of supercoiled DNA to linear form and a 100fold higher concentration of the nuclease completely digests the DNA into small fragments
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degradation of native DNA is 80%, that for denatured DNA 70%
88% of products are longer than tetranecleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades native DNA 7fold faster than denatured DNA
products have an avarage chain length of 7 residues
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades native DNA 4-5times faster than denatured DNA
mainly nucleotides larger than pentanucleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades native DNA 2times faster than denatured DNA
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades native DNA 2times faster than denatured DNA
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
complementary DNA S2 allowed to hybridize with S1 forms DNA duplexes (the substrate for DNase I) on gold nanoparticles
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for native DNA, A-T rich DNAs more rapidly degraded, no activity on hydroxymethylcytosine-glycosidilic DNA
almost converted into low molecular weight products
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades native DNA 1.5times faster than denatured DNA
half the 5'-termini are deoxythymidinemonophosphate, 90% of the products are larger than pentanucleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
after 60 min of enzymatic digestion, the DNA content reaches 57% of the initial amount and 20% after 105 min, until complete digestion is achieved after 2 h
-
-
?
DNA + H2O
5'-phosphotrinucleotides + ?
-
no preference for any nucleotide
as the main products
?
DNA + H2O
5'-phosphotrinucleotides + ?
-
no preference for any nucleotide
as the main products
?
double-stranded circular DNA + H2O
?
-
-
-
-
?
double-stranded circular DNA + H2O
?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
immobilized DNase I is used in a bioreactor
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I-DNA interaction alters protein secondary structure, with a major reduction in alpha helix and an increase in beta sheet and random structures, and reveals a partial B-to-A DNA conformational change. No DNA digestion upon protein-DNA complexation
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for single-stranded and supercoiled DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cleaves both strands of a double helix at or near the same level, about 400 nucleotides removed at each endonucleolytic scission, causes a "shattering" at the point of cleavage, leading to the libration of small oligonucleotides by an exonucleolytic mode of attack
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
double-strand breaks occure more rapidly in the presence of Ca2+
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I activity was assayed in serum of acute myocardial infarction (AMI). Compared to the control groups the level of DNase I was 2fold higher within 3 hours of the onset of symptoms
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I acts as a transcription activator of the fas gene by direct binding to its promoter
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
the N-terminal fragment of gelsolin disrupts the actin-DNase I interaction in vitro. Colfilin stabilizes the actin-DNase I complex preventing release of DNaseI from actin by gelosin in vitro
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
involved in seed sprouting
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I is involved in chromatin disposal in necrotic tissue
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase Y is involved in chromatin disposal in necrotic tissue
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
low activity on plasmid DNA, high activity on nuclear DNA
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
high activity on plasmid DNA, weak activity on nuclear DNA
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
introduces preferentially breaks on the 5' side of dT
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
functionally active during digestion, participation in the repair of damaged DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
involved in DNA degradation during apoptosis
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
different structure-specific DNA substrates representing stem loop structures with different loop length were used as substrate. Slx1 cuts these substrates at th 3' side of double-strand/single-strand junctions
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
?
double-stranded DNA + H2O
?
-
-
-
-
?
double-stranded linear DNA + H2O
?
-
-
-
-
?
double-stranded linear DNA + H2O
?
-
-
-
-
?
double-stranded linear DNA + H2O
?
-
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
wild-type enzyme and mutant D99A perform double scission on duplex DNA in presence of Mg2+ and Ca2+, not mutant D201A
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
in presence of Mg2+ and Ca2+ under neutral conditions
production of 3'-OH and 5'-phosphate ends
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
predominant single-strand nicking in presence of Mg2+ and Ca2+
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
predominant single-strand nicking in presence of Mg2+ and Ca2+
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
?
-
very low activity
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
only in the presence of both Ca2+ and Mg2+
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
-
-
90% of the products are larger than pentanucleotides
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
-
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
-
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
-
-
-
?
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
-
-
-
?
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
-
-
-
?
plasmid DNA + H2O
?
-
-
-
-
?
plasmid DNA + H2O
?
-
depending on metal ions, duplex DNA is hydrolyzed by DNase I in a single or double scission mode
-
-
?
plasmid DNA + H2O
?
-
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
-
acts more rapidly on circular duplex DNA than on supercoiled DNA
-
?
RNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
RNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
salmon sperm DNA + H2O
?
-
-
-
-
?
salmon sperm DNA + H2O
?
-
only linear, double-stranded DNA is a substrate for SsnA
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
preferred substrate
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
formation of a relaxed circle that subsequently converts to linear DNA if it is nicked on the other strand at the same position
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
formation of a relaxed circle that subsequently converts to linear DNA if it is nicked on the other strand at the same position
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
formation of a relaxed circle that subsequently converts to linear DNA if it is nicked on the other strand at the same position
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
formation of a relaxed circle that subsequently converts to linear DNA if it is nicked on the other strand at the same position
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
Xenopus laevis DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades chromosomal DNA with the characteristic DNA ladders and induces apoptosis of Xenopus embryos
-
-
?
Xenopus laevis DNA + H2O
5'-phosphooligonucleotides + ?
-
degrades chromosomal DNA with the characteristic DNA ladders and induces apoptosis of Xenopus embryos
-
-
?
additional information
?
-
-
OmpA is a potential virulence factor involved in the induction of host cell death. Acinetobacter baumannii can secrete OmpA during colonization and infection. The pathogenic strategy is that OmpA translocates into the nuclei of host cells and degrades chromosomal DNA by DNAse I-like enzymatic activity
-
-
?
additional information
?
-
-
OmpA is a potential virulence factor involved in the induction of host cell death. Acinetobacter baumannii can secrete OmpA during colonization and infection. The pathogenic strategy is that OmpA translocates into the nuclei of host cells and degrades chromosomal DNA by DNAse I-like enzymatic activity
-
-
?
additional information
?
-
-
presence of DNase I hypersensitve sites at the 5' and/or 3' ends of most genes irrespective of their expression levels. Hypersensitive sites occur near cis-regulatory elements in the promoters of these genes and participate in the translational regulation by enhancing the access of chromatin remodeling factors and/or transcription factors to their target sites
-
-
?
additional information
?
-
-
substrate specificity, 5'-AMP, bis(4-nitrophenyl)phosphate, and 4-nitrophenyl phosphate are no substrates, preferential liberation of 5'-deoxy-GMP, no cleavage of C-linkages, (dC)10 is no substrate, no liberation of 5'-deoxy-CMP
-
?
additional information
?
-
-
immunization of healthy rabbits with bovine DNase I produces IgGs with intrinsic DNase and RNase activities
-
-
?
additional information
?
-
-
interaction of DNase I with yeast transfer RNA alters protein secondary structure with major reduction of the alpha-helix, and increases the random coil, beta-anti and turn structures, while tRNA remains in the A-conformation. No digestion of tRNA by DNase I in the protein-tRNA complexes
-
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
genome-wide mapping of DNase I hypersensitive sites in the multicellular model organism Caenorhabditis elegans by a high-resolution tiling array. Distribution of DNase I hypersensitive sites is strongly associated with functional elements in the genome
-
-
?
additional information
?
-
-
genome-wide mapping of DNase I hypersensitive sites in the multicellular model organism Caenorhabditis elegans by a high-resolution tiling array. Distribution of DNase I hypersensitive sites is strongly associated with functional elements in the genome
-
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
no activity with homo-oligomers of dA, dC, dG and annealed homo-oligomers of dA/dT, no activity with RNA
-
?
additional information
?
-
-
enzyme is an integral component of the larval digestive system, enzyme plays an important role in the conversion of the insecticidal crystal protein from Bacillus thuringiensis to the active DNA-free toxin in the larval gut, purified enzyme acts synergistically with the toxin
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
-
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
postnatal spermatogonia show higher sensitivity to DNase-I digestion than isolated Sertoli cells or MSC-1 Sertoli cell line
-
-
?
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
?
additional information
?
-
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
additional information
?
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for single-stranded and supercoiled DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cleaves both strands of a double helix at or near the same level, about 400 nucleotides removed at each endonucleolytic scission, causes a "shattering" at the point of cleavage, leading to the libration of small oligonucleotides by an exonucleolytic mode of attack
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
double-strand breaks occure more rapidly in the presence of Ca2+
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
involved in seed sprouting
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
introduces preferentially breaks on the 5' side of dT
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
functionally active during digestion, participation in the repair of damaged DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
involved in DNA degradation during apoptosis
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
-
?
additional information
?
-
-
OmpA is a potential virulence factor involved in the induction of host cell death. Acinetobacter baumannii can secrete OmpA during colonization and infection. The pathogenic strategy is that OmpA translocates into the nuclei of host cells and degrades chromosomal DNA by DNAse I-like enzymatic activity
-
-
?
additional information
?
-
-
OmpA is a potential virulence factor involved in the induction of host cell death. Acinetobacter baumannii can secrete OmpA during colonization and infection. The pathogenic strategy is that OmpA translocates into the nuclei of host cells and degrades chromosomal DNA by DNAse I-like enzymatic activity
-
-
?
additional information
?
-
-
presence of DNase I hypersensitve sites at the 5' and/or 3' ends of most genes irrespective of their expression levels. Hypersensitive sites occur near cis-regulatory elements in the promoters of these genes and participate in the translational regulation by enhancing the access of chromatin remodeling factors and/or transcription factors to their target sites
-
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
enzyme is an integral component of the larval digestive system, enzyme plays an important role in the conversion of the insecticidal crystal protein from Bacillus thuringiensis to the active DNA-free toxin in the larval gut, purified enzyme acts synergistically with the toxin
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
-
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
?
additional information
?
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
?
additional information
?
-
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cu2+
-
highest activity at 5 mM, but only 40% activtiy compared to Mg2+
KCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
Ba2+
-
-
Ba2+
-
can substitute for Ca2+, but less effective
Ca2+
-
exhibits divalent cation-dependent endonuclease activity
Ca2+
-
2 Ca2+ bound to the enzyme under crystallization conditions
Ca2+
-
activation at 1 mM
Ca2+
-
addition of Ca2+ stabilizes the enzyme, facilitates second cut in double-stranded DNA
Ca2+
-
activation at 0.1 mM
Ca2+
-
resistance to proteolysis conveyed by Ca2+
Ca2+
-
no lag phase in the reaction obtained, if only Ca2+ is present or both Mg2+ and Ca2+ are present, double strand digestion preferred
Ca2+
-
Ca2+-binding causes a conformational change that maintains a more active structure of the enzyme
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
dependent on, D201 and D99 are involved in binding, conformation, protects wild-type and mutant D99A enzymes against trypsin inactivation, not mutant D201A
Ca2+
-
in the absence of Ca2+, but with Mg2+ the DNase cleaved the substrate DNA in a single nicking mode
Ca2+
-
in the presence of Ca2+, native (0.2 U) and inactivated DNase I of 5fold greater enzyme units applied (1.0 U) hydrolyze the Mg2+-DNA substrate forming some linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission, while 0.2 U of 2-nitro-5-thiosulfobenzoic acid-treated DNase I can only cleave the Mg2+-DNA substrate in a single nicking mode
Ca2+
-
two Ca2+ ions that stabilize surface loops as well as an additional metal ion binding site at the active site
Ca2+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Ca2+
essential, binding site characterization
Ca2+
-
activates, transition state metal ions also activate, but are less effective
Ca2+
-
in presence of Ca2+ less sensitive to buffer strength
Ca2+
-
in the presence of 3 mM Mg2+, activation at 2 mM
Ca2+
essential, binding site characterization
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
stabilizing enzyme structure
Ca2+
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Ca2+
-
1 mM optimal concentration
Ca2+
-
highest activity at 5 mM, but only 50% activtiy compared to Mg2+
Ca2+
-
required for stability
Ca2+
essential, binding site characterization
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
activation at 0.1 mM
Ca2+
-
stimulation at 1 mM
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
22% stimulation at 10 mM
Co2+
-
-
Co2+
-
reaction performs mainly double strand scissions, Co2+ is a better activator than other divalent metals
Co2+
-
can substitute for Mg2+, but only 10% efficiency
Co2+
-
absolute requirement for Mn2+ or Mg2+
Co2+
-
activation at 10 mM
Co2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Co2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Co2+
-
22% stimulation at 10 mM
Co2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mg2+
-
exhibits divalent cation-dependent endonuclease activity
Mg2+
-
only single strand cleavage occurs during the lag period of the reaction if only Mg2+ is present
Mg2+
-
enzyme about 99.5% inactive if Ca2+ contamination is reduced to a minimum, must bind to the substrate, whereas Ca2+ must bind to the enzyme
Mg2+
-
presence of Mg2+ alone leads to cutting only one of the two strands
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
in the absence of Ca2+, only native DNase I cleaves the Mg2+-DNA substrate in a single nicking mode with the formation of only the relaxed open-circular DNA, while the 2-nitro-5-thiosulfobenzoic acid-treated DNase I fails to cleave the plasmid DNA substrate
Mg2+
-
in the presence of Mg2+ only, the wild-type cleaves the Mg2+-DNA substrate in a single nicking mode with the formation of only the relaxed open-circular DNA
Mg2+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Mg2+
-
best activator, transition state metal ions also activate, but are less effective
Mg2+
-
absolute requirement for activity, highest activity if both Mg2+ and Ca2+ are present
Mg2+
-
in the presence of 2 mM Ca2+, activation at 3 mM
Mg2+
-
essential cofactor for activity and structural integrity
Mg2+
-
absolute requirement for Mg2+ or Mn2+
Mg2+
half-maximal activation at 4 mM
Mg2+
-
optimal concentration 5 mM
Mg2+
-
activation at 10 mM, 2fold activation, if 1 mM CaCl2 is added
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
required for stabilizing the enzyme structure
Mg2+
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Mg2+
-
dependent on, can be replaced by Mn2+
Mg2+
-
highest activity at 5 mM
Mg2+
-
10 mM optimal concentration
Mg2+
-
DNA fragmentation by digestion with DNase I in the presence of Mg2+ followed by blunting with the Klenow fragment improves the yield of small DNA fragments by 4fold as compared to the reaction with DNase I in the presence of Mn2+. In the case of using Mg2+ as a cofactor, DNase I attacks each strand of dsDNA independently
Mg2+
-
either Mg2+ or Mn2+ is required in addition to Ca2+
Mg2+
-
highest activity at 10 mM, doubled activity upon addition of 1 mM Ca2+
Mg2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
2.0-7.5 mM for DNases A, B or C
Mg2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mg2+
either Mg2+ or Mn2+ is required in addition to Ca2+
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
22% stimualtion at 10 mM
Mg2+
-
highest activity at 2.5 mM
Mg2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mg2+
-
highest activity at 2 mM
Mn2+
-
-
Mn2+
-
can substitute for Mg2+
Mn2+
-
reaction performs mainly double strand scissions
Mn2+
-
most active, faster production of linear form of supercoiled DNA
Mn2+
-
in the presence of Mn2+, native and 2-nitro-5-thiosulfobenzoic acid-treated DNase I of two different enzyme units used are all able to hydrolyze the plasmid DNA substrate in a double scission mode
Mn2+
-
in the presence of Mn2+, the wild-type is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
Mn2+
-
increasing activation up to 30 mM
Mn2+
half-maximal activation at 1 mM
Mn2+
-
activation at 10 mM
Mn2+
-
120% activity of Mg2+ activated enzyme at 10 mM
Mn2+
-
employs more of the cutting mechanism of supercoiled plasmid-DNA
Mn2+
-
dependent on, can be replaced by Mg2+
Mn2+
-
highest activity at 5 mM
Mn2+
-
DNA fragmentation by digestion with DNase I in the presence of Mn2+ followed by blunting with T4 DNA polymerase is 4fold less effective than the reaction with DNase I in the presence of Mg2+. In the reaction with DNase I in the presence of Mn2+, one molecule of DNA is completely cleaved to produce two molecules of DNA
Mn2+
-
either Mg2+ or Mn2+ is required in addition to Ca2+
Mn2+
activity of recombinant DNase1 in the presence of Mn2+ is increased only slightly, whereas recombinant DNase1/3 displays strongly enhanced nucleolysis
Mn2+
-
highest activity at 1 mM, addition of Ca2+ doesn't change activity
Mn2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mn2+
-
less active than Mg2+
Mn2+
-
0.8-2.5 mM for DNases A, B or C
Mn2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mn2+
either Mg2+ or Mn2+ is required in addition to Ca2+
Mn2+
-
22% stimulation at 10 mM
Mn2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mn2+
-
highest activity at 2 mM
NaCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
NaCl
-
activates at concentrations up to 40 mM
NaCl
-
highest activity at 100 mM
Sr2+
-
-
Sr2+
-
can substitute for Ca2+, but less effective
Zn2+
-
-
Zn2+
-
peaked activity at 0.1 mM
Zn2+
-
highest activity at 5 mM, but only 40% activtiy compared to Mg2+
additional information
-
metalloprotein, enzyme has no obligate requirement for metal ions to be active, nor is its activity stimulated by addition of metal ions
additional information
-
metal binding and influence on activity, wild-type and mutant enzymes, overview
additional information
divalent cations are absolutely required for activity
additional information
-
divalent cations are absolutely required for activity
additional information
-
divalent alkaline metal ion requirement
additional information
-
metal-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(4-amidinophenyl)-6-indolecarbamidine
-
significantly inhibits DNase I activity
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-Nitro-5-thiocyanobenzoic acid
2-nitro-5-thiosulfobenzoic acid
5'-deoxy-GMP
-
competitive, product inhibition
Aflatoxin B2a
-
non-competitive inhibitor
Aflatoxin G2
-
non-competitive inhibitor
Aflatoxin G2a
-
non-competitive inhibitor
Aflatoxin M1
-
non-competitive inhibitor
Aprotinin
inhibits DNase1 as a result of plasmin inhibition
aurintricarboxylic acid
i.e ATA, a general inhibitor of nucleases, weak inhibition
Bile acids
-
inhibit the enzyme in concert with cholesterol sulfate
calf spleen inhibitor protein II
-
molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7
-
calf thymus inhibitor protein
-
molecular weight: 49000 Da, maximum stability at pH 6
-
carbodiimide
-
presence of divalent cations slows the rate of inactivation
Cholesterol sulfate
-
from human gastric fluid, the sulfate group and the hydrophobic side chain of cholesterol sulfate are indispensable for the inhibitory effect, irreversible, dependent on bile acids, a ratio of 342:1 of bile acids to cholesterol sulfate is required for complete inhibition
Cu-iodoacetate
-
at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min
DTT
-
80% inhibition at 1 mM
E2-immunity protein
-
complete inhibition of activity on plasmid DNA
-
guanidinium hydrochloride
-
over 80% inhibition at 0.5 M
K+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
methanesulfonylchloride
-
inactivation at pH 5.0
Na+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
oligonucleotides
-
competitive inhibition
plasmin
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
-
protein Im9
-
an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell
-
RNA
-
enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA
Somatostatin
2 enzyme forms: a somatostatin-sensitive and a somatostatin-resistant, controls the enzyme level in the lower gut, in vivo transient down-regulation of gene expression of the sensitive enzyme form
Tris
increasing concentrations of Tris (approximately half activity in the presence of 80 mM Tris) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (no inhibitory influence of Tris)
Urea
-
20% inhibition at 4 M
2-mercaptoethanol
-
70% inhibition at 1 mM
2-mercaptoethanol
-
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
2-mercaptoethanol
slight inhibition
2-mercaptoethanol
-
inhibition after treatment with EGTA
2-mercaptoethanol
-
inhibition, but reversal by addition of 3 mM CaCl2
2-Nitro-5-thiocyanobenzoic acid
-
inhibition at identical rates
2-Nitro-5-thiocyanobenzoic acid
-
inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135
2-Nitro-5-thiocyanobenzoic acid
-
inhibition at identical rates
2-nitro-5-thiosulfobenzoic acid
-
the presence of Ca2+ or Mg2+ at pH 7.5 results in 80% inactivation without fragmentation of the enzyme. In the absence of metal ions it retains 80% of its activity. It binds DNase I through covalent modification, since dialysis and gel filtration can not reverse the inactivation reaction. After dilution into an acid buffer of pH 4.7, the inactivated enzyme regains about 40% of its initial activity. The inhibitor fails to inactivate other enzymes, suggesting that the inhibition is unique to DNase I
2-nitro-5-thiosulfobenzoic acid
-
is a novel inhibitor specific for DNase I
actin
-
inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone
actin
-
40 mM HEPES pH 7.0, 5 mM MgCl2, 1 mM CaCl2
actin
inhibits the DNA-nicking activity of DNAse I/CdtB chimera
actin
inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage
Ca2+
-
inhibitory above 1 mM
Ca2+
-
slight inhibition of mutant D201A
Ca2+
-
80% inhibition at 0.1 mM
Ca2+
-
complete inhibition at 1-10 mM
Cu2+
-
complete inhibition at 1-10 mM
Cu2+
-
complete inhibition
EDTA
-
-
EDTA
-
current peaks of the Fc-oligo-SH-immobilized electrode are relatively stable within error before and after treatment of DNase I solution with EDTA or RNaseA solution, suggesting that this electrode can be used for the detection of DNase I activity specifically
EDTA
complete inhibition at 20 mM
EDTA
complete inhibition at 20 mM
EDTA
10 mM, complete loss of activity
EDTA
-
50% inhibition at 0.3 mM
EDTA
-
complete inhibition at 1 mM
EDTA
-
inhibition observed above 50 microM, complete inhibition at 0.5 mM
EDTA
-
complete ihibition at 1 mM; complete inhibition at 1 mM
EDTA
-
complete inhibition at 10 mM
EDTA
-
complete inhibition at 5 mM
EDTA
-
complete inhibition at 1 mM
EGTA
-
inhibition at 0.01 mM in the presence of 2.5 mM Mg2+
EGTA
complete inhibition at 5 mM
EGTA
-
activity inhibited
EGTA
1 mM, complete loss of activity
EGTA
-
inhibition at 1 mM
EGTA
-
activity inhibited
EGTA
-
complete inhibition at 1 mM
EGTA
-
activity inhibited
EGTA
complete inhibition of the enzyme from serum at 5 mM
EGTA
-
complete ihibition at 1 mM; complete inhibition at 1 mM
EGTA
-
complete inhibition at 10 mM
EGTA
-
complete inhibition at 1 mM
G-actin
-
-
-
G-actin
-
DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity
-
G-actin
-
complete inhibition at 0.05 mg/ml
-
G-actin
slight inhibition
-
G-actin
-
50% inhibition at 0.002 mg/ml
-
G-actin
-
15% inactivation at 0.004 mg
-
G-actin
-
complete inhibition at 0.001 mg
-
G-actin
specific, strong inhibition
-
G-actin
-
heat labile inhibitor of DNase 1, released from white blood cells and platelets. Binds to and almost completely inhibits the nucleolytic activity of DNase 1. Inhibition of DNase 1 by actin (about 95% inhibition at equimolar ratio) requires ATP and leads both to the inhibition of DNase 1 and the depolymerization of the actin
-
G-actin
-
inhibition with actin-gelsolin segment I complex
-
G-actin
-
66% inhibition in an 1:1 molar ratio of DNase I-actin complex
-
gamma-actin
-
-
-
heparin
-
directly inhibits recombinant DNase1/3
heparin
directly inhibits recombinant DNase1/3
Hg2+
-
-
iodoacetate
-
inhibition in the presence of Mn2+ or Ca2+ at pH 7.2
iodoacetate
-
formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
iodoacetate
strong inhibition in presence of Cu2+
iodoacetate
-
complete inhibition
iodoacetate
-
50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min
iodoacetate
-
complete inhibition
KCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
KCl
-
less inhibitory than NaCl
mannitol
-
inhibition of enzyme activity during the entire growth period of seedlings
mannitol
-
induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days
N-bromosuccinimide
-
inactivation by modification at Trp155
N-bromosuccinimide
-
modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
NaCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
NaCl
-
Na-DNA is inhibitory
NaCl
-
inhibitory at concentrations below 100 mM
NaCl
-
10fold lower activity at 150 mM
NaCl
-
50% inhibition at 60 mM, mutated enzyme less sensitive against increased salt concentrations
NaCl
-
decreasing activity with increasing ionic strength
NaCl
-
50% inhibition at 80 mM and pH 5.8 and at 165 mM and pH 7.0
NaCl
-
inhibitory at concentrations above 80 mM
NaCl
increasing concentrations of NaCl (approximately half activity in the presence of 50 mM NaCl) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (approximately half activity in the presence of 150 mM NaCl)
phosphate
-
-
SDS
-
over 80% inhibition at 0.04% w/v
Tris-HCl buffer
-
-
Tris-HCl buffer
-
inhibition at high concentration
Trypsin
-
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
-
Trypsin
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
-
Zn2+
-
-
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
complete inhibition at 1-10 mM
Zn2+
-
inhibition at millimolar concentrations
Zn2+
-
complete inhibition
additional information
-
the phosphate residue is responsible for the inhibitory effect of guanosine 5'-nucleotides
-
additional information
-
no inhibition by sulfatides and membrane lipids, galactose ceramide, no inhibition by steroid sulfates such as estrone sulfate, pregnenolone sulfate, dehydroepiandrosterone sulfate, no inhibition by DMSO, Tween 20, sodium cholate, and sodium taurocholate
-
additional information
-
thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I
-
additional information
-
DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
-
additional information
no inhibition by G-actin
-
additional information
-
no inhibition by G-actin; no inhibition by G-actin
-
additional information
no inhibition by G-actin; no inhibition by G-actin
-
additional information
resistant to trypsin inactivation in absence of Ca2+
-
additional information
-
resistant to trypsin inactivation in absence of Ca2+
-
additional information
is resistant to trypsin
-
additional information
-
is resistant to trypsin
-
additional information
G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
-
additional information
-
G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
-
additional information
-
efficiency of cleavage of DNA duplex on gold nanoparticles by DNase I is about 82% whereas the cleavage efficiency in solution phase at the same conditions is nearly 100%. Cleavage efficiencies using Pb2+-mediated DNA enzyme on gold nanoparticles and in solution phase are about 55% and 95%, respectively
-
additional information
no inhibition by G-actin
-
additional information
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
-
additional information
-
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
-
additional information
no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
-
additional information
-
no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
-
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D44H
shifts the pH optimum from pH 8.0 to lower values of pH 6.5-7.0, 70% reduced activity compared to thw wild-type enzyme
E190S
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
M118R
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
M236Q
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
Q134L
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
C101A
-
no thioredoxin-like activity as observed for the wild-type
D201A
-
site-directed mutagenesis, exchange of one of 2 Ca2+-binding site residues, 2-3fold increased Km and decrased Vmax compared to the wild-type enzyme, no double-scission ability, no protection by Ca2+ against trypsin inactivation
D99A
-
site-directed mutagenesis, exchange of one of 2 Ca2+-binding site residues, 2-3fold increased Km and unaltered Vmax compared to the wild-type enzyme
Delta1-10
inactive enzyme
Delta1-11
inactive enzyme
Delta251-260
inactive enzyme
Delta255-260
inactive enzyme
Delta256-260
inactive enzyme
Delta257-260
inactive enzyme
Delta258-260
inactive enzyme
Delta259-260
inactive enzyme
E102G/S103P
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 4fold increase in thioredoxin-like activity
E102P/S103G
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 4fold increase in thioredoxin-like activity
F192C/A217C
-
active, more heat stable compared to wild-type
G100K/E102P/S103G/G105W
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity about half of wild-type, 4.5fold increase in thioredoxin-like activity
G100K/G105W
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I and thioredoxin-like activity similar to wild-type
G100W/E102/G/S103P/G105K
mutation in non-essential disulfide motif CESC that exhibits thioredoxn-like activity. DNase I activity similar to wild-type, 6fold increase in thioredoxin-like activity
H44A
-
DNase I activity is similar to that of the wild-type
H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
N106Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type
N18Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type
N18Q/N106Q
-
enzyme activity is lower than those of the single mutants, is unstable to heat, trypsin resistance decreases in a time-dependent manner
S43A
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
S43A/H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
S43C
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14A
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14A/H44D
-
inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode
T14A/S43A
-
in the presence of Mn2+, though being less active than the wild-type, can still cleave the plasmid DNA in the double scission mode
T14A/S43A/H44D
-
inactive
T14A/S43C
-
DNase I activity is similar to that of the wild-type
T14C
-
in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
T14C/H44D
-
significant increase in DNase I activity
T14C/S43A
-
DNase I activity is similar to that of the wild-type
T14C/S43A/H44D
-
significant increase in DNase I activity
G52E
-
the mutation reduces the diphtheria toxin's toxicity
F114A
site-directed mutagenesis, change to human enzyme sequence type, complete abolished affinity for actin
V68I
site-directed mutagenesis, change to human enzyme sequence type, 90% reduced affinity for actin
F114A
-
protein is not expressed
I67V
-
inhibition by gamma-actin
N106Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q/N106Q
enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin
F114A
-
protein is not expressed
V67I
-
no inhibition by g-actin
A224del
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.69, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.52
A224P
also naturally occuring mutation, ID number (NCBI database): rs8176939, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.23, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.36
C209Y
also naturally occuring mutation, ID number (NCBI database): rs8176939, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.24, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.23
E128W
-
point mutation by sequential PCR steps, altered secondary structure, 80% reduced activity compared to the wild-type enzyme
E13D
also naturally occuring mutation, ID number (NCBI database): rs34907394, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.35, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
G105A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.05, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.68
G105K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 3.27, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.64
G105R
also naturally occuring mutation, ID number (NCBI database): rs176919, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 3.22, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.63
G240D
also naturally occuring mutation, ID number (NCBI database): rs8176924, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.46, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.56
G55R
adds DNA contact residues, increases the specific activity of the hybrid protein
H84C
-
point mutation by sequential PCR steps, very slightly increased activity
H84W
-
point mutation by sequential PCR steps, altered secondary structure, very slightly increased activity
K18Term
termination codon at triplet 18, also naturally occuring mutation, no activity detected
L186L
also naturally occuring mutation, ID number (NCBI database): rs8176920, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.8, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
L62E
added a metal ion-binding residue, increases the specific activity of the hybrid protein
N106Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q/N106Q
enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin
N7A
complete loss of activity
N7S
complete loss of activity
P132A
also naturally occuring mutation, ID number (NCBI database): rs1799891, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 2.10, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.93
P197A
also naturally occuring mutation, ID number (NCBI database): rs34186031
P197S
also naturally occuring mutation, ID number (NCBI database): rs34186031, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 2.03, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.75
Q222E
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.26, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
Q222K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.71, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
Q222L
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.17, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.81
Q244R
-
polymorphism of DNase 1, is associated with systemic lupus erythematosus susceptibility but is not correlated with DNase 1 activity
Q35A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.39, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.55
Q35E
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.79, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.53
Q35H
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.60, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.60
Q38H
naturally occuring mutation, ID number (NCBI database): rs4554238
Q9E
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) about 0.35
Q9R/E13R/N74K
-
most hyperactive variant, 35fold more active than wild type enzyme
R100E
adds a residue that hydrogen bonds to the catalytic H160 in DNAse I, increases the specific activity of the hybrid protein
R185C
naturally occuring mutation
R21S
also naturally occuring mutation, ID number (NCBI database): rs8176927, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.75, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.96
R85A
no activity detected
R85G
also naturally occuring mutation, ID number (NCBI database): rs8176928, no activity detected
R85K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.87, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.56
S99Y
adds DNA contact residues, increases the specific activity of the hybrid protein
V134R
adds DNA contact residues, increases the specific activity of the hybrid protein
V82M
also naturally occuring mutation
V89A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.21, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.53
V89L
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.55, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.33
V89M
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.24, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.20
V92M
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) about 1.0
Y95S
also naturally occuring mutation, ID number (NCBI database): rs34923865, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.32, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.67
A144Y
mutant with extremely reduced actin binding capacity. Induction of apoptosis or necrosis by staurosporine or oxidative stress results in faster chromatin fragmentation in mutant cells. Inclusion of actin under these conditions inhibits chromatin degradation in wild-type, but not in mutant
C151A
-
activity similar to wild type
D81N
-
50% activity compared to wild type
H46A
-
activity similar to wild type
H371A
-
site-directed mutagenesis, exchange of a well-conserved His residue, loss of most of the nuclease activity, stilla ctive in DNA-binding
N110S
site-directed mutagenesis, exchange mutant has the same sequence as the rat and bovine enzymes and becomes insensitive to low pH like the rat and bovine enzymes
S114A
inhibition by gamma-actin
S114F
no inhibition by gamma-actin
T178S
site-directed mutagenesis, similar to the wild-type enzyme in pH-sensitivity
F114A
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protein is not expressed
Q222R
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single nucleotide polymorphism in exon 8, is associated with several diseases. Gene DNASE1-1 is more common in Africans and gene DNASE1-2 is more common in Caucasians. Optimum pH for the DNase I type-1 enzyme is 6.75, while that for the type-2 enzyme is 6.5. Activity of the DNase I type-2 enzyme is 1.33times higher than that of the type-1 enzyme. The type-1 enzyme is heat labile when compared to the type-2 enzyme
Q222R
also naturally occuring mutation, ID number (NCBI database): rs1053874, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.48, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.2
additional information
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analysis of genetic polymorphisms and correlation between genotype and its activity. Study on allele frequencies in DNase1 polymorphisms and polymorphisms in intron 4, designated HumDN1
additional information
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an A to G transversion in exon 2 at position 172 of the coding sequence in two female systemic lupus erythematosus patients. The mutations result in a replacement of lysine (AAG) with a stop signal (TAG) at residue 5, which results in an inactivated DNAse 1. The two patients have substantially lower levels of DNase 1 activity in the sera than other systemic lupus erythematosus patients without the DNase 1 mutation or healthy controls. Titer of IgG against nucleosomal antigens is 7-8 times higher in patients with the DNase 1 mutation than in other systemic lupus erythematosus patients and 70-80 times higher in the patients with the mutation than in normal controls
additional information
DNase1 knockout mice, contain residual nuclease activity. Addition of aprotinin or plasminogen activator inhibitor 1 to the sera of DNase1 KO mice completes chromatolysis to mononucleosomes and even to oligonucleotides
additional information
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DNase1 knockout mice, contain residual nuclease activity. Addition of aprotinin or plasminogen activator inhibitor 1 to the sera of DNase1 KO mice completes chromatolysis to mononucleosomes and even to oligonucleotides
additional information
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young DNase+/- and DNase-/- mice are healthy, but at the age of 6-8 months several animals show symptoms of disease and die. DNase+/- and DNase-/- animals reveal the presence of ANAs and signs of glomerulonephritis, suggesting a correlation between the activity of DNase1 and a systemic lupus erythematosus-like disease. The prevalence of ANAs and glomerulonephritis is higher in female mice than in males and higher in DNase-/- animals than in DNase+/- mice. Female DNase 1-deficient mice contain antibodies against dsDNA
additional information
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DNase1 knockout mice, contain residual nuclease activity. Addition of aprotinin or plasminogen activator inhibitor 1 to the sera of DNase1 KO mice completes chromatolysis to mononucleosomes and even to oligonucleotides
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additional information
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construction of mutants with deletions at the N- and/or the C-terminus, mutants reveal the localisation fo activities within the enzyme sequence, overview
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additional information
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the gonadotrophin releasing hormone cGnRH II is pro-apoptotic to pyriform cells, exerting its effects by activating an alternative cell death pathway, probably involving calcium as first messenger and DNase I as first executioner
analysis
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study of chromatin structure, visualizing cellular microfilaments by DNase I-actin interaction
analysis
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preparation of substrates for the nick translation reaction, production of random DNA fragments, analysis of DNA-protein complexes
analysis
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enzymatic activity assay for determination of enzyme stability. Method bases on a colorimetric endpoint activity assay using degradation of a DNA/methyl green complex and is feasible on an automated analyzer system within a rather short time
analysis
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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. Urine samples give an activity of 1.49 U/ml, blood plasma of 0.36 U/ml
analysis
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use of DNase I pre-treatment significantly increases the reliability and sensitivity of immunodetection of CIP/KIP cyclin-dependent kinase inhibitors. Applications in developmental neurobiology and cancer diagnosis
analysis
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construction of a sensor electrode carrying Fc-oligo-SH to achieve an electrochemical DNase I assay. Under the optimum conditions of DNase I digestion at 37°C for 30 min, a quantitative analysis can be achieved in the range of 0.0001-0.01 units/microl of DNase I
analysis
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graphene-based real-time fluorescent assay of deoxyribonuclease I activity and inhibition. The system is composed of graphene oxide and a fluorescent dye fluorescein amidite-labeled dsDNA substrate. At first, the fluorescence of the substrate is quenched upon addition of graphene oxide. When nuclease is added to the mixture of dsDNA and graphene oxide, hydrolysis of dsDNA is initiated and small DNA fragments are produced. The short fluorescein amidite-linked DNA fragments are released, and the fluorescence gets a restoration. DNase I activity can be quantitatively analyzed by the velocity of the enzymatic reaction, and 1.75 U/ml DNase I can be detected
analysis
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use of fluorescent DNA-templated gold/silver nanoclusters as a probe for sensitive detection of deoxyribonuclease I. The procedure is based on quenching fluorescence of DNA-templated gold/silver nanoclusters by DNase I digestion of the DNA 5'-CCCTTAATCCCC-3' template. This decrease in fluorescence intensity permits sensitive detection of DNase I in a linear range of 0.013-60 microg per ml, with a detection limit of 3 ng per ml at a signal-to-noise ratio of 3. The practicality of this probe for detection of DNase I in human serum and saliva samples has been validated
degradation
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treatment of established 72 h biofilms with 100 microg per ml of DNase for 24 h induces incomplete Listeria monocytogenes biofilm dispersal, with about 25% biofilm remaining compared to control. Addition of proteinase K completely inhibits biofilm formation, and 72 h biofilms including those grown under stimulatory conditions are completely dispersed with 100 microg per ml proteinase K
degradation
the degradation of extracellular DNA with enzymes such as DNase I is a rapid method to remove Campylobacter jejuni biofilms, and is likely to potentiate the activity of antimicrobial treatments and thus synergistically aid disinfection treatments
diagnostics
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decrease in DNase activity in blood correlates with chronic pancreatitis, stomach cancer and glomerulonephritis
diagnostics
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increase in DNase activity in blood was observed during development of breast cancer
diagnostics
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increased DNase I activity in patient serum could be used as diagnostic marker for the early detection of acute myocardial infarction
diagnostics
cell-free DNA circulating in blood cannot be a reliable marker of increased cell death during pregnancy. Thus, assessment of the level of cell death during pregnancy should be done by simultaneous analysis of cell-free DNA level and DNase I activity
medicine
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inhibition of viral synthesis by DNase I in cell cultures
medicine
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inhaled DNase I into the airways reduces viscoelasticity of sputum, improves lung function of cystic fibrosis patients
medicine
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improvement of respiratory tract functioning in patients with cystic fibrosis
medicine
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analysis of genetic polymorphisms and correlation between genotype and its activity. Study on allele frequencies in DNase1 polymorphisms and polymorphisms in intron 4, designated HumDN1
medicine
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enzymatic activity assay for determination of enzyme stability. Method bases on a colorimetric endpoint activity assay using degradation of a DNA/methyl green complex and is feasible on an automated analyzer system within a rather short time. Application of method proves the reliability of enzyme during aerosolization with inhalation devices
medicine
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use of DNase I pre-treatment significantly increases the reliability and sensitivity of immunodetection of CIP/KIP cyclin-dependent kinase inhibitors. Applications in developmental neurobiology and cancer diagnosis
medicine
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DNase 1 activity is important to prevent immune stimulation and therefore its reduction or loss may result in a high risk to produce ANAs thus contributing to a potential prerequisite to develop a systemic lupus erythematosus-like disease. Survival of DNase 1-treated mice is longer that non-treated mice
medicine
DNAse I/cdtB gene chimera has therapeutic applications for inhibiting the proliferation of cancer cells
medicine
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early use of dornase alpha provides nutritional benefits, thus is significantly associated with a higher body mass index percentile over time. Children who received dornase alpha before age two have an average body mass index percentile that is 10.2 percentiles greater than children who have not
medicine
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extracellular DNase 1 is implicated in the chromatin breakdown of necrotic cells in vitro. Connection between DNase 1 activity and the development of human systemic lupus erythematosus. Systemic lupus erythematosus patients have lower DNase 1 activity than patients with rheumatoid arthritis and scleroderma. Usage of DNase 1 as a therapeutic agent in systemic lupus erythematosus
medicine
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single nucleotide polymorphism in exon 8, is associated with several diseases
medicine
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usage of DNase 1 as a therapeutic agent in systemic lupus erythematosus
medicine
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DNase I activity activity in systemic Lupus erythematosus patients is lower than in healthy controls. DNase I activity is in positive correlation with systemic Lupus erythematosus activity index-2K, levels of antinuclear, anti-dsDNA, anti-nucleosome and anti-histone antibodies and in negative correlation with complement component C3 concentration. An increase of DNase I activity characterizes relapse in most SLE patients, although it does not reach the levels of healthy individuals
medicine
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patients with type 2 diabetes show a significant elevation of DNase I activity in serum, and increase in DNase I expression is observed in the pancreas of diabetic persons
medicine
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rats with diabetes induced by streptozotocin injection and high fat diet show a significant elevation of DNase I activity in serum, and increase in DNase I expression is observed in the pancreas of diabetic rats. High glucose induces both DNase I and caspase-3 expression and at the same time increases apoptosis rate of INS-1 cells
medicine
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treatment of established 72 h biofilms with 100 microg per ml of DNase for 24 h induces incomplete Listeria monocytogenes biofilm dispersal, with about 25% biofilm remaining compared to control. Addition of proteinase K completely inhibits biofilm formation, and 72 h biofilms including those grown under stimulatory conditions are completely dispersed with 100 microg per ml proteinase K
molecular biology
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a DNase bioreactor can be used to remove DNA from RNA samples prior to reverse transcription followed by PCR
molecular biology
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DNase-I hypersensitive sites may constitute a molecular marker to identify alleles and subsequently acquire the appropriate methylation imprint. This molecular identifier may be present or absent for a specific gene according to the sex of the gamete
pharmacology
bacterial biofilm infections are highly prevalent and are a significant cause of morbidity and mortality. With the rapid emergence of resistance to conventional antibiotic therapies and intrinsic biofilm resistance to antibiotic penetration, Pseudomonas aeruginosa biofilm treatment options are limited. Consequently, novel anti-biofilm strategies to prevent biofilm formation and remove existing biofilms are being sought. Glutathione enhances antibiotic efficiency and effectiveness of DNase I in disrupting Pseudomonas aeruginosa biofilms while also inhibiting pyocyanin activity, Thus facilitating restoration of cell enzymatic activity, confluence and viability
pharmacology
DNase I has a cytotoxic effect on B16 melanoma cells. DNase I inhibits the migratory activity of melanoma cells in vitro, causing a decrease in the distance of cell front migration and in the area of scratch healing 48 h after the enzyme addition, as well as reducing the rate of cell migration. In mice with B16 metastatic melanoma, intramuscular administration of DNase I in the dose range of 0.12-1.20 mg/kg results in a two- to threefold decrease in the number of surface lung metastases and causes nonspecific antigenic immune stimulation. The pronounced antimetastatic effect of DNase I observed in the in vivo model of metastatic B16 melanoma may be due to both the inhibitory activity of the enzyme on the molecular level (i.e., exDNA degradation) and to its systemic effect on the immune system