Information on EC 3.1.21.1 - deoxyribonuclease I

650325, 653799

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for single-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

Glu128 is required for activity, contains conserved sequence LEDFXR, endonuclease activity

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

conserved residues Glu79, His135, Asp213, and His 252 are involved in catalysis

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

Asp44 is involved in catalysis, while Met118, Gln134, Glu190, and Met236 are not

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for double-stranded DNA

Takifugu rubripes

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

catalytic mechanism, the N-terminal 62 residues and the C-terminal 39 residues have important roles in 3'-exonuclease activity, residues 63-453 are responsible for 5'- and 3'-exonuclease activities, residues 24-492 form a region with 7fold higher catalytic activity than the intact enzyme

endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products

preference for single-stranded DNA and 3'AMP, guanylic acid preferential endo-exonuclease, mode of action, overview

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REACTION TYPE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

hydrolysis of phosphoric ester

31 entries

hydrolysis of phosphoric ester

650325, 653799

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

664587

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

663963, 665221

hydrolysis of phosphoric ester

666887, 664843

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

664612

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

664029

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

665821

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

hydrolysis of phosphoric ester

Triakis scyllium

Q5R2I3

hydrolysis of phosphoric ester

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CAS REGISTRY NUMBER

COMMENTARY

9003-98-9

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

Reversibility
r=reversible
ir=irreversible
?=not specified

(pC)10 + H2O

Substrates: -
Products: -

190mer DNA fragment + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

3'AMP + H2O

adenosine + phosphate

Substrates: phosphomonoesterase activity
Products: -

calf thymus DNA + H2O

5'-phosphooligonucleotides + ?

chromatin + H2O

circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

cosmid DNA + H2O

Substrates: -
Products: -

crab d(A-T) polymer + H2O

5'-hexanucleotides + ?

Substrates: unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure
Products: enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage

d(pA)10 + H2O

Substrates: -
Products: -

d(pApCpTpApCpApGpTpCpTpApCpA) + H2O

Substrates: -
Products: -

d(pGpGpCpApCpTpTpApC) + H2O

Substrates: -
Products: -

d(pT)10 + H2O

Substrates: -
Products: -

d(pTpApGpApApGpApTpCpApApA) + H2O

Substrates: -
Products: -

d-ApApTp + H2O

pTp + d-ApA

Substrates: -
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

DNA + H2O

5'-phosphodinucleotides + 5'-phosphooligonucleotides

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

18 entries

DNA + H2O

5'-phosphotrinucleotides + ?

double-stranded circular DNA + H2O

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

53 entries

double-stranded DNA + H2O

double-stranded linear DNA + H2O

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

dsDNA + H2O

Fc-oligo-SH + H2O

Substrates: 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
Products: -

H2AL2 nucleosome core particle + H2O

710137

Substrates: 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
Products: -

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

HMIP-2 + H2O

707845

Substrates: identifies three tissue-specific DNase I hypersensitive sites in the core intergenic interval
Products: -

lambda phage DNA + H2O

Substrates: -
Products: -

linearized plasmid-DNA + H2O

5'-phosphooligonucleotides + H2O

NO2-Ph-pdTp-NO2-Ph + H2O

p-nitrophenol + ?

Substrates: -
Products: -

NO2-Ph-pdTp-NO2Ph + H2O

p-nitrophenol + NO2-Ph-pdT-3'-phosphate

Substrates: rapidly hydrolyzed at a single bond
Products: -

p-nitrophenyl phenylphosphonate + H2O

p-nitrophenol + phenylphosphoric acid

134197, 134202

Substrates: -
Products: -

phage M13 DNA + H2O

Substrates: endolytically cleavage generating single base nicks
Products: -

plasmid DNA + H2O

poly(dA) + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

poly(dT) + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

pUC18 DNA + H2O

Substrates: -
Products: -

relaxed circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

RNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

RNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

RNA + H2O

Substrates: low activity
Products: -

salmon sperm DNA + H2O

5'-phosphooligonucleotides + ?

696291

Substrates: -
Products: -

salmon sperm DNA + H2O

salmon testis DNA + H2O

5'-phosphooligonucleotides + ?

single-stranded circular DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for single-stranded regions
Products: -

single-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

single-stranded DNA + H2O

Substrates: -
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

ssDNA + H2O

Substrates: -
Products: -

supercoiled DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: in presence of Mg2+ and Ca2+ under neutral conditions
Products: production of 3'-OH and 5'-phosphate ends

supercoiled plasmid DNA + H2O

linear DNA + ?

8 entries

supercoiled pUC18 DNA + H2O

Substrates: endolytically cleavage generating single base nicks
Products: -

Xenopus laevis DNA + H2O

5'-phosphooligonucleotides + ?

additional information

26 entries

calf thymus DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

calf thymus DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

chromatin + H2O

Substrates: -
Products: -

chromatin + H2O

Substrates: 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
Products: -

chromatin + H2O

circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: lamdaDNA, HindIII
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

134208, 134215, 134227, 134234, 134237

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for native DNA
Products: 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 + ?

Substrates: 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
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: degradation of native DNA is 80%, that for denatured DNA 70%
Products: 88% of products are longer than tetranecleotides

DNA + H2O

5'-phosphooligonucleotides + ?

133978

Substrates: degrades native DNA 7fold faster than denatured DNA
Products: products have an avarage chain length of 7 residues

DNA + H2O

5'-phosphooligonucleotides + ?

134225, 134230

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: degrades native DNA 4-5times faster than denatured DNA
Products: mainly nucleotides larger than pentanucleotides

DNA + H2O

5'-phosphooligonucleotides + ?

134207, 134214

Substrates: degrades native DNA 2times faster than denatured DNA
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

701234

Substrates: complementary DNA S2 allowed to hybridize with S1 forms DNA duplexes (the substrate for DNase I) on gold nanoparticles
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for native DNA, A-T rich DNAs more rapidly degraded, no activity on hydroxymethylcytosine-glycosidilic DNA
Products: almost converted into low molecular weight products

DNA + H2O

5'-phosphooligonucleotides + ?

134203, 134212, 134215

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: degrades native DNA 1.5times faster than denatured DNA
Products: half the 5'-termini are deoxythymidinemonophosphate, 90% of the products are larger than pentanucleotides

DNA + H2O

5'-phosphooligonucleotides + ?

134211

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

DNA + H2O

5'-phosphooligonucleotides + ?

Xanthisma gracile

701148

Substrates: 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
Products: -

DNA + H2O

5'-phosphotrinucleotides + ?

Substrates: no preference for any nucleotide
Products: as the main products

DNA + H2O

5'-phosphotrinucleotides + ?

Substrates: no preference for any nucleotide
Products: as the main products

double-stranded circular DNA + H2O

Substrates: -
Products: -

double-stranded circular DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134199, 134213, 134221, 134227, 134234, 134237

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: 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 + ?

Substrates: major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
Products: 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 + ?

Substrates: 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+
Products: 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 + ?

Substrates: cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134210

Substrates: hydrolysis of both double- and single-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

666411

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

665821

Substrates: immobilized DNase I is used in a bioreactor
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

696064

Substrates: 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
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Caenorhabditis elegans

Caenorhabditis elegans N2

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for single-stranded and supercoiled DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

133978

Substrates: 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
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

664587, 664707

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134200, 134207, 134214, 134228

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: double-strand breaks occure more rapidly in the presence of Ca2+

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: hydrolysis of both double- and single-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

666887

Substrates: 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
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

664843

Substrates: DNase I acts as a transcription activator of the fas gene by direct binding to its promoter
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

664612

Substrates: 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
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

664146, 695549, 695970

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: involved in seed sprouting
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: low activity on plasmid DNA, high activity on nuclear DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

665221

Substrates: DNase I is involved in chromatin disposal in necrotic tissue
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

665221

Substrates: DNase Y is involved in chromatin disposal in necrotic tissue
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: high activity on plasmid DNA, weak activity on nuclear DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134200, 134212

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: introduces preferentially breaks on the 5' side of dT
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: functionally active during digestion, participation in the repair of damaged DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: involved in DNA degradation during apoptosis
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: 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
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134211, 664154

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Triakis scyllium

Q5R2I3

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded linear DNA + H2O

Substrates: -
Products: -

double-stranded linear DNA + H2O

Substrates: -
Products: -

double-stranded linear DNA + H2O

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: wild-type enzyme and mutant D99A perform double scission on duplex DNA in presence of Mg2+ and Ca2+, not mutant D201A
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: in presence of Mg2+ and Ca2+ under neutral conditions
Products: production of 3'-OH and 5'-phosphate ends

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: predominant single-strand nicking in presence of Mg2+ and Ca2+
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: predominant single-strand nicking in presence of Mg2+ and Ca2+
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

Substrates: very low activity
Products: -

dsDNA + H2O

Substrates: -
Products: -

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

134207, 134214, 134230

Substrates: -
Products: -

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: only in the presence of both Ca2+ and Mg2+

heat-denatured DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: 90% of the products are larger than pentanucleotides

linearized plasmid-DNA + H2O

5'-phosphooligonucleotides + H2O

Substrates: -
Products: -

linearized plasmid-DNA + H2O

5'-phosphooligonucleotides + H2O

134197, 134202

Substrates: -
Products: -

plasmid DNA + H2O

Substrates: -
Products: -

plasmid DNA + H2O

Substrates: depending on metal ions, duplex DNA is hydrolyzed by DNase I in a single or double scission mode
Products: -

plasmid DNA + H2O

Substrates: -
Products: -

plasmid DNA + H2O

Substrates: -
Products: -

relaxed circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

relaxed circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

relaxed circular plasmid DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: acts more rapidly on circular duplex DNA than on supercoiled DNA
Products: -

RNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

RNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Medicago sativa

Substrates: -
Products: -

salmon sperm DNA + H2O

Substrates: -
Products: -

salmon sperm DNA + H2O

Substrates: only linear, double-stranded DNA is a substrate for SsnA
Products: -

salmon testis DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

salmon testis DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

salmon testis DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: preferred substrate
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Medicago sativa

Substrates: -
Products: -

supercoiled plasmid DNA + H2O

linear DNA + ?

Substrates: -
Products: superhelical form converted to circular-relaxed and linear forms

supercoiled plasmid DNA + H2O

linear DNA + ?

Substrates: -
Products: superhelical form converted to circular-relaxed and linear forms

supercoiled plasmid DNA + H2O

linear DNA + ?

Substrates: -
Products: 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 + ?

Substrates: -
Products: 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 + ?

Substrates: -
Products: superhelical form converted to circular-relaxed and linear forms

supercoiled plasmid DNA + H2O

linear DNA + ?

Substrates: -
Products: -

supercoiled plasmid DNA + H2O

linear DNA + ?

134197, 134202

Substrates: -
Products: 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 + ?

134212, 134216

Substrates: -
Products: superhelical form converted to circular-relaxed and linear forms

Xenopus laevis DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: degrades chromosomal DNA with the characteristic DNA ladders and induces apoptosis of Xenopus embryos
Products: -

Xenopus laevis DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: degrades chromosomal DNA with the characteristic DNA ladders and induces apoptosis of Xenopus embryos
Products: -

additional information

Substrates: 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
Products: -

additional information

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Arabidopsis thaliana

682348

Substrates: 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
Products: -

additional information

Substrates: 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
Products: -

additional information

699637

Substrates: immunization of healthy rabbits with bovine DNase I produces IgGs with intrinsic DNase and RNase activities
Products: -

additional information

700518

Substrates: 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
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Caenorhabditis elegans

Caenorhabditis elegans N2

Substrates: 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
Products: -

additional information

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: no activity with homo-oligomers of dA, dC, dG and annealed homo-oligomers of dA/dT, no activity with RNA
Products: -

additional information

Substrates: 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
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: DNase I is not involved in aopoptosis, but DNase lambda is
Products: -

additional information

Substrates: DNase I is not involved in aopoptosis, but DNase lambda is
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

698336

Substrates: postnatal spermatogonia show higher sensitivity to DNase-I digestion than isolated Sertoli cells or MSC-1 Sertoli cell line
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

Substrates: 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
Products: -

additional information

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

DNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

34 entries

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

dsDNA + H2O

Substrates: -
Products: -

ssDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

additional information

19 entries

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134199, 134213, 134221, 134227, 134234, 134237

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134210

Substrates: hydrolysis of both double- and single-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

666411

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for single-stranded and supercoiled DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

133978

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

664587

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134200, 134207, 134214, 134228

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: double-strand breaks occure more rapidly in the presence of Ca2+

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: hydrolysis of both double- and single-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: involved in seed sprouting
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134200, 134212

Substrates: -
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: preference for double-stranded DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: introduces preferentially breaks on the 5' side of dT
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: functionally active during digestion, participation in the repair of damaged DNA
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

Substrates: involved in DNA degradation during apoptosis
Products: -

double-stranded DNA + H2O

5'-phosphooligonucleotides + ?

134211, 664154

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

dsDNA + H2O

5'-phosphodinucleotide + 5'-phosphooligonucleotide

Substrates: -
Products: -

additional information

additional information

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Arabidopsis thaliana

682348

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: DNase I is not involved in aopoptosis, but DNase lambda is
Products: -

additional information

Substrates: DNase I is not involved in aopoptosis, but DNase lambda is
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

Substrates: DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
Products: -

additional information

additional information

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ba2+

Ca2+

Cd2+

Co2+

Cu2+

highest activity at 5 mM, but only 40% activtiy compared to Mg2+

KCl

stimulating between 25 and 50 mM, inhibitory above 50 mM

Mg2+

MgCl2

Mn2+

NaCl

Ni2+

Sr2+

Zn2+

additional information

Ba2+

Ba2+

can substitute for Ca2+, but less effective

Ca2+

exhibits divalent cation-dependent endonuclease activity

Ca2+

activates

Ca2+

essential, binding site characterization

Ca2+

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

134227

Ca2+

activation synergistic with Mg2+

134215, 134220

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+

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+

716661

Ca2+

essential, binding site characterization

Ca2+

activates

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+

activates

Ca2+

essential, binding site characterization

Ca2+

activates

Ca2+

Ca2+

activation synergistic with Mg2+

134197, 134202, 134225, 134228, 134230

Ca2+

stabilizing enzyme structure

Ca2+

Ca2+

highest activity at 5 mM, but only 50% activtiy compared to Mg2+

Ca2+

1 mM optimal concentration

Ca2+

activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism

Ca2+

required for stability

Ca2+

Ca2+

Ca2+

required

Ca2+

activates

Ca2+

required

Ca2+

activates

Ca2+

activation synergistic with Mg2+

Ca2+

Ca2+

required

Ca2+

required

Ca2+

Ca2+

activation at 0.1 mM

Ca2+

stimulation at 1 mM

Ca2+

activation synergistic with Mg2+

Ca2+

22% stimulation at 10 mM

Ca2+

required

Ca2+

stimulation

Ca2+

required

Ca2+

or Mg2+, required

Ca2+

activates

Ca2+

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+

Co2+

absolute requirement for Mn2+ or Mg2+

Co2+

Co2+

activation at 10 mM

Co2+

activates

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+

activates

Mg2+

Mg2+

2.0-7.5 mM for DNases A, B or C

Mg2+

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+

5% activation

Mg2+

presence of Mg2+ alone leads to cutting only one of the two strands

Mg2+

activation synergistic with Ca2+

Mg2+

dependent on

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+

required

Mg2+

Mg2+

activates

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+

activates

Mg2+

essential cofactor for activity and structural integrity

Mg2+

Mg2+

activates

Mg2+

absolute requirement for Mg2+ or Mn2+

Mg2+

Mg2+

half-maximal activation at 4 mM

Mg2+

Mg2+

optimal concentration 5 mM

Mg2+

activation at 10 mM, 2fold activation, if 1 mM CaCl2 is added

Mg2+

activation synergistic with Ca2+

134197, 134202, 134225, 134228, 134230

Mg2+

required for stabilizing the enzyme structure

Mg2+

Mg2+

dependent on, can be replaced by Mn2+

Mg2+

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

695549

Mg2+

activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism

Mg2+

Mg2+

either Mg2+ or Mn2+ is required in addition to Ca2+

Mg2+

Mg2+

highest activity at 10 mM, doubled activity upon addition of 1 mM Ca2+

Mg2+

activates

Mg2+

5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required

Mg2+

activates

Mg2+

activation synergistic with Ca2+

Mg2+

Mg2+

5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required

Mg2+

either Mg2+ or Mn2+ is required in addition to Ca2+

Mg2+

Mg2+

5% activation

Mg2+

activation synergistic with Ca2+

134215, 134216

Mg2+

22% stimualtion at 10 mM

Mg2+

highest activity at 2.5 mM

Mg2+

required

Mg2+

Mg2+

5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required

Mg2+

or Ca2+, required

Mg2+

highest activity at 2 mM

Mg2+

Takifugu rubripes

activates

Mg2+

Mn2+

0.8-2.5 mM for DNases A, B or C

Mn2+

134208, 134234, 134236

Mn2+

reaction performs mainly double strand scissions

Mn2+

most active, faster production of linear form of supercoiled DNA

Mn2+

can substitute for Mg2+

Mn2+

activates

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+

activates

Mn2+

Mn2+

increasing activation up to 30 mM

Mn2+

activates

Mn2+

Mn2+

half-maximal activation at 1 mM

Mn2+

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+

activates

Mn2+

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+

5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required

Mn2+

either Mg2+ or Mn2+ is required in addition to Ca2+

Mn2+

Mn2+

22% stimulation at 10 mM

Mn2+

required

Mn2+

most active

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+

134234

Zn2+

peaked activity at 0.1 mM

Zn2+

Zn2+

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

show all columns Go to Inhibitor Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

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

701234

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-mercaptoethanol

2-Nitro-5-thiocyanobenzoic acid

2-nitro-5-thiosulfobenzoic acid

3'-AMP

5'-deoxy-GMP

competitive, product inhibition

5'-GDP

5'-GMP

5'-GTP

actin

Aflatoxin B2a

non-competitive inhibitor

Aflatoxin G2

non-competitive inhibitor

Aflatoxin G2a

non-competitive inhibitor

Aflatoxin M1

non-competitive inhibitor

Ag2+

Al3+

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

650325

Ca2+

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

650325

Co2+

Crystal violet

Cu-iodoacetate

at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min

Cu2+

diphosphate

dithiothreitol

DTT

80% inhibition at 1 mM

E2-immunity protein

complete inhibition of activity on plasmid DNA

EDTA

24 entries

EGTA

20 entries

Fe3+

G-actin

16 entries

gamma-actin

guanidinium hydrochloride

over 80% inhibition at 0.5 M

heparin

Hg2+

HPO42-

iodoacetate

K+

no inhibition at 50 mM, 50% inhibition at 200 mM

KCl

LiCl

mannitol

methanesulfonylchloride

inactivation at pH 5.0

Mg2+

N-bromosuccinimide

Na+

no inhibition at 50 mM, 50% inhibition at 200 mM

NaCl

Ni2+

oligonucleotides

competitive inhibition

P2O74-

phosphate

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

664029

RNA

enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA

SDS

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)

Tris-HCl buffer

Trypsin

Urea

20% inhibition at 4 M

Zn2+

11 entries

additional information

19 entries

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-mercaptoethanol

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

696291

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+

complete inhibition at 1-10 mM

Ca2+

inhibitory above 1 mM

Ca2+

slight inhibition of mutant D201A

Ca2+

80% inhibition at 0.1 mM

Crystal violet

Crystal violet

Cu2+

complete inhibition at 1-10 mM

Cu2+

complete inhibition

Cu2+

EDTA

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

695544

EDTA

complete inhibition at 20 mM

EDTA

EDTA

EDTA

EDTA

complete inhibition at 20 mM

EDTA

10 mM, complete loss of activity

EDTA

EDTA

50% inhibition at 0.3 mM

EDTA

EDTA

EDTA

EDTA

complete inhibition at 1 mM

EDTA

inhibition observed above 50 microM, complete inhibition at 0.5 mM

EDTA

EDTA

complete ihibition at 1 mM; complete inhibition at 1 mM

EDTA

complete inhibition at 10 mM

EDTA

134215, 134216

EDTA

complete inhibition at 5 mM

EDTA

EDTA

slight inhibition

EDTA

complete inhibition at 1 mM

EGTA

activity inhibited

EGTA

inhibition at 0.01 mM in the presence of 2.5 mM Mg2+

EGTA

134234

EGTA

complete inhibition at 5 mM

EGTA

activity inhibited

EGTA

EGTA

1 mM, complete loss of activity

EGTA

EGTA

inhibition at 1 mM

EGTA

activity inhibited

EGTA

EGTA

complete inhibition at 1 mM

EGTA

complete inhibition of the enzyme from serum at 5 mM

EGTA

EGTA

complete ihibition at 1 mM; complete inhibition at 1 mM

EGTA

EGTA

complete inhibition at 10 mM

EGTA

EGTA

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

134220, 134223

G-actin

complete inhibition at 0.05 mg/ml

G-actin

slight inhibition

G-actin

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

G-actin

G-actin

G-actin

inhibition with actin-gelsolin segment I complex

G-actin

G-actin

66% inhibition in an 1:1 molar ratio of DNase I-actin complex

gamma-actin

gamma-actin

gamma-actin

heparin

directly inhibits recombinant DNase1/3

heparin

heparin

directly inhibits recombinant DNase1/3

Hg2+

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

Medicago sativa

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

134222

NaCl

stimulating between 25 and 50 mM, inhibitory above 50 mM

NaCl

Na-DNA is inhibitory

NaCl

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

activity of wild-type is partly repressed at 0.1 M. Mutant Q9R/E13R/N74K exhibits hyperactive DNA-cutting activity in the presence of up to 1 M NaCl

NaCl

NaCl

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)

NaCl

NaCl

NaCl

phosphate

phosphate

SDS

over 80% inhibition at 0.04% w/v

SDS

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+

complete inhibition at 1-10 mM

Zn2+

Zn2+

complete inhibition at 1 mM

Zn2+

Zn2+

Zn2+

Zn2+

Zn2+

inhibition at millimolar concentrations

Zn2+

complete inhibition

Zn2+

Zn2+

additional information

no inhibition by G-actin

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

650325

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

697759

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

701234

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

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

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

aflatoxin B1

effective activator below 0.08 mM

Aflatoxin B2

effective activator below 0.08 mM

Aflatoxin M2

effective activator below 0.08 mM

Aprotinin

activates DNase1/3-like activity

Bile

bile from rat , reconstitution of activity of inhibited DNase I-actin complex

134229

bovine serum albumin

0.01 mg/reaction volume stimulates about 50% at both pH 6.2 and 7.7

dithiothreitol

heparin

activates DNase1

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

Mg2+

stimulation, required for activity of mutant Q9R/E13R/N74K

Mn2+

stimulation, required for activity of mutant Q9R/E13R/N74K

N-ethylmaleimide

stimulation about 10-20% at both pH 6.2 and 7.7

okadaic acid

10 nM, increases accessibility to DNA in chromatin of carcinoma cells, changes the chromatin supraorganization to a more homgenous and fine chromatin texture as compared to control cells, causes apoptosis after exposure longer than 6 h, no effect on CEM-VLB100 cells

Slx4

the Slx4 protein is essential for efficient processing of DNA substrates

additional information

His44 may play a critical role in substrate DNA binding in the putative secondary active site, and introduction of sulfhydryl groups at Thr14 and Ser43 may facilitate Mn2+-coordination and further contribute to the catalytic activity of DNase I

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show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.005

(pC)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0042

d(pA)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0053

d(pApCpTpApCpApGpTpCpTpApCpA)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0072

d(pGpGpCpApCpTpTpApC)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0056

d(pT)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0037

d(pTpApGpApApGpApTpCpApApA)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

additional information

Double-stranded DNA

additional information

Double-stranded DNA

20 microgram/ml

additional information

Double-stranded DNA

25 microgram/ml

additional information

Double-stranded DNA

values in microgram DNA/ml

additional information

Double-stranded DNA

values in microgram DNA/ml

additional information

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0214

(25R)-3beta-hydroxycholest-5-en-27-oate

37°C, 20 mM Tris-HCl pH 8.3, 1 mM MgCl2

167 - 493.3

(pC)10

106.6

d(pA)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

703.3

d(pApCpTpApCpApGpTpCpTpApCpA)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0492 - 453.3

d(pGpGpCpApCpTpTpApC)

713

d(pT)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

136.6

d(pTpApGpApApGpApTpCpApApA)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0214

lambda phage DNA

37°C, 20 mM Tris-HCl pH 8.3, 1 mM MgCl2

167

(pC)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

493.3

(pC)10

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

0.0492

d(pGpGpCpApCpTpTpApC)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

453.3

d(pGpGpCpApCpTpTpApC)

20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.04

5'-deoxy-GMP

pH 8.5, 37°C

0.0058

5'-GDP

pH 8.5, 37°C

0.0283

5'-GMP

pH 8.5, 37°C

0.0028

5'-GTP

pH 8.5, 37°C

0.00091

actin

0.0000013

gamma-actin

additional information

additional information

additional information

show all columns Go to IC50 Value Search

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.106

2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione

Bos taurus

pH and temperature not specified in the publication

0.134

2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione

Bos taurus

pH and temperature not specified in the publication

0.148

2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione

Bos taurus

pH and temperature not specified in the publication

0.148

2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine

Bos taurus

pH and temperature not specified in the publication

0.128

2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine

Bos taurus

pH and temperature not specified in the publication

0.156

2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine

Bos taurus

pH and temperature not specified in the publication

0.197

2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine

Bos taurus

pH and temperature not specified in the publication

0.195

2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine

Bos taurus

pH and temperature not specified in the publication

0.3659

Crystal violet

Bos taurus

pH not specified in the publication, temperature not specified in the publication

773134

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.008

as plasmid nicking activities in the presence of both Mg2+ and Ca2+ for a DNaseI-Fc fusion protein

0.033

0.05

0.096

as plasmid nicking activities in the presence of both Mg2+ and Ca2+

1009

wild-type, pH 7.0

1020

mutant G100W/E102/G/S103P/G105K, pH 7.0

1092

mutant E102G/S103P, pH 7.0

14.2

14540

purified enzyme, substrate RNA

3600

pH 6.5

531

mutant G100K/E102P/S103G/G105W, pH 7.0

597200

purified enzyme, substrate ssDNA

962

mutant E102P/S103G, pH 7.0

968

mutant G100K/G105W, pH 7.0

975

0.1 M Tris-HCl pH 7.0, 10 mM CaCl2, 10 mM MnCl2, 0.05 mg/ml calf thymus DNA

additional information

44 entries

additional information

purified enzyme

additional information

units defined as absorbance at 260 nm/ml assay solution

134199

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

320 units/mg protein

additional information

938 units/mg protein

additional information

908 units/mg protein

134199

additional information

additional information

specificity in DNA-DNase I interaction is mediated by DNA flexibility, which influences the induced-fit transitions required to form productive complexes. Productive DNA-DNase I interactions appear to be governed by one main DNA structural element: the minor groove width. Minor groove dimension results from various molecular mechanisms. For unbent DNA the local flexibility favors a wide minor groove. Since DNA flexibility is highly sequence dependent, base sequence influences the induced-fit transitions required to form DNA-DNase I complexes

715904

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

21 units/min/ng DNA digested

additional information

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

purified isozymes A and B

additional information

purified isozymes A and B

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

1683 units/mg protein

additional information

1683 units/mg protein

additional information

RT-PCR-based and immunohistochemic detection and quantification

additional information

additional information

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

679657

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. Urine samples give an activity of 1.49 U/ml, blood plasma of 0.36 U/ml

681215

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

670 units/mg protein

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

purified enzyme

additional information

RT-PCR-based immunohistochemic detection and quantification

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

units defined as absorbance at 260 nm/ml assay solution

additional information

5100 units/mg protein

additional information

222 units/mg protein

additional information

400 units/mg protein

134229

additional information

5'-exonuclease, 3'-exonuclease and DNA-binding activities of wild-type and truncated mutants and mutant H371A

additional information

purified enzyme

additional information

purified enzyme

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

10.5 - 11

5.4

in 33 mM sodium phosphate buffer

5.5

in 33 mM acetate buffer, 6 times faster than in phosphate buffer

5.5 - 6.5

wild-type

5.5 - 9.5

mutant Q9R/E13R/N74K

5.8

in the presence of Mg-EGTA

in the presence of Mg2+, dependent on bivalent metal ions

6 - 8

Asp44 is responsible for the higher pH optimum compared to vertebrates, residue 44 might have been involved in the evolutionary change of pH optimum for activity from piscine, reptile and amphibia to vertebrates, who possess a His44 residue and a lower pH optimum

6.2

in 25 mM cacodylate hydrochlorid and 3 mM Co2+

6.4

in the presence of Co2+ in 50 mM cacodylate-HCl buffer

6.5

6.75

DNase I type-1 enzyme

6.8

DNase I

7 - 8

depending on the metal ion used

7.2

with 5 mM Mn2+

7.2 - 7.6

in 33 mM Tris-HCl buffer

7.5

7.5 - 8.5

7.7

in 25 mM Tris-HCl and 1 mM Mn2+

7.8

8.2

8.25

for DNase A

8.5

8.75

for DNase C

assay at

additional information

6.5

6.5

6.5

in the presence of 10 mM MgCl2

6.5

DNase I type-2 enzyme

6.5

in the presence of Mg2+, pH optima dependent on bivalent metal ions

assay at

serum DNase I in the presence of Mg2+ and Ca2+

with 5 mM Mg2+

7.5

7.5

in the presence of Mn2+ in 50 mM Tris-HCl buffer

7.5

7.5

assay at

7.5

for pancreas DNase I in the presence of Mg2+ and Ca2+

7.5

assay at

7.5

7.5

in the presence of Mn2+, different pH-optima, dependent on bivalent metal ions

7.8

7.8

about, Asp44 is responsible for the higher pH optimum compared to vertebrates, residue 44 might have been involved in the evolutionary change of pH optimum for activity from piscine, reptile and amphibia to vertebrates, who possess a His44 residue and a lower pH optimum

bell-shaped optimum

bell-shaped optimum

bell-shaped optimum

assay at

8.5

for DNase B

8.5

8.5

in the presence of Mg2+

additional information

DNase I is a neutral enzyme

additional information

DNase I is a neutral enzyme

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5 - 8.5

pH optimum of recombinant DNase1 is 6.5-7.5 in the presence of Mg2+, and 7.5-8.5 in the presence of Mn2+. PH optimum of recombinant DNase1/3 in the presence of Mg2+ shifts from pH 4.5-5.5 to pH 5.5-6.5 by Mn2+

4.5 - 9.5

5 - 8

64% activity below pH 5.0, 80% activity above pH 8.0

5 - 9

best activity above pH 8.0

9.5 - 12

pH activity profile

additional information

5 - 9

5 - 9

additional information

no activity at acidic pH, e.g. pH 4.8

additional information

sensitive to low pH, Asn110 is responsible

additional information

sensitive to low pH, Asn110 is responsible

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

assay at

assay at

assay at

assay at

assay at

assay at

assay at

assay at

show all columns Go to Temperature Range Search

assay at

assay at

assay at

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

37 - 60

show all columns Go to Pi Value Search

activity remains unchanged

stable up to

85% loss of activity after 5 min, complete inactivation after 10 min

rather stable up to

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3.5

pI values vary from 3.5-4.3 due to single nucleotide polymorphism

4.43

isozyme B, isoelectric focusing

4.56

isozyme A, isoelectric focusing

4.9

DNase1

6.8

isoelectric focusing

8.7

DNase1/3

additional information

the enzyme shows microheterogeneity on 2D-PAGE gels. 3 forms of carp liver DNase with pI 4.9, 4.8, and 4.7 are observed

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

strain ATCC19606T

brenda

strain ATCC19606T

brenda

eel

SwissProt

brenda

SwissProt

brenda

brenda

brenda

multifunctional enzyme

brenda

SwissProt

brenda

Caenorhabditis elegans

Caenorhabditis elegans N2

brenda

brenda

SwissProt

brenda

brenda

spruce budworm

brenda

brenda

japanese quail

brenda

brenda

brenda

SwissProt

brenda

133978, 134232, 664029, 664587, 664707

brenda

brenda

brenda

SwissProt

brenda

15 entries

2 active compounds, A and B

brenda

cv. Thessalia

brenda

cv. Luzerne Euver

brenda

C57BL/6 mice

Uniprot

brenda

brenda

Ovis aries

4 active compounds, A, B, C, D

brenda

sea bream

SwissProt

brenda

sea urgin

brenda

brenda

brenda

134200, 134203, 134204, 134212, 134215, 134216, 134229

brenda

brenda

brenda

isolate SX332

brenda

brenda

i.e. PRV

brenda

fungus

brenda

brenda

SwissProt

brenda

brenda

brenda

brenda

134199, 134208, 134210, 134213, 134215, 134219, 134222, 134223, 134227, 134233, 134234, 134236, 134237, 650325, 653799

brenda

Uniprot

brenda

665821, 666411, 666854

brenda

Uniprot

brenda

695970, 696064, 696291, 696832, 697759

brenda

Uniprot

brenda

699637, 700518, 701077, 701089, 715904, 716661, 728955, 729850

brenda

750023, 750625, 750637, 751527, 768955, 771707, 773134, 774897

Uniprot

brenda

4 active compounds: A, B, C, D

134220, 134221, 134238

brenda

recombinant

695544

brenda

brenda

phage beta infected

brenda

brenda

SwissProt

brenda

brenda

carp

SwissProt

brenda

2 isozymes A and B

SwissProt

brenda

chicken

brenda

134197, 134198, 134200, 134202, 134207, 134214, 134225, 134228, 134230, 649684, 650792, 651445, 664146, 664148, 664612

brenda

SwissProt

brenda

664843, 666887, 681215, 695549, 695970

brenda

SwissProt

brenda

brenda

SwissProt

brenda

699202, 699637, 701234, 707845

brenda

SwissProt

brenda

brenda

SwissProt

brenda

brenda

SwissProt

brenda

different enzyme types of the human DNase I family: DNase I, DNase X, DNase lambda, and DNASIL2

SwissProt

brenda

dornase alpha, recombinant enzyme

brenda

Japanese population

brenda

134200, 663963, 665221

brenda

SwissProt

brenda

695970, 698336, 710137

brenda

750453, 773143

SwissProt

brenda

C57BL/6 mice

Uniprot

brenda

tilapia

SwissProt

brenda

tilapia fish

brenda

brenda

SwissProt

brenda

664154, 680068, 701077, 730378

brenda

761303, 773134, 775968

SwissProt

brenda

Sprague-Dawley rats

SwissProt

brenda

brenda

SwissProt

brenda

brenda

SwissProt

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

blood plasma of 40 non-pregnant women, 40 healthy pregnant women (over 37 weeks) and 40 pregnant women with a diagnosis of intrauterine growth restriction

brenda

leukemic cells

brenda

multi-drug resistant cell line

brenda

chief cell

commercial preparation

brenda

brenda

brenda

mid-previtellogenesis epithelium and late previtellogenesis epithelium

brenda

brenda

brenda

brenda

low activity

brenda

low activity

brenda

pars glandularis

brenda

gut

brenda

low activity

brenda

somatostatin-sensitive enzyme form

brenda

somatostatin-sensitive enzyme form

brenda

brenda

brenda

brenda

low activity

brenda

larva

brenda

brenda

brenda

brenda

brenda

brenda

somatostatin-sensitive enzyme form

brenda

brenda

microplasmodium

brenda

brenda

brenda

brenda

brenda

low activity

brenda

brenda

poor activity

brenda

brenda

brenda

brenda

additional information

brenda

of embryo

brenda

brenda

133978, 134232, 664587, 664029

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

enzyme secretion

brenda

enzyme secretion

brenda

commercial preparation

650325, 728955, 729850

brenda

commercial preparation

773134, 771707, 768955

brenda

embryo

brenda

embryonic brain

brenda

highest enzyme expression and activity

brenda

brenda

brenda

hepatopancreas

brenda

brenda

low activity

brenda

low activity

brenda

poor activity

brenda

high expression level

brenda

brenda

brenda

high DNase1 content

brenda

high DNase1 content

brenda

kidney

somatostatin-resistant enzyme form

brenda

brenda

low activity

brenda

low activity

brenda

brenda

poor activity

brenda

somatostatin-resistant enzyme form

brenda

brenda

low activity

brenda

highest activity in vitellogenic, activity increases during oogenesis, low activity in young oocytes

brenda

brenda

MII oocyte

brenda

brenda

high activity

brenda

134199, 134208, 134210, 134213, 134219, 134221, 134222, 134223, 134227, 134233, 134234, 134236, 134237, 134238, 650325, 653799, 666854

brenda

brenda

brenda

brenda

699637, 700518, 701077, 701089, 695970, 696064, 696291, 716661

brenda

pancreas

750637, 750625, 750023

brenda

brenda

751527, 773134, 771707

brenda

high activity

brenda

highest enzyme activity and expression

brenda

high activity

brenda

brenda

poor activity

brenda

brenda

brenda

brenda

very high expression level

brenda

brenda

from homozygote subjects

brenda

pancreas

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

high activity

brenda

brenda

highest activity

brenda

brenda

somatostatin-resistant enzyme form

brenda

brenda

brenda

low activity

brenda

brenda

brenda

brenda

brenda

brenda

brenda

DNase1/3

brenda

systemic lupus erythematosus patients have lower serum DNase 1 activity compared with healthy controls

brenda

brenda

contains two nucleases, DNase1 and DNase1/3. DNase1/3 is not N-glycosylated, whereas DNase1 is di-N-glycosylated

brenda

serum

lupus-prone NZB/NZW mice have significantly lower serum concentrations of DNase 1 than normal mice, and this reduction is not related to the presence of actin

brenda

serum

contains two nucleases, DNase1 and DNase1/3. DNase1/3 is not N-glycosylated, whereas DNase1 is di-N-glycosylated

brenda

serum

somatostatin-sensitive enzyme form

brenda

brenda

brenda

brenda

low activity

brenda

low activity

brenda

low activity

brenda

low activity

brenda

brenda

poor activity

brenda

high expression level

brenda

somatostatin-sensitive enzyme form

brenda

low activity

brenda

brenda

high DNase1/3 content

brenda

spleen

high DNase1/3 content

brenda

stomach

brenda

brenda

brenda

somatostatin-sensitive enzyme form

brenda

brenda

brenda

134200, 134207, 134214, 134228, 681215, 699637

brenda

10 phenotypes

brenda

highest activity

brenda

lupus-prone NZB/NZW mice have significantly lower urine concentrations of DNase 1 than normal mice, and this reduction is not related to the presence of actin

brenda

brenda

additional information

no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine

brenda

additional information

pancreas-parotid

brenda

additional information

no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine

brenda

additional information

no activity in spleen, parotid gland, lung, heart, cerebellum, and cerebrum

brenda

additional information

no activity in spleen, parotid gland, lung, heart, cerebellum, and cerebrum

brenda

additional information

no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine

brenda

additional information

no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine

brenda

additional information

no activity in brain

brenda

additional information

no activity in brain

brenda

additional information

marked correlation between tissue distribution of enzyme and its sensitivity/resistance to proteolysis

brenda

additional information

secretion of enzyme is controlled by the chief cells in the stomach

brenda

additional information

tissue distribution of enzymes of the DNase I family, complete overview

brenda

additional information

tissue distribution of enzymes of the DNase I family, complete overview

brenda

additional information

a fraction of abzymes from autoimmune patients hydrolyzing both DNA and RNA can contain a subfraction of antibodies against DNase I

699637

brenda

additional information

EG-1 cell

698336

brenda

additional information

Podarcis siculus

pyriform cell

697190

brenda

additional information

secretion of enzyme is controlled by the chief cells in the stomach

brenda

additional information

no activity in spleen, heart, lung, stomach, large intestine, cerebrum, cerebellum, submaxillary gland, and thymus

brenda

additional information

no activity in spleen, heart, lung, stomach, large intestine, cerebrum, cerebellum, submaxillary gland, and thymus

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

endoplasmic reticulum

786

brenda

brenda

secretory granule

additional information

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

endoplasmic reticulum

5783

brenda

endoplasmic reticulum

brenda

brenda

brenda

secreted into the culture medium

brenda

brenda

secreted into duodenal juice

brenda

secreted into urine

134200, 134207, 134214, 134228

brenda

brenda

brenda

brenda

secreted into urine

brenda

brenda

serum

brenda

brenda

secreted into pancreatic juice

brenda

secreted into urine

brenda

brenda

brenda

brenda

activity 6 times higher than in cytoplasm

brenda

brenda

brenda

DNase I digestion in interphase nuclei

5634

701148

brenda

outer membrane

19867

brenda

outer membrane

brenda

exocrine

brenda

exocrine

brenda

additional information

the intracellular recombinant OmpA is degraded into several forms of subfragments in the cytosol of the host and two subfragments of recombinant OmpA are translocated into the nuclei

brenda

additional information

the intracellular recombinant OmpA is degraded into several forms of subfragments in the cytosol of the host and two subfragments of recombinant OmpA are translocated into the nuclei

brenda

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Highest Expressing Human Cell Lines

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show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

additional information

physiological function

in uninduced K-562 cells, several sites within HMIP-2 show sensitivity to DNase I above background levels. When cells are induced to differentiate, the region shows a general increase in DNase I sensitivity: 3 sites refer to here as HBS1L-MYB HS1, HS2, and HS3, in particular, show a marked increase in sensitivity compared with background levels. DNase I sensitivity also increases for betaHS2 and betaHS3 controls. HBS1L-MYB HS1, HS2, and HS3 also show stronger sensitivity to DNase I than the betaHS3 control, thereby reaching a threshold level for hypersensitivity. No difference in DNase I sensitivity for NEFM in uninduced and induced K-562 cells. BetaHS2 is not sensitive to DNase I in Jurkat cells. Jurkat cells show similar background levels and generally, a similar DNase I sensitivity profile to induced K562 cells, but with much less sensitivity at HBS1L-MYB HS1, HS2, and HS3. The strongest sensitivity to DNase I in Jurkat cells coincides with the putative promoter region of the alternative HBS1L exon (exon 1a), which shows a low degree of sensitivity in K-562 cells (both uninduced and induced)

707845

physiological function

expression of DNase I induces all other endonucleases at varying time periods after transfection, causes DNA breaks in endonuclease genes, and elevates protein expression of several endonucleases. Catalytic activity of DNase I is required for these effects

761303

additional information

DNase I hypersensitivity analysis of the mouse brain and retina identifies region-specific regulatory elements

750453

additional information

DNase I hypersensitivity analysis of the mouse brain and retina identifies region-specific regulatory elements

750453

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (404 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

Aliivibrio salmonicida LFI1238

14 entries

13 entries

Francisella tularensis subsp. novicida

12 entries

Leptographium truncatum

Streptococcus pyogenes serotype M1

Francisella tularensis subsp. novicida

Francisella tularensis subsp. novicida

Streptococcus pyogenes serotype M1

Streptococcus pyogenes serotype M1

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

108000

SDS-PAGE, the pre-mature DNase contains a signal peptide and has an molecular weight of 112000

12000

SDS-PAGE

14000

SDS-PAGE

16000 - 17000

gel filtration, SDS-PAGE

17000

SDS-PAGE

22000

gel filtration

22400

gel filtration

23000

x * 23000, SDS-PAGE

25000

mature form after cleavage of the signal peptide

28000

SDS-PAGE

29000

SDS-PAGE

29800

calculated molecular mass of DNase1

30000

30070

calculated from amino acid and carbohydrate composition for DNase A

30859

x * 30000, SDS-PAGE, x * 30859, isozyme A, mass spectrometry, x * 30882, isozyme B, mass spectrometry

30882

x * 30000, SDS-PAGE, x * 30859, isozyme A, mass spectrometry, x * 30882, isozyme B, mass spectrometry

31000

32000

32498

x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation

33000

33000 - 38000

for serum and pancreas DNase I, gel filtration

33100

calculated molecular mass of DNase1/3

34000

7 entries

34500

1 * 34500, SDS-PAGE, gel filtration

345000

SDS-PAGE

35000

SDS-PAGE

36000

gel filtration

37000

38000

gel filtration

40000

41000

61000

x * 61000, SDS-PAGE

80000

SDS-PAGE

30000

gel filtration, SDS-PAGE

30000

gel filtration, SDS-PAGE, thin-layer IEF, MS analysis

30000

calculated from sequence

30000

1 * 30000, deglycosylated enzyme, SDS-PAGE, 42000-47000, glycosylated enzyme, SDS-PAGE

30000

x * 30000, SDS-PAGE, x * 30859, isozyme A, mass spectrometry, x * 30882, isozyme B, mass spectrometry

31000

31000

amino acid analysis

31000

SDS-PAGE

31000

SDS-PAGE

32000

SDS-PAGE

32000

gel filtration, sucrose density gradient centrifugation

32000

SDS-PAGE, gel filtration

32000

SDS-PAGE, gel filtration

32000

SDS-PAGE

32000

x * 32000, SDS-PAGE

33000

sucrose density gradient centrifugation, gel filtration

33000

SDS-PAGE, gel filtration

33000

x * 33000, SDS-PAGE

34000

34000

SDS-PAGE, gel filtration

34000

SDS-PAGE

34000

SDS-PAGE

34000

SDS-PAGE

34000

SDS-PAGE

34000

DNase1/3, by DPZ

37000

DNase1, by DPZ

37000

x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation

40000

gel filtration

40000

gel filtration

40000

gel filtration

41000

SDS-PAGE, gel filtration

41000

gel filtration

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

heterotrimer

CdtB/DNAse I, but not DNAseI/CdtB

monomer

15 entries

additional information

x * 23000, SDS-PAGE

x * 61000, SDS-PAGE

x * 32000, SDS-PAGE

x * 30000, SDS-PAGE, x * 30859, isozyme A, mass spectrometry, x * 30882, isozyme B, mass spectrometry

x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation

x * 33000, SDS-PAGE

dimer

1 * 12000 and 1 * 14000, gel filtration, SDS-PAGE

dimer

2 * 17000, gel filtration

dimer

2 * 28000, gel filtration

monomer

1 * 40000, SDS-PAGE

monomer

1 * 16000-17000, four active fractions

monomer

1 * 30000, deglycosylated enzyme, SDS-PAGE, 42000-47000, glycosylated enzyme, SDS-PAGE

monomer

four active fractions, gel filtration, SDS-PAGE

monomer

1 * 40000, SDS-PAGE

monomer

1 * 40000, SDS-PAGE

monomer

1 * 34000, SDS-PAGE

134197, 134198, 134207

monomer

1 * 32000, SDS-PAGE, gel filtration

monomer

1 * 30000, SDS-PAGE, gel filtration

monomer

1 * 35000, SDS-PAGE, gel filtration

monomer

1 * 32000, SDS-PAGE, gel filtration

monomer

monomer

1 * 32000, SDS-PAGE, gel filtration

monomer

1 * 34000, SDS-PAGE

monomer

1 * 34500, SDS-PAGE, gel filtration

additional information

structural analysis, insertion of a serine residue at position 205 and addition of a cysteine-rich C-stretch at the C-terminus are significant

additional information

structural analysis, insertion of a serine residue at position 205 and addition of a cysteine-rich C-stretch at the C-terminus are significant

additional information

structural analysis, insertion of a serine residue at position 205 and addition of a cysteine-rich C-stretch at the C-terminus are significant

additional information

structural analysis, insertion of a serine residue at position 205 and addition of a cysteine-rich C-stretch at the C-terminus are significant

additional information

interaction of enzyme with actin and inhibition by actin. Inhibition may serve as a self-protection mechanism against premature DNA degradtion during cell damage

additional information

the enzyme is divided into a catalytic domain and a DNA-binding domain

show all columns Go to Posttranslational Modification Search

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

25 entries

no glycoprotein

proteolytic modification

enzyme sequence contains a precursor peptide

additional information

glycoprotein

15% carbohydrate content

glycoprotein

2 N-acetylglucosamine proximal to the carbohydrate chain at Asn18, followed by a variable number of mannose residues

134233

glycoprotein

DNase A: 2 N-acetylglucosamine residues, 6 mannose residues, DNase B: 1 sialic acid residue, 3 N-acetylglucosamine residues, 5 mannose residues

glycoprotein

DNase D contains sialic acid in the carbohydrate portion

glycoprotein

carbohydrate-chain at Asn 18

134199, 134220

glycoprotein

DNase A with a neutral carbohydrate side-chain, DNase B with a sialic acid carbohydrate side-chain

134199, 134213, 134215, 134220, 134233, 134238

glycoprotein

1 potential N-glycosylation site

glycoprotein

glycoprotein

3.4% carbohydrate content

glycoprotein

protein contains a N-linked carbohydrate moiety. Potential glycosylation sites at N18 and N106

glycoprotein

binds to concanavalin A, contains an N-glycosylation site

glycoprotein

glycoprotein

contains fucose, mannose, galactose, glucosamine, sialic acid

glycoprotein

phosphoglycoprotein

glycoprotein

enzyme contains 2 potential N-glycosylation sites

glycoprotein

glycoprotein

11.8% carbohydrate content

glycoprotein

carbohydrate-chain at Asn 18

glycoprotein

glycoprotein

glycoprotein

glycoprotein

contains fucose, mannose, galactose, glucosamine, sialic acid

glycoprotein

2 carbohydrate side-chains attached at Asn18 and Asn106

134211

glycoprotein

glycoprotein

no glycoprotein

no glycoprotein

no glycoprotein

no glycoprotein

additional information

protein exhibits one large essential (C173-C209) disulfide loop and one small non-essential (C101-C104) disulfide loop

additional information

protein exhibits one large essential (C173-C209) disulfide loop and one small non-essential (C101-C104) disulfide loop

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

2.5 A resolution, alpha-beta-protein, carbohydrate attached to Asn18, active centre close to His 131

at 2 A resolution

complex between DNase I and uncleaved octamer duplex DNA, 2.3 A resolution

134213, 134219

H134 and H252 involved in catalysis

show all columns Go to Protein Variants Search

134219

in complex with magnesium and phosphate ions, both bound in the active site, to 1.95 A resolution. Data suggest a magnesium-assisted pentavalent phosphate transition state during catalysis, where Asp168 may play a key role as a general catalytic base. Residue Asn7 plays a critical role in the catalytic mechanism, participating indirectly in the coordination sphere of the Mg2+ ion with an H-bond of its amide oxygen with a coordinated water molecule and connects Asp168 and Glu39 with an H-bonding network via its amide nitrogen

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

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

C173A

active

C209A

active

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

active enzyme

Delta1-10

inactive enzyme

Delta1-11

inactive enzyme

Delta1-2

inactive enzyme

DELTA1-3

inactive enzyme

Delta1-8

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

Delta260

active 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

L1D

active enzyme

L1D/L259K

active enzyme

L1K

active enzyme

L1K/L259D

active enzyme

L259A

active enzyme

L259D

active enzyme

L259I

active enzyme

L259K

active enzyme

L259Y

active enzyme

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

729209

N7S

complete loss of activity

729209

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

Q222R

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

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

D81G

no activity

D81N

50% activity compared to wild type

H46A

activity similar to wild type

R334A/E74A

inactive

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

protein is not expressed

additional information

7 entries

Q222R

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

Q9R/E13R/N74K

most hyperactive variant, 35fold more active than wild type enzyme

Q9R/E13R/N74K

mutant can efficiently digest DNA in the presence of monovalent metal ions at a high concentration (e.g., 1 M NaCl). The mutant enzyme cuts DNA containing 5-methylcytosine and 2'-deoxycytidine efficiently and displays high DNA-cutting activity over the pH range 5.5-9.5

additional information

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

681708

additional information

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

additional information

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

additional information

construction of mutants with deletions at the N- and/or the C-terminus, mutants reveal the localisation fo activities within the enzyme sequence, overview

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 9

stable within the range for 24 h at 4°C

activity completely lost

activity completely lost

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

-20

stable for 1 month

-30

no loss of activity in crude extract

stable for 7 days

100

DNAse I DNA nicking-activity is less than 50% of the control after 5 min of heating

inactivation after 10 min incubation

inactive above 65°C

inactivation above

additional information

no activity

stable for one week, when concentration is greater than 3000 U/ml

stable up to, more stable up to 60°C, if Ca2+ is present

stable up to at pH 6.5, loss of activity at 60°C

15 min, stable

stable for 20 min

additional information

both N-linked glycosylation sites N18 and N106 are required for heat stability

additional information

697759

additional information

both N-linked glycosylation sites N18 and N106 are required for heat stability

additional information

both N-linked glycosylation sites N18 and N106 are required for heat stability

additional information

both N-linked glycosylation sites N18 and N106 are required for heat stability

additional information

both N-linked glycosylation sites N18 and N106 are required for heat stability

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

Ca2+ is able to protect DNase completely against inactivation by trypsin

134236, 134238

extremely sensitive to inactivation by proteases in the absence of Ca2+

less active in phosphate buffer

N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance

prolonged storage in the frozen state in H2O causes a gradual decrease of activity, half life of DNases A and B is 2 months

sensitives to repeated freezing and thawing

stable at high concentrations of urea and organic solvents but susceptible to low concentrations of SDS and guanidine hydrochloride

less active in phosphate buffer

less active in phosphate buffer

N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance

N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance

N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance

sensitives to repeated freezing and thawing

sensitives to repeated freezing and thawing

show all columns Go to Organic Solvent Search

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ORGANIC SOLVENT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimethyl formamide

20% decrease in activity at 40% v/v

dimethyl sulfoxide

20% decrease in activity at 15% v/v

Ethylene glycol

80% loss of activity during overnight at 0°C

formamide

stable to at 50% v/v

Glycerol

10% glycerol v/v protects against inactivation

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20, 50 mM Tris-HCl 10 mM 2-mercatpoethanol 100 mM NaCl 10 mM EDTA 50% glycerol, several months, minimal loss of activity

-20°C, 10 mM Tris-HCl, pH 7.0, 10 mM KCl, 5 M urea, 6 months

-20°C, 10 mM Tris-HCl, pH 7.5, 5 mM CaCl2, 30% polyethylene glycol, more than 3 months

-20°C, 20 mM Tris-HCl, pH 7.5, 30% glycerol, 6 months

-20°C, 20 mM Tris-HCl, pH 7.5, 5 mM CaCl2, 10% v/v glycerol, 6 months

-70°C, 10 mM Tris/HCl, pH 7.4, 50% v/v glycerol, 2 years

0°C, 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 5 mM CaCl2, 30% polyethylene glycol, 4 weeks

37°C, protease free preparation, absence of Ca2+, pH 8.0, more than 10 days

4°C, 0.1 M sodium phosphate, pH 7.0, 0.2 M NaCl, 2 months

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

10000fold from hepatopancreas

10000fold from pancreas

1300fold from pancreas

14000fold from hepatopancreas

1400fold from pancreas

17000fold from hepatopancreas

17000fold from hepatopancreas, to homogeneity

1800fold from pancreas

2 chromatography steps to homogeneity

2479fold from pancreas, isozymes A and B to homogeneity

260fold from pancreas, to homogeneity

26500fold from pancreas, to homogeneity

6057fold to homogeneity

affinity chromatography

affinity chromatography and gel filtration, highly pure protein was used for assays

by chromatography on hydroxylapatite

696291

commercial preparation

715904

conconavalin A-agarose as an effective step for DNases with neutral carbohydrate side-chains, preparing a protease free DNase I

DNase1/3-like nuclease, by affinity chromatography

from larval gut

from parotid gland

Hi-Trap chelating column chromatography and Superdex-200 gel filtration

high homogeneity by chromatography steps

near homogeneity

near homogeneity by affinity chromatography

near homogeneity by fractionation steps

near homogeneity by isoelectric focusing and gel filtration

one chromatographic step to homogeneity

one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column

overexpressed DNaseI-Fc fusion protein

overexpressed enzyme

recombinant His-tagged enzyme from 293 cells

recombinant wild-type and deletion mutants from Escherichia coli, to homogeneity

recombinant wild-type and mutant enzymes from Escherichia coli

separation from E2-immunity protein by guanidine-HCl dissociation

three chromatographic steps

to homogeneity

to homogeneity by 2step chromatography

to homogeneity by 4step chromatography

to homogeneity by 6step chromatography

134207, 134214

to homogeneity by affinity chromatography

134203, 134216

to homogeneity by chromatography steps

to homogeneity by chromatography techniques for serum and pancreas DNase I

to homogeneity by chromatography techniques, isoelectric focusing, gel filtration

to homogeneity by conconavalin A-agarose

1800fold from pancreas

1800fold from pancreas

2 chromatography steps to homogeneity

2 chromatography steps to homogeneity

666887

high homogeneity by chromatography steps

high homogeneity by chromatography steps

one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column

one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column

one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column

three chromatographic steps

three chromatographic steps

to homogeneity

to homogeneity

to homogeneity by chromatography steps

to homogeneity by chromatography steps

134211

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

deducing amino acid composition from cDNA

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

DNA and amino acid sequence determination and analysis, expression in COS-7 cells as His-tagged enzyme

DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in COS-7 cells

DNA and amino acid sequences determination and analysis, expression in Escherichia coli BL21(DE3) in the insoluble fraction

DNA sequence determination and analysis

DNase I cDNA, derived from genes DNASE1-1 and DNASE1-2 ligated into a pcDNA3.1 (+) vector and expressed in COS-7 cells

DNAse I or DNAse I/cdtB gene chimera expressed from vectors pETBDN2 (cdB-DNAse I chimera), pETDNB1 (DNAse I-cdB chimera) and pETBDN2-1 to pETBDN2-5 (cdB-DNAse I mutated chimera) in Escherichia coli BL-21(DE3)

expression in COS cells

expression in COS-7 cell

expression in COS-7 cells

expression in Escherichia coli

expression in Escherichia coli as His-tag fusion construct

expression in human 293 cells

expression in MCF-7 cell

expression in NIH-3T3 fibroblasts

expression of wild-type and deletion mutants in Escherichia coli BL21 (DE3)

expression of wild-type and mutant enzymes in Escherichia coli

expression of wild-type and mutants in COS-7 cells

into the pET28a expression vector and overexpressed in Escherichia coli BL21 (DE3). His-tagged OmpA expressed in HEp-2 cells

into vector pET15b and expressed in Escherichia coli strain BL21(DE3)pLysE

mutant G52E (CRM197) is expressed in Escherichia coli BL21AI cells

NIH-3T3 cells with expression vectors for murine DNase1 and DNase1/3 cDNA

overexpression in chinese hamster ovary cells

134198

overexpression in Escherichia coli

134199

overexpression in Sf9 cells as a DNaseI-Fc fusion- and a non-fusion protein

quantification of gene transcript in somatostatin treated animals

transient ectopic expression in HeLa S3 cells, no toxic effect on host cells, expression in human embryonic kidney 293 cells as His-tagged enzyme

transient expression in COS-7 cell

deducing amino acid composition from cDNA

deducing amino acid composition from cDNA

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

651802, 650419

DNA and amino acid sequence determination and analysis, expression in COS-7 cells

DNA and amino acid sequence determination and analysis, expression in COS-7 cells as His-tagged enzyme

DNA and amino acid sequence determination and analysis, expression in COS-7 cells as His-tagged enzyme

expression in COS-7 cells

expression in COS-7 cells

expression in COS-7 cells

expression in COS-7 cells

expression in COS-7 cells

expression in Escherichia coli

expression in Escherichia coli

666887

expression in Escherichia coli

expression in NIH-3T3 fibroblasts

expression in NIH-3T3 fibroblasts

expression of wild-type and mutant enzymes in Escherichia coli

expression of wild-type and mutant enzymes in Escherichia coli

expression of wild-type and mutants in COS-7 cells

expression of wild-type and mutants in COS-7 cells

expression of wild-type and mutants in COS-7 cells

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

high glucose induces both DNase I and caspase-3

730378

significant increase of DNase I activity in cases of intrauterine growth restriction. Increase in DNase I activity over a certain threshold indicates presence of pathological processes in the organism

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

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

697759

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

degradation

diagnostics

medicine

molecular biology

pharmacology

additional information

Podarcis siculus

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

697190

analysis

study of chromatin structure, visualizing cellular microfilaments by DNase I-actin interaction

analysis

preparation of substrates for the nick translation reaction, production of random DNA fragments, analysis of DNA-protein complexes

analysis

analysis

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

analysis

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

695544

analysis

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

728955

analysis

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

728956

analysis

detection method for viral dsRNA in parasites. The protocol comprises RNA extraction from the parasites, RNA purification, enzymatic digestions with DNase I and Nuclease S1, and visualization by gel electrophoresis

768955

analysis

DNase I mutant Q9R/E13R/N74K displays hyperactive DNA cutting in the presence of high salts and over a wider pH range. Mutant can be used in an LC-MS/MS assay for unbiased quantification of 5-methylcytosine levels and for accurate quantification of DNA modifications in salt-containing DNA samples

degradation

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

729850

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

750625

diagnostics

increased DNase I activity in patient serum could be used as diagnostic marker for the early detection of acute myocardial infarction

664612

diagnostics

increase in DNase activity in blood was observed during development of breast cancer

diagnostics

decrease in DNase activity in blood correlates with chronic pancreatitis, stomach cancer and glomerulonephritis

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

750009

medicine

inhibition of viral synthesis by DNase I in cell cultures

medicine

inhaled DNase I into the airways reduces viscoelasticity of sputum, improves lung function of cystic fibrosis patients

134197, 134198, 134202

medicine

improvement of respiratory tract functioning in patients with cystic fibrosis

medicine

medicine

medicine

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

681708

medicine

single nucleotide polymorphism in exon 8, is associated with several diseases

medicine

DNAse I/cdtB gene chimera has therapeutic applications for inhibiting the proliferation of cancer cells

medicine

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

699202

medicine

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

usage of DNase 1 as a therapeutic agent in systemic lupus erythematosus

medicine

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 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

729608

medicine

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

730378

medicine

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

medicine

systemic DNase I administration during cardiopulmonary bypass efficiently reduced circulating cellfree DNA/neutrophil extracellular traps-mediated endothelial dysfunction and inflammation. In rats that underwent cardiopulmonary bypass with deep hypothermic circulatory arrest, a positive correlation is found between plasma circulating cellfree DNA/neutrophil extracellular traps levels and compromised endothelial vasorelaxation after cardiopulmonary bypass . DNase I administration significantly diminishes plasma circulating cellfree DNA/neutrophil extracellular traps levels. Digestion of neutrophil extracellular traps by DNase I significantly diminishes neutrophil extracellular traps-dependent upregulation of adhesion molecules in human endothelial cells

775968

medicine

topical DNase I application promotes corneal epithelial wound healing and mechanical sensation restoration in diabetic mice. Increased neutrophils extracellular traps production during the delayed corneal epithelial wound healing of diabetic mice is significantly improved through either DNase I or Cl-amidine administration. DNase I improves inflammation resolution, reactivates epithelial regeneration-related signalling pathways and attenuates the accumulation of reactive oxygen species. DNase I application also promotes corneal nerve regeneration and restores the impaired corneal sensitivity in diabetic mice

773143

medicine

application of DNase I to improve the activity of cefotaxime, amikacin, and ciprofloxacin against Klebsiella pneumoniae biofilms. Combination with DNase I does not improve the biofilm-preventive capacity of the antibiotics or the biofilm-eradicating capacity of cefotaxime and amikacin. The biofilm-eradicating capacity of ciprofloxacin is increased by 8fold and 4fold in K. pneumoniae ATCC 700603 and a clinical isolate, respectively, with DNase I. The combination therapy causes 99% reduction in biofilm biomass in a mouse model of subcutaneous catheter-associated infection

774897

molecular biology

a DNase bioreactor can be used to remove DNA from RNA samples prior to reverse transcription followed by PCR

665821

molecular biology

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

698336

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

750637

pharmacology