Information on EC 3.1.21.1 - deoxyribonuclease I

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.1.21.1
-
RECOMMENDED NAME
GeneOntology No.
deoxyribonuclease I
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA. Similar enzymes: streptococcal DNase (streptodornase), T4 endonuclease II, T7 endonuclease II, E. coli endonuclease I, "nicking" nuclease of calf thymus, colicin E2 and E3, formerly EC 3.1.4.5
-
-
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for single-stranded DNA
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
Asp44 is involved in catalysis, while Met118, Gln134, Glu190, and Met236 are not
Q5KTT1
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
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
show the reaction diagram
conserved residues Glu79, His135, Asp213, and His 252 are involved in catalysis
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
Glu128 is required for activity, contains conserved sequence LEDFXR, endonuclease activity
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
Q767J3
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
Q9YGI5
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
Q5KTT0
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
O42446
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
-
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for single-stranded DNA and 3'AMP, guanylic acid preferential endo-exonuclease, mode of action, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deoxyribonuclease
-
-
-
-
deoxyribonuclease A
-
-
-
-
deoxyribonucleic phosphatase
-
-
-
-
desoxyribonuclease
-
-
-
-
DNA endonuclease
-
-
-
-
DNase
-
-
-
-
DNase I
-
-
-
-
Dornase alfa
-
-
-
-
endodeoxyribonuclease I
-
-
-
-
Escherichia coli endonuclease I
-
-
-
-
nuclease, deoxyribo-
-
-
-
-
nuclease, Escherichia coli endo-, I
-
-
-
-
pancreatic deoxyribonuclease
-
-
-
-
pancreatic DNase
-
-
-
-
streptodornase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9003-98-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC19606T
-
-
Manually annotated by BRENDA team
Acinetobacter baumannii ATCC19606T
strain ATCC19606T
-
-
Manually annotated by BRENDA team
multifunctional enzyme
-
-
Manually annotated by BRENDA team
4 active compounds: A, B, C, D
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
Bufo vulgaris japonicus
-
SwissProt
Manually annotated by BRENDA team
Caenorhabditis elegans N2
strain N2
-
-
Manually annotated by BRENDA team
spruce budworm
-
-
Manually annotated by BRENDA team
phage beta infected
-
-
Manually annotated by BRENDA team
japanese quail
-
-
Manually annotated by BRENDA team
2 isozymes A and B
SwissProt
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
different enzyme types of the human DNase I family: DNase I, DNase X, DNase lambda, and DNASIL2
SwissProt
Manually annotated by BRENDA team
dornase alpha, recombinant enzyme
-
-
Manually annotated by BRENDA team
Japanese population
-
-
Manually annotated by BRENDA team
2 active compounds, A and B
-
-
Manually annotated by BRENDA team
cv. Thessalia
-
-
Manually annotated by BRENDA team
cv. Luzerne Euver
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
C57BL/6 mice
Uniprot
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
Uniprot
Manually annotated by BRENDA team
tilapia fish
-
-
Manually annotated by BRENDA team
4 active compounds, A, B, C, D
-
-
Manually annotated by BRENDA team
sea bream
SwissProt
Manually annotated by BRENDA team
Potyvirus sp.
-
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
SwissProt
Manually annotated by BRENDA team
strain MGAS5005
-
-
Manually annotated by BRENDA team
isolate SX332
-
-
Manually annotated by BRENDA team
i.e. PRV
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(pC)10 + H2O
?
show the reaction diagram
-
-
-
-
-
190mer DNA fragment + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
3'AMP + H2O
adenosine + phosphate
show the reaction diagram
-
phosphomonoesterase activity
-
?
calf thymus DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
chromatin + H2O
?
show the reaction diagram
-
-
-
-
?
chromatin + H2O
?
show the reaction diagram
O55070
recombinant DNase1 degrades chromatin effectively only in cooperation with serine proteases, such as plasmin or thrombin, which remove DNA-bound proteins. Recombinant DNase1/3 degrades chromatin without proteolytic help
-
-
?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
cosmid DNA + H2O
?
show the reaction diagram
-
-
-
-
?
crab d(A-T) polymer + H2O
5'-hexanucleotides + ?
show the reaction diagram
-
unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure
enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage
?
d(pA)10 + H2O
?
show the reaction diagram
-
-
-
-
-
d(pApCpTpApCpApGpTpCpTpApCpA) + H2O
?
show the reaction diagram
-
-
-
-
-
d(pGpGpCpApCpTpTpApC) + H2O
?
show the reaction diagram
-
-
-
-
-
d(pT)10 + H2O
?
show the reaction diagram
-
-
-
-
-
d(pTpApGpApApGpApTpCpApApA) + H2O
?
show the reaction diagram
-
-
-
-
-
d-ApApTp + H2O
pTp + d-ApA
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for native DNA, A-T rich DNAs more rapidly degraded, no activity on hydroxymethylcytosine-glycosidilic DNA
almost converted into low molecular weight products
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for native DNA
produces nicks on one strand in preference to scission of both strands, autoretardation causes the continuous formation of products which are poorer substrates than those from which they are derived
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degrades native DNA 7fold faster than denatured DNA
products have an avarage chain length of 7 residues
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degradation of native DNA is 80%, that for denatured DNA 70%
88% of products are longer than tetranecleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degrades native DNA 4-5times faster than denatured DNA
mainly nucleotides larger than pentanucleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degrades native DNA 1.5times faster than denatured DNA
half the 5'-termini are deoxythymidinemonophosphate, 90% of the products are larger than pentanucleotides
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degrades native DNA 2times faster than denatured DNA
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
degrades native DNA 2times faster than denatured DNA
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
after 60 min of enzymatic digestion, the DNA content reaches 57% of the initial amount and 20% after 105 min, until complete digestion is achieved after 2 h
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
complementary DNA S2 allowed to hybridize with S1 forms DNA duplexes (the substrate for DNase I) on gold nanoparticles
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNAse I converts 100% of 1 microg of supercoiled plasmid DNA to relaxed form in 1 h at 37C. A 10fold higher concentration of DNAse I converts 98% of 1 microg of supercoiled DNA to linear form and a 100fold higher concentration of the nuclease completely digests the DNA into small fragments
-
-
?
DNA + H2O
5'-phosphotrinucleotides + ?
show the reaction diagram
-
no preference for any nucleotide
as the main products
?
DNA + H2O
5'-phosphodinucleotides + 5'-phosphooligonucleotides
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q767J3
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P21704
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q4AEE3
-
-
-
?
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
lamdaDNA, HindIII, degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
-
?
double-stranded circular DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded circular DNA + H2O
?
show the reaction diagram
Potyvirus sp.
-
-
-
-
?
double-stranded DNA + H2O
?
show the reaction diagram
P24855
-
-
-
?
double-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
P00639
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
Q5R2I2
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
Q5R2I3
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
double-strand breaks occure more rapidly in the presence of Ca2+
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for single-stranded and supercoiled DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
introduces preferentially breaks on the 5' side of dT
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
involved in seed sprouting
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
functionally active during digestion, participation in the repair of damaged DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
involved in DNA degradation during apoptosis
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
cleaves both strands of a double helix at or near the same level, about 400 nucleotides removed at each endonucleolytic scission, causes a "shattering" at the point of cleavage, leading to the libration of small oligonucleotides by an exonucleolytic mode of attack
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
different structure-specific DNA substrates representing stem loop structures with different loop length were used as substrate. Slx1 cuts these substrates at th 3' side of double-strand/single-strand junctions
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I activity was assayed in serum of acute myocardial infarction (AMI). Compared to the control groups the level of DNase I was 2fold higher within 3 hours of the onset of symptoms
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I acts as a transcription activator of the fas gene by direct binding to its promoter
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I is involved in chromatin disposal in necrotic tissue, DNase Y is involved in chromatin disposal in necrotic tissue
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
P21704
high activity on plasmid DNA, weak activity on nuclear DNA
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
immobilized DNase I is used in a bioreactor
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
low activity on plasmid DNA, high activity on nuclear DNA
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
the N-terminal fragment of gelsolin disrupts the actin-DNase I interaction in vitro. Colfilin stabilizes the actin-DNase I complex preventing release of DNaseI from actin by gelosin in vitro
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I-DNA interaction alters protein secondary structure, with a major reduction in alpha helix and an increase in beta sheet and random structures, and reveals a partial B-to-A DNA conformational change. No DNA digestion upon protein-DNA complexation
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
Caenorhabditis elegans N2
-
-
-
-
?
double-stranded linear DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded linear DNA + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded linear DNA + H2O
?
show the reaction diagram
Potyvirus sp.
-
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P24855
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q90WM1
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q90W31
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Bufo vulgaris japonicus
Q90WM0
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P11936
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P24855
in presence of Mg2+ and Ca2+ under neutral conditions
production of 3'-OH and 5'-phosphate ends
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
predominant single-strand nicking in presence of Mg2+ and Ca2+
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
wild-type enzyme and mutant D99A perform double scission on duplex DNA in presence of Mg2+ and Ca2+, not mutant D201A
-
?
dsDNA + H2O
?
show the reaction diagram
-
-
-
?
dsDNA + H2O
?
show the reaction diagram
-
very low activity
-
?
Fc-oligo-SH + H2O
?
show the reaction diagram
-
degradation of a thiolated ferrocenyloligonucleotide, efficiency of DNase I reaction on the electrode is 48, 72, or 73% when treated with 1 microl of 2, 1, or 0.5 micromol ferrocenyloligonucleotide, respectively. DNase I can cleave the oligonucleotide on the gold surface and does not show a nonspecific surface absorption
-
-
?
H2AL2 nucleosome core particle + H2O
?
show the reaction diagram
-
DNase I and hydroxyl radical footprinting as well as micrococcal and exonuclease III digestion show alterations in the structure of the histone variant H2AL2 nucleosome all over the nucleosomal DNA length
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
90% of the products are larger than pentanucleotides
-
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
only in the presence of both Ca2+ and Mg2+
?
HMIP-2 + H2O
?
show the reaction diagram
-
identifies three tissue-specific DNase I hypersensitive sites in the core intergenic interval
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
show the reaction diagram
-
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
show the reaction diagram
-
-
-
?
NO2-Ph-pdTp-NO2-Ph + H2O
p-nitrophenol + ?
show the reaction diagram
-
-
-
?
NO2-Ph-pdTp-NO2Ph + H2O
p-nitrophenol + NO2-Ph-pdT-3'-phosphate
show the reaction diagram
-
rapidly hydrolyzed at a single bond
-
?
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
show the reaction diagram
-
-
-
?
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
show the reaction diagram
-
-
-
?
phage M13 DNA + H2O
?
show the reaction diagram
-
endolytically cleavage generating single base nicks
-
?
plasmid DNA + H2O
?
show the reaction diagram
-
-
-
-
?
plasmid DNA + H2O
?
show the reaction diagram
-
-
-
-
?
plasmid DNA + H2O
?
show the reaction diagram
-
depending on metal ions, duplex DNA is hydrolyzed by DNase I in a single or double scission mode
-
-
?
poly(dA) + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
poly(dT) + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
pUC18 DNA + H2O
?
show the reaction diagram
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
acts more rapidly on circular duplex DNA than on supercoiled DNA
-
?
RNA + H2O
?
show the reaction diagram
-
low activity
-
?
RNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
RNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
salmon sperm DNA + H2O
?
show the reaction diagram
-
-
-
-
?
salmon sperm DNA + H2O
?
show the reaction diagram
-
only linear, double-stranded DNA is a substrate for SsnA
-
-
?
salmon sperm DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
single-stranded circular DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for single-stranded regions
-
?
single-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
single-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
preferred substrate
-
?
ssDNA + H2O
?
show the reaction diagram
-
-
-
?
supercoiled DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P24855
in presence of Mg2+ and Ca2+ under neutral conditions
production of 3'-OH and 5'-phosphate ends
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
superhelical form converted to circular-relaxed and linear forms
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
-
-
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 + ?
show the reaction diagram
-
-
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 + ?
show the reaction diagram
-
-
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 + ?
show the reaction diagram
-
-
formation of a relaxed circle that subsequently converts to linear DNA if it is nicked on the other strand at the same position
?
supercoiled pUC18 DNA + H2O
?
show the reaction diagram
-
endolytically cleavage generating single base nicks
-
?
Xenopus laevis DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
Acinetobacter baumannii, Acinetobacter baumannii ATCC19606T
-
degrades chromosomal DNA with the characteristic DNA ladders and induces apoptosis of Xenopus embryos
-
-
?
linearized plasmid-DNA + H2O
5'-phosphooligonucleotides + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
-
no activity with homo-oligomers of dA, dC, dG and annealed homo-oligomers of dA/dT, no activity with RNA
-
?
additional information
?
-
-
substrate specificity, 5'-AMP, bis(4-nitrophenyl)phosphate, and 4-nitrophenyl phosphate are no substrates, preferential liberation of 5'-deoxy-GMP, no cleavage of C-linkages, (dC)10 is no substrate, no liberation of 5'-deoxy-CMP
-
?
additional information
?
-
P24855
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
-
enzyme is an integral component of the larval digestive system, enzyme plays an important role in the conversion of the insecticidal crystal protein from Bacillus thuringiensis to the active DNA-free toxin in the larval gut, purified enzyme acts synergistically with the toxin
-
?
additional information
?
-
Q90WM1
phylogenetic analysis
-
?
additional information
?
-
Q90W31
phylogenetic analysis
-
?
additional information
?
-
Bufo vulgaris japonicus
Q90WM0
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
Q767J3
phylogenetic analysis
-
?
additional information
?
-
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
-
additional information
?
-
-
presence of DNase I hypersensitve sites at the 5' and/or 3' ends of most genes irrespective of their expression levels. Hypersensitive sites occur near cis-regulatory elements in the promoters of these genes and participate in the translational regulation by enhancing the access of chromatin remodeling factors and/or transcription factors to their target sites
-
-
-
additional information
?
-
O55070
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
-
additional information
?
-
-
OmpA is a potential virulence factor involved in the induction of host cell death. Acinetobacter baumannii can secrete OmpA during colonization and infection. The pathogenic strategy is that OmpA translocates into the nuclei of host cells and degrades chromosomal DNA by DNAse I-like enzymatic activity
-
-
-
additional information
?
-
-
genome-wide mapping of DNase I hypersensitive sites in the multicellular model organism Caenorhabditis elegans by a high-resolution tiling array. Distribution of DNase I hypersensitive sites is strongly associated with functional elements in the genome
-
-
-
additional information
?
-
-
immunization of healthy rabbits with bovine DNase I produces IgGs with intrinsic DNase and RNase activities
-
-
-
additional information
?
-
-
interaction of DNase I with yeast transfer RNA alters protein secondary structure with major reduction of the alpha-helix, and increases the random coil, beta-anti and turn structures, while tRNA remains in the A-conformation. No digestion of tRNA by DNase I in the protein-tRNA complexes
-
-
-
additional information
?
-
-
postnatal spermatogonia show higher sensitivity to DNase-I digestion than isolated Sertoli cells or MSC-1 Sertoli cell line
-
-
-
additional information
?
-
Caenorhabditis elegans N2
-
genome-wide mapping of DNase I hypersensitive sites in the multicellular model organism Caenorhabditis elegans by a high-resolution tiling array. Distribution of DNase I hypersensitive sites is strongly associated with functional elements in the genome
-
-
-
additional information
?
-
Acinetobacter baumannii ATCC19606T
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
degradation of DNA from supernumerary spermatozoa which enter the ovum durig polyspermic fertilisation in birds
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
-
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
double-strand breaks occure more rapidly in the presence of Ca2+
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
DNase I hypersensitive sites of chromatin near the 5'-ends of some genes, necessary for transcription by RNA polymerase II
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
preference for single-stranded and supercoiled DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
introduces preferentially breaks on the 5' side of dT
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
involved in seed sprouting
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
functionally active during digestion, participation in the repair of damaged DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
involved in DNA degradation during apoptosis
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
predominantly by a single-stranded nicking mechanism in the presence of both Ca2+ and Mg2+
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
cleaves both strands of a double helix at or near the same level, about 400 nucleotides removed at each endonucleolytic scission, causes a "shattering" at the point of cleavage, leading to the libration of small oligonucleotides by an exonucleolytic mode of attack
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
hydrolysis of both double- and single-stranded DNA
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
P24855
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q90WM1
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Q90W31
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
Bufo vulgaris japonicus
Q90WM0
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
dsDNA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
P24855
DNase I is not involved in aopoptosis, but DNase lambda is
-
?
additional information
?
-
-
enzyme is an integral component of the larval digestive system, enzyme plays an important role in the conversion of the insecticidal crystal protein from Bacillus thuringiensis to the active DNA-free toxin in the larval gut, purified enzyme acts synergistically with the toxin
-
?
additional information
?
-
Q90WM1
phylogenetic analysis
-
?
additional information
?
-
Q90W31
phylogenetic analysis
-
?
additional information
?
-
Bufo vulgaris japonicus
Q90WM0
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
Q767J3
phylogenetic analysis
-
?
additional information
?
-
-
exogenous DNA transferred to the oocyte by spermatozoa during sperm mediated gene transfer in vitro fertilisation protocol is protected from DNase I degradation and persists in the ooplasm till 6 h
-
-
-
additional information
?
-
-
presence of DNase I hypersensitve sites at the 5' and/or 3' ends of most genes irrespective of their expression levels. Hypersensitive sites occur near cis-regulatory elements in the promoters of these genes and participate in the translational regulation by enhancing the access of chromatin remodeling factors and/or transcription factors to their target sites
-
-
-
additional information
?
-
O55070
DNase1 and DNase1/3 may substitute or cooperate with each other during DNA degradation, providing effective clearance after exposure or release from dying cells
-
-
-
additional information
?
-
Acinetobacter baumannii, Acinetobacter baumannii ATCC19606T
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
can substitute for Ca2+, but less effective
Ba2+
-
-
Ca2+
-
stabilizing enzyme structure
Ca2+
-
22% stimulation at 10 mM
Ca2+
-
in the presence of 3 mM Mg2+, activation at 2 mM
Ca2+
-
addition of Ca2+ stabilizes the enzyme, facilitates second cut in double-stranded DNA
Ca2+
-
in presence of Ca2+ less sensitive to buffer strength
Ca2+
-
activation at 1 mM
Ca2+
-
stimulation
Ca2+
-
stimulation at 1 mM
Ca2+
-
2 Ca2+ bound to the enzyme under crystallization conditions
Ca2+
-
activation at 0.1 mM; activation synergistic with Mg2+
Ca2+
-
activation synergistic with Mg2+; resistance to proteolysis conveyed by Ca2+
Ca2+
-
Ca2+-binding causes a conformational change that maintains a more active structure of the enzyme
Ca2+
-
activation synergistic with Mg2+
Ca2+
-
required for stability
Ca2+
-
activation synergistic with Mg2+
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+
Bufo vulgaris japonicus
Q90WM0
essential, binding site characterization
Ca2+
-
essential, binding site characterization
Ca2+
Q90WM1
essential, binding site characterization
Ca2+
Q90W31
essential, binding site characterization
Ca2+
P24855
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Ca2+
Q5KTT1
activates
Ca2+
O42446
activates
Ca2+
Q5KTT0
activates
Ca2+
-
activates
Ca2+
-
activates, transition state metal ions also activate, but are less effective
Ca2+
Q8JIP7
activates
Ca2+
Q767J3
activates
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+
-
required
Ca2+
-
highest activity at 5 mM, but only 50% activtiy compared to Mg2+
Ca2+
-
1 mM optimal concentration
Ca2+
-
required
Ca2+
-
required
Ca2+
-
required
Ca2+
-
required
Ca2+
-
in the absence of Ca2+, but with Mg2+ the DNase cleaved the substrate DNA in a single nicking mode
Ca2+
-
or Mg2+, required
Ca2+
-
two Ca2+ ions that stabilize surface loops as well as an additional metal ion binding site at the active site
Ca2+
-
exhibits divalent cation-dependent endonuclease activity
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+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Cd2+
-
-
Co2+
-
absolute requirement for Mn2+ or Mg2+
Co2+
-
22% stimulation at 10 mM
Co2+
-
activation at 10 mM
Co2+
-
can substitute for Mg2+, but only 10% efficiency
Co2+
-
-
Co2+
-
reaction performs mainly double strand scissions, Co2+ is a better activator than other divalent metals
Co2+
P24855
activates
Co2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
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+
-
absolute requirement for Mg2+ or Mn2+
Mg2+
-
required for stabilizing the enzyme structure
Mg2+
-
highest activity at 10 mM, doubled activity upon addition of 1 mM Ca2+
Mg2+
-
22% stimualtion at 10 mM
Mg2+
-
-
Mg2+
-
highest activity at 2 mM
Mg2+
-
in the presence of 2 mM Ca2+, activation at 3 mM
Mg2+
-
activation at 10 mM, 2fold activation, if 1 mM CaCl2 is added
Mg2+
-
presence of Mg2+ alone leads to cutting only one of the two strands
Mg2+
-
absolute requirement for activity, highest activity if both Mg2+ and Ca2+ are present
Mg2+
-
5% activation; activation synergistic with Ca2+
Mg2+
-
activation synergistic with Ca2+
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+
-
2.0-7.5 mM for DNases A, B or C
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
activation synergistic with Ca2+; optimal concentration 5 mM
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
activation synergistic with Ca2+
Mg2+
-
-
Mg2+
-
only single strand cleavage occurs during the lag period of the reaction if only Mg2+ is present
Mg2+
-
dependent on, can be replaced by Mn2+
Mg2+
Bufo vulgaris japonicus
Q90WM0
-
Mg2+
Q90WM1
-
Mg2+
Q90W31
-
Mg2+
P24855
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Mg2+
Q5KTT1
activates
Mg2+
O42446
activates
Mg2+
Q5KTT0
activates
Mg2+
-
activates
Mg2+
-
best activator, transition state metal ions also activate, but are less effective
Mg2+
Q8JIP7
activates
Mg2+
Q767J3
activates
Mg2+
Q9YGI5
half-maximal activation at 4 mM
Mg2+
-
dependent on
Mg2+
-
essential cofactor for activity and structural integrity
Mg2+
-
either Mg2+ or Mn2+ is required in addition to Ca2+
Mg2+
P21704
either Mg2+ or Mn2+ is required in addition to Ca2+
Mg2+
-
highest activity at 5 mM
Mg2+
-
10 mM optimal concentration
Mg2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
Mg2+
-
required
Mg2+
-
highest activity at 2.5 mM
Mg2+
-
or Ca2+, required
Mg2+
-
DNA fragmentation by digestion with DNase I in the presence of Mg2+ followed by blunting with the Klenow fragment improves the yield of small DNA fragments by 4fold as compared to the reaction with DNase I in the presence of Mn2+. In the case of using Mg2+ as a cofactor, DNase I attacks each strand of dsDNA independently
Mg2+
O55070
-
Mg2+
-
exhibits divalent cation-dependent endonuclease activity
Mg2+
-
required
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+
MgCl2
Potyvirus sp.
-
-
Mn2+
-
employs more of the cutting mechanism of supercoiled plasmid-DNA
Mn2+
-
highest activity at 1 mM, addition of Ca2+ doesn't change activity
Mn2+
-
22% stimulation at 10 mM
Mn2+
-
highest activity at 2 mM
Mn2+
-
increasing activation up to 30 mM
Mn2+
-
activation at 10 mM
Mn2+
-
most active
Mn2+
-
-
Mn2+
-
can substitute for Mg2+
Mn2+
-
most active, faster production of linear form of supercoiled DNA
Mn2+
-
0.8-2.5 mM for DNases A, B or C
Mn2+
-
-
Mn2+
-
120% activity of Mg2+ activated enzyme at 10 mM
Mn2+
-
less active than Mg2+
Mn2+
-
reaction performs mainly double strand scissions
Mn2+
-
dependent on, can be replaced by Mg2+
Mn2+
P24855
activates
Mn2+
-
activates
Mn2+
Q767J3
activates
Mn2+
Q9YGI5
half-maximal activation at 1 mM
Mn2+
-
activates
Mn2+
-
either Mg2+ or Mn2+ is required in addition to Ca2+
Mn2+
P21704
either Mg2+ or Mn2+ is required in addition to Ca2+
Mn2+
-
highest activity at 5 mM
Mn2+
-
5 mM Mg2+, Mn2+ or Co2+ together with Ca2+ required
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+
O55070
activity of recombinant DNase1 in the presence of Mn2+ is increased only slightly, whereas recombinant DNase1/3 displays strongly enhanced nucleolysis
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
NaCl
-
activates at concentrations up to 40 mM
NaCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
NaCl
-
highest activity at 100 mM
Sr2+
-
can substitute for Ca2+, but less effective
Sr2+
-
-
Zn2+
-
peaked activity at 0.1 mM
Zn2+
-
-
Zn2+
-
-
Zn2+
-
highest activity at 5 mM, but only 40% activtiy compared to Mg2+
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
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
-
divalent alkaline metal ion requirement
additional information
Q767J3
divalent cations are absolutely required for activity
additional information
-
metal-dependent enzyme
additional information
-
metal binding and influence on activity, wild-type and mutant enzymes, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(4-amidinophenyl)-6-indolecarbamidine
-
significantly inhibits DNase I activity
2-mercaptoethanol
-
inhibition, but reversal by addition of 3 mM CaCl2
2-mercaptoethanol
-
inhibition after treatment with EGTA
2-mercaptoethanol
-
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
2-mercaptoethanol
-
70% inhibition at 1 mM
2-mercaptoethanol
Q9YGI5
slight inhibition
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-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
5'-deoxy-GMP
-
competitive, product inhibition
actin
-
40 mM HEPES pH 7.0, 5 mM MgCl2, 1 mM CaCl2
actin
P49183
inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage
actin
-
inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone
actin
-
inhibits the DNA-nicking activity of DNAse I/CdtB chimera
Aflatoxin B2a
-
non-competitive inhibitor
Aflatoxin G2
-
non-competitive inhibitor
Aflatoxin G2a
-
non-competitive inhibitor
Aflatoxin M1
-
non-competitive inhibitor
Aprotinin
O55070
inhibits DNase1 as a result of plasmin inhibition
aurintricarboxylic acid
P24855
i.e ATA, a general inhibitor of nucleases, weak inhibition
Bile acids
-
inhibit the enzyme in concert with cholesterol sulfate
Ca2+
-
inhibitory above 1 mM
Ca2+
-
complete inhibition at 1-10 mM
Ca2+
-
80% inhibition at 0.1 mM
Ca2+
-
slight inhibition of mutant D201A
calf spleen inhibitor protein II
-
molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7
-
calf thymus inhibitor protein
-
molecular weight: 49000 Da, maximum stability at pH 6
-
carbodiimide
-
presence of divalent cations slows the rate of inactivation
Cholesterol sulfate
-
from human gastric fluid, the sulfate group and the hydrophobic side chain of cholesterol sulfate are indispensable for the inhibitory effect, irreversible, dependent on bile acids, a ratio of 342:1 of bile acids to cholesterol sulfate is required for complete inhibition
Cu-iodoacetate
-
at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min
Cu2+
-
complete inhibition
Cu2+
-
complete inhibition at 1-10 mM
dithiothreitol
-
-
DTT
-
80% inhibition at 1 mM
E2-immunity protein
-
complete inhibition of activity on plasmid DNA
-
EDTA
-
complete inhibition at 10 mM
EDTA
-
-
EDTA
-
50% inhibition at 0.3 mM
EDTA
-
slight inhibition
EDTA
-
complete inhibition at 20 mM
EDTA
Q767J3
complete inhibition at 20 mM
EDTA
-
-
EDTA
P21704
-
EDTA
-
complete inhibition at 1 mM
EDTA
-
complete ihibition at 1 mM; complete inhibition at 1 mM
EDTA
-
complete inhibition at 1 mM
EDTA
Potyvirus sp.
-
inhibition observed above 50 microM, complete inhibition at 0.5 mM
EDTA
-
complete inhibition at 5 mM
EDTA
-
10 mM, complete loss of activity
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
EGTA
-
-
EGTA
-
complete inhibition at 10 mM
EGTA
-
inhibition at 1 mM
EGTA
-
activity inhibited
EGTA
-
inhibition at 0.01 mM in the presence of 2.5 mM Mg2+
EGTA
-
activity inhibited
EGTA
-
activity inhibited
EGTA
-
-
EGTA
P21704
complete inhibition of the enzyme from serum at 5 mM
EGTA
-
-
EGTA
Q767J3
complete inhibition at 5 mM
EGTA
P21704
-
EGTA
-
complete inhibition at 1 mM
EGTA
-
complete ihibition at 1 mM; complete inhibition at 1 mM
EGTA
-
complete inhibition at 1 mM
EGTA
-
1 mM, complete loss of activity
G-actin
-
inhibition with actin-gelsolin segment I complex
-
G-actin
-
50% inhibition at 0.002 mg/ml
-
G-actin
-
-
-
G-actin
-
complete inhibition at 0.05 mg/ml
-
G-actin
-
DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity
-
G-actin
-
15% inactivation at 0.004 mg
-
G-actin
-
66% inhibition in an 1:1 molar ratio of DNase I-actin complex
-
G-actin
-
complete inhibition at 0.001 mg
-
G-actin
P24855
specific, strong inhibition
-
G-actin
-
slight inhibition
-
G-actin
P21704
-
-
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
-
gamma-actin
-
-
-
gamma-actin
-
-
-
guanidinium hydrochloride
-
over 80% inhibition at 0.5 M
heparin
-
-
heparin
-
directly inhibits recombinant DNase1/3
heparin
O55070
directly inhibits recombinant DNase1/3
iodoacetate
-
50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min
iodoacetate
-
complete inhibition
iodoacetate
-
inhibition in the presence of Mn2+ or Ca2+ at pH 7.2
iodoacetate
-
complete inhibition
iodoacetate
-
formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
iodoacetate
Q9YGI5
strong inhibition in presence of Cu2+
K+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
KCl
-
less inhibitory than NaCl
KCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
mannitol
-
inhibition of enzyme activity during the entire growth period of seedlings
mannitol
-
induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days
methanesulfonylchloride
-
inactivation at pH 5.0
N-bromosuccinimide
-
inactivation by modification at Trp155
N-bromosuccinimide
-
modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
Na+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
NaCl
-
10fold lower activity at 150 mM
NaCl
-
50% inhibition at 60 mM, mutated enzyme less sensitive against increased salt concentrations
NaCl
-
inhibitory at concentrations below 100 mM
NaCl
-
decreasing activity with increasing ionic strength
NaCl
-
-
NaCl
-
Na-DNA is inhibitory
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
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
NaCl
O55070
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)
Ni2+
P24855
-
oligonucleotides
-
competitive inhibition
plasmin
O55070
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
-
protein Im9
-
an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell
-
RNA
-
enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA
SDS
-
-
SDS
-
over 80% inhibition at 0.04% w/v
Somatostatin
P21704
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
O55070
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
-
-
Tris-HCl buffer
-
inhibition at high concentration
Trypsin
-
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
-
Urea
-
20% inhibition at 4 M
Zn2+
-
inhibition at millimolar concentrations
Zn2+
-
complete inhibition
Zn2+
-
complete inhibition at 1-10 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
-
Zn2+
P21704
-
Zn2+
-
-
additional information
Bufo vulgaris japonicus
Q90WM0
no inhibition by G-actin
-
additional information
-
no inhibition by G-actin
-
additional information
Q90WM1
no inhibition by G-actin
-
additional information
Q90W31
no inhibition by G-actin
-
additional information
-
no inhibition by sulfatides and membrane lipids, galactose ceramide, no inhibition by steroid sulfates such as estrone sulfate, pregnenolone sulfate, dehydroepiandrosterone sulfate, no inhibition by DMSO, Tween 20, sodium cholate, and sodium taurocholate
-
additional information
-
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
-
the phosphate residue is responsible for the inhibitory effect of guanosine 5'-nucleotides
-
additional information
Q9YGI5
resistant to trypsin inactivation in absence of Ca2+
-
additional information
-
is resistant to trypsin
-
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 125C are 37% and the activities after heating to 210C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I
-
additional information
O55070
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20C to thawing to room temperature and subsequently stored at 4C, it looses its DNase1/3-like activity within 2 weeks
-
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
-
DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
-
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
-
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
O55070
activates DNase1/3-like activity
Bile
-
bile from rat , reconstitution of activity of inhibited DNase I-actin complex
-
Bovine serum albumin
-
0.01 mg/reaction volume stimulates about 50% at both pH 6.2 and 7.7
-
dithiothreitol
-
-
heparin
O55070
activates DNase1
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
-
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
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
-
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, 37C
0.0042
d(pA)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0053
d(pApCpTpApCpApGpTpCpTpApCpA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0072
d(pGpGpCpApCpTpTpApC)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0056
d(pT)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0037
d(pTpApGpApApGpApTpCpApApA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
additional information
Double-stranded DNA
-
20 microgram/ml; values in microgram DNA/ml
additional information
Double-stranded DNA
-
25 microgram/ml; values in microgram DNA/ml
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
167
(pC)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
493.3
(pC)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
106.6
d(pA)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
703.3
d(pApCpTpApCpApGpTpCpTpApCpA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0492
d(pGpGpCpApCpTpTpApC)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
453.3
d(pGpGpCpApCpTpTpApC)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
713
d(pT)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
136.6
d(pTpApGpApApGpApTpCpApApA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0314
additional information
Potyvirus sp.
-
37C, 20 mM Tris-HCl pH 8.3, 1 mM MgCl2
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
5'-deoxy-GMP
-
pH 8.5, 37C
0.0058
5'-GDP
-
pH 8.5, 37C
0.0283
5'-GMP
-
pH 8.5, 37C
0.0028
5'-GTP
-
pH 8.5, 37C
0.00091
actin
-
-
0.0000013
gamma-actin
-
-
-
additional information
additional information
P24855
-
-
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
-
-
0.096
-
as plasmid nicking activities in the presence of both Mg2+ and Ca2+
14.2
-
-
531
-
mutant G100K/E102P/S103G/G105W, pH 7.0
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
1009
-
wild-type, pH 7.0
1020
-
mutant G100W/E102/G/S103P/G105K, pH 7.0
1092
-
mutant E102G/S103P, pH 7.0
3600
-
pH 6.5
14540
-
purified enzyme, substrate RNA
597200
-
purified enzyme, substrate ssDNA
additional information
-
908 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
670 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
5100 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
1683 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
21 units/min/ng DNA digested
additional information
-
1683 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
938 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
222 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
320 units/mg protein; units defined as absorbance at 260 nm/ml assay solution
additional information
-
400 units/mg protein
additional information
-
5'-exonuclease, 3'-exonuclease and DNA-binding activities of wild-type and truncated mutants and mutant H371A
additional information
-
-
additional information
Bufo vulgaris japonicus
Q90WM0
purified enzyme
additional information
-
purified enzyme
additional information
Q90WM1
purified enzyme
additional information
Q90W31
purified enzyme
additional information
-
purified enzyme
additional information
-
purified enzyme
additional information
O42446
purified enzyme
additional information
Q5KTT0
purified enzyme
additional information
-
RT-PCR-based and immunohistochemic detection and quantification
additional information
-
RT-PCR-based immunohistochemic detection and quantification
additional information
-
purified enzyme
additional information
Q767J3
purified enzyme
additional information
Q9YGI5
purified isozymes A and B
additional information
-
-
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
-
in 33 mM sodium phosphate buffer
5.5
-
in 33 mM acetate buffer, 6 times faster than in phosphate buffer
5.8
-
in the presence of Mg-EGTA
6 - 8
Q5KTT0
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
-
in the presence of Mg2+, dependent on bivalent metal ions
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
-
-
6.5
-
in the presence of 10 mM MgCl2
6.5
-
DNase I type-2 enzyme
6.75
-
DNase I type-1 enzyme
6.8
P24855
DNase I
7 - 8
Q9YGI5
depending on the metal ion used
7
-
with 5 mM Mg2+
7
-
serum DNase I in the presence of Mg2+ and Ca2+
7
-
in the presence of Mg2+, pH optima dependent on bivalent metal ions
7
-
assay at
7.2 - 7.6
-
in 33 mM Tris-HCl buffer
7.2
-
with 5 mM Mn2+
7.5 - 8.5
-
-
7.5
-
-
7.5
-
in the presence of Mn2+ in 50 mM Tris-HCl buffer
7.5
-
for pancreas DNase I in the presence of Mg2+ and Ca2+
7.5
-
in the presence of Mn2+, different pH-optima, dependent on bivalent metal ions
7.5
-
assay at
7.5
-
assay at
7.7
-
in 25 mM Tris-HCl and 1 mM Mn2+
7.8
-
-
8
Bufo vulgaris japonicus
Q90WM0
bell-shaped optimum
8
-
bell-shaped optimum
8
Q90WM1
bell-shaped optimum
8
Q90W31
bell-shaped optimum
8
Q5KTT1
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
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
8
O42446
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
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
8
-
assay at
8.2
-
-
8.25
-
for DNase A
8.5
-
in the presence of Mg2+
8.5
-
for DNase B
8.75
-
for DNase C
9
-
assay at
additional information
P24855
DNase I is a neutral enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
O55070
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
-
-
8
Potyvirus sp.
-
best activity above pH 8.0
9.5 - 12
-
pH activity profile
additional information
-
sensitive to low pH, Asn110 is responsible
additional information
-
no activity at acidic pH, e.g. pH 4.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Q9YGI5
assay at
37
-
assay at
37
-
assay at
37
P24855
assay at
37
-
assay at
37
-
assay at
37
Q5KTT1
assay at
37
-
assay at
37
O42446
assay at
37
Q5KTT0
assay at
37
-
assay at
37
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 60
-
activity remains unchanged
50
-
stable up to
60
-
85% loss of activity after 5 min, complete inactivation after 10 min
60
-
rather stable up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
pI values vary from 3.5-4.3 due to single nucleotide polymorphism
4.43
Q9YGI5
isozyme B, isoelectric focusing
4.56
Q9YGI5
isozyme A, isoelectric focusing
4.9
O55070
DNase1
6.8
-
isoelectric focusing
8.7
O55070
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
leukemic cells
Manually annotated by BRENDA team
Potyvirus sp.
-
-
Manually annotated by BRENDA team
-
multi-drug resistant cell line
Manually annotated by BRENDA team
-
embryonic brain
Manually annotated by BRENDA team
-
mid-previtellogenesis epithelium and late previtellogenesis epithelium
Manually annotated by BRENDA team
-
pars glandularis
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
highest enzyme expression and activity
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Q767J3
low activity
Manually annotated by BRENDA team
-
poor activity
Manually annotated by BRENDA team
P24855
high expression level
Manually annotated by BRENDA team
P21704
somatostatin-resistant enzyme form
Manually annotated by BRENDA team
O55070
high DNase1 content
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Q767J3
low activity
Manually annotated by BRENDA team
-
poor activity
Manually annotated by BRENDA team
P21704
somatostatin-resistant enzyme form
Manually annotated by BRENDA team
-
highest activity in vitellogenic, activity increases during oogenesis, low activity in young oocytes
Manually annotated by BRENDA team
-
MII oocyte
Manually annotated by BRENDA team
Q90WM1
high activity
Manually annotated by BRENDA team
Q90W31
high activity
Manually annotated by BRENDA team
Bufo vulgaris japonicus
Q90WM0
high activity
Manually annotated by BRENDA team
-
poor activity
Manually annotated by BRENDA team
Q767J3
highest enzyme activity and expression
Manually annotated by BRENDA team
P24855
very high expression level
Manually annotated by BRENDA team
-
from homozygote subjects
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
P21704
somatostatin-resistant enzyme form
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
O55070
contains two nucleases, DNase1 and DNase1/3. DNase1/3 is not N-glycosylated, whereas DNase1 is di-N-glycosylated
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
systemic lupus erythematosus patients have lower serum DNase 1 activity compared with healthy controls
Manually annotated by BRENDA team
Q90W31
low activity
Manually annotated by BRENDA team
Bufo vulgaris japonicus
Q90WM0
low activity
Manually annotated by BRENDA team
P24855
high expression level
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
O55070
high DNase1/3 content
Manually annotated by BRENDA team
P21704
somatostatin-sensitive enzyme form
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
10 phenotypes
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
no activity in brain
Manually annotated by BRENDA team
additional information
Q90WM1
no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine
Manually annotated by BRENDA team
additional information
Q90W31
no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine
Manually annotated by BRENDA team
additional information
Bufo vulgaris japonicus
Q90WM0
no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine
Manually annotated by BRENDA team
additional information
-
no activity in cerebrum, heart, lung, liver, kidney, spleen, skin, muscle, oesophagus, stomach, duodenum, and large intestine
Manually annotated by BRENDA team
additional information
-
no activity in spleen, heart, lung, stomach, large intestine, cerebrum, cerebellum, submaxillary gland, and thymus
Manually annotated by BRENDA team
additional information
Q767J3
no activity in spleen, parotid gland, lung, heart, cerebellum, and cerebrum
Manually annotated by BRENDA team
additional information
-
secretion of enzyme is controlled by the chief cells in the stomach
Manually annotated by BRENDA team
additional information
P24855
tissue distribution of enzymes of the DNase I family, complete overview
Manually annotated by BRENDA team
additional information
-
marked correlation between tissue distribution of enzyme and its sensitivity/resistance to proteolysis
Manually annotated by BRENDA team
additional information
-
a fraction of abzymes from autoimmune patients hydrolyzing both DNA and RNA can contain a subfraction of antibodies against DNase I
Manually annotated by BRENDA team
additional information
-
EG-1 cell
Manually annotated by BRENDA team
additional information
-
pancreas-parotid
Manually annotated by BRENDA team
additional information
-
pyriform cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secreted into duodenal juice
-
Manually annotated by BRENDA team
-
secreted into pancreatic juice
-
Manually annotated by BRENDA team
-
secreted into the culture medium
-
Manually annotated by BRENDA team
-
secreted into urine
-
Manually annotated by BRENDA team
-
secreted into urine
-
Manually annotated by BRENDA team
-
activity 6 times higher than in cytoplasm
Manually annotated by BRENDA team
-
DNase I digestion in interphase nuclei
Manually annotated by BRENDA team
Acinetobacter baumannii ATCC19606T
-
-
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
additional information
Acinetobacter baumannii ATCC19606T
-
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
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
-
SDS-PAGE
134209
14000
-
SDS-PAGE
134209
16000 - 17000
-
gel filtration, SDS-PAGE
134224
17000
-
SDS-PAGE
665370
22000
-
gel filtration
134209
22400
-
gel filtration
666780
25000
-
mature form after cleavage of the signal peptide
664707
28000
-
SDS-PAGE
134205
29000
-
SDS-PAGE
134199
29800
O55070
calculated molecular mass of DNase1
697891
30000
-
gel filtration, SDS-PAGE, thin-layer IEF, MS analysis
134201
30000
-
gel filtration, SDS-PAGE
134230
30000
-
calculated from sequence
664148
30070
-
calculated from amino acid and carbohydrate composition for DNase A
134220
31000
-
-
134208
31000
-
SDS-PAGE
134226
31000
-
amino acid analysis
134238
31000
-
SDS-PAGE
664654
32000
-
SDS-PAGE, gel filtration
134203
32000
-
SDS-PAGE
134215
32000
-
gel filtration, sucrose density gradient centrifugation
134216
32000
-
SDS-PAGE, gel filtration
134231
32000
-
SDS-PAGE
664154
33000 - 38000
-
for serum and pancreas DNase I, gel filtration
134225
33000
-
sucrose density gradient centrifugation, gel filtration
134218
33000
Q5R2I2
SDS-PAGE, gel filtration
664833
33100
O55070
calculated molecular mass of DNase1/3
697891
34000
-
SDS-PAGE
134197
34000
-
-
134198
34000
-
SDS-PAGE
134204
34000
-
SDS-PAGE, gel filtration
134207
34000
-
SDS-PAGE
134211
34000
-
SDS-PAGE
134215
34000
O55070
DNase1/3, by DPZ
697891
35000
-
SDS-PAGE
664154
36000
-
gel filtration
134212
37000
O55070
DNase1, by DPZ
697891
38000
-
gel filtration
134228
40000
Bufo vulgaris japonicus
Q90WM0
gel filtration
649715
40000
-
gel filtration
649715
40000
Q90WM1
gel filtration
649715
40000
Q90W31
gel filtration
649715
41000
-
SDS-PAGE, gel filtration
134214
41000
-
gel filtration
651077
80000
-
SDS-PAGE
664146
108000
-
SDS-PAGE, the pre-mature DNase contains a signal peptide and has an molecular weight of 112000
665170
345000
-
SDS-PAGE
664154
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
?
-
x * 32000, SDS-PAGE
?
-
x * 23000, SDS-PAGE
?
-
x * 33000, SDS-PAGE
?
Q9YGI5
x * 30000, SDS-PAGE, x * 30859, isozyme A, mass spectrometry, x * 30882, isozyme B, mass spectrometry
?
P24855
x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation
dimer
-
2 * 28000, gel filtration
dimer
-
1 * 12000 and 1 * 14000, gel filtration, SDS-PAGE
dimer
-
2 * 17000, gel filtration
heterotrimer
-
CdtB/DNAse I, but not DNAseI/CdtB
monomer
-
-
monomer
Q90WM1
1 * 40000, SDS-PAGE
monomer
Q90W31
1 * 40000, SDS-PAGE
monomer
Bufo vulgaris japonicus
Q90WM0
1 * 40000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 34000, SDS-PAGE
monomer
-
1 * 34000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE, gel filtration
monomer
-
1 * 16000-17000, four active fractions
monomer
-
1 * 32000, SDS-PAGE, gel filtration
monomer
-
1 * 32000, SDS-PAGE, gel filtration
monomer
-
1 * 32000, SDS-PAGE, gel filtration
monomer
-
four active fractions, gel filtration, SDS-PAGE
monomer
-
1 * 30000, deglycosylated enzyme, SDS-PAGE, 42000-47000, glycosylated enzyme, SDS-PAGE
monomer
-
1 * 34500, SDS-PAGE, gel filtration
monomer
-
1 * 35000, SDS-PAGE, gel filtration
additional information
Q90WM1
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
Q90W31
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
Bufo vulgaris japonicus
Q90WM0
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
-
the enzyme is divided into a catalytic domain and a DNA-binding domain
additional information
P49183
interaction of enzyme with actin and inhibition by actin. Inhibition may serve as a self-protection mechanism against premature DNA degradtion during cell damage
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
15% carbohydrate content
glycoprotein
-
2 N-acetylglucosamine proximal to the carbohydrate chain at Asn18, followed by a variable number of mannose residues
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
no glycoprotein
Bufo vulgaris japonicus
Q90WM0
-
glycoprotein
Q767J3
1 potential N-glycosylation site
glycoprotein
-
-
no glycoprotein
-
-
no glycoprotein
-
-
glycoprotein
-
3.4% carbohydrate content
glycoprotein
-
protein contains a N-linked carbohydrate moiety. Potential glycosylation sites at N18 and N106
glycoprotein
Q9YGI5
binds to concanavalin A, contains an N-glycosylation site
glycoprotein
-
-
glycoprotein
-
contains fucose, mannose, galactose, glucosamine, sialic acid
glycoprotein
-
phosphoglycoprotein
glycoprotein
P24855
enzyme contains 2 potential N-glycosylation sites
glycoprotein
-
11.8% carbohydrate content
proteolytic modification
P24855
enzyme sequence contains a precursor peptide
glycoprotein
-
carbohydrate-chain at Asn 18
glycoprotein
-
-
no glycoprotein
Q90WM1
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
contains fucose, mannose, galactose, glucosamine, sialic acid
glycoprotein
-
-
glycoprotein
-
2 carbohydrate side-chains attached at Asn18 and Asn106
no glycoprotein
Q90W31
-
glycoprotein
-
DNase A with a neutral carbohydrate side-chain, DNase B with a sialic acid carbohydrate side-chain
additional information
-
protein exhibits one large essential (C173-C209) disulfide loop and one small non-essential (C101-C104) disulfide loop
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.5 A resolution, alpha-beta-protein, carbohydrate attached to Asn18, active centre close to His 131; complex between DNase I and uncleaved octamer duplex DNA, 2.3 A resolution
-
at 2 A resolution
-
complex between DNase I and uncleaved octamer duplex DNA, 2.3 A resolution; H134 and H252 involved in catalysis
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
activity completely lost
134215
5 - 9
-
stable within the range for 24 h at 4C
134214
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-30
-
no loss of activity in crude extract
134216
-20
-
stable for 1 month
134228
0
-
stable for 7 days
134230
4
-
stable for one week, when concentration is greater than 3000 U/ml
134205
4
-
no activity
134206
45
-
stable up to, more stable up to 60C, if Ca2+ is present
134207
45
-
stable up to at pH 6.5, loss of activity at 60C
134214
55
-
inactivation after 10 min incubation
134201
60
-
stable for 20 min
134209
60
-
15 min, stable
651077
65
-
inactive above 65C
666854
70
Q9YGI5
inactivation above
653044
100
-
DNAse I DNA nicking-activity is less than 50% of the control after 5 min of heating
697988
additional information
-
both N-linked glycosylation sites N18 and N106 are required for heat stability
696832
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 125C are 37% and the activities after heating to 210C are ca. 8%
697759
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ is able to protect DNase completely against inactivation by trypsin
-
extremely sensitive to inactivation by proteases in the absence of Ca2+
-
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance
-
sensitives to repeated freezing and thawing
-
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance
-
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
-
less active in phosphate buffer
-
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
-
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 0C
formamide
-
stable to at 50% v/v
Glycerol
-
10% glycerol v/v protects against inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 5 mM CaCl2, 30% polyethylene glycol, 4 weeks
-
37C, protease free preparation, absence of Ca2+, pH 8.0, more than 10 days
-
-20C, 20 mM Tris-HCl, pH 7.5, 5 mM CaCl2, 10% v/v glycerol, 6 months
-
-70C, 10 mM Tris/HCl, pH 7.4, 50% v/v glycerol, 2 years
-
4C, 0.1 M sodium phosphate, pH 7.0, 0.2 M NaCl, 2 months
-
-20, 50 mM Tris-HCl 10 mM 2-mercatpoethanol 100 mM NaCl 10 mM EDTA 50% glycerol, several months, minimal loss of activity
-
-20C, 10 mM Tris-HCl, pH 7.5, 5 mM CaCl2, 30% polyethylene glycol, more than 3 months
-
-20C, 10 mM Tris-HCl, pH 7.0, 10 mM KCl, 5 M urea, 6 months
-
-20C, 20 mM Tris-HCl, pH 7.5, 30% glycerol, 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10000fold from pancreas
Q5KTT1
6057fold to homogeneity
-
by chromatography on hydroxylapatite
-
commercial preparation
-
conconavalin A-agarose as an effective step for DNases with neutral carbohydrate side-chains, preparing a protease free DNase I
-
high homogeneity by chromatography steps
-
near homogeneity by isoelectric focusing and gel filtration
-
overexpressed enzyme
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
to homogeneity
-
1300fold from pancreas
Bufo vulgaris japonicus
Q90WM0
260fold from pancreas, to homogeneity
Q767J3
near homogeneity by affinity chromatography
-
from larval gut
-
Hi-Trap chelating column chromatography and Superdex-200 gel filtration
-
1400fold from pancreas
-
17000fold from hepatopancreas
-
17000fold from hepatopancreas, to homogeneity
-
2 chromatography steps to homogeneity
-
from parotid gland
-
separation from E2-immunity protein by guanidine-HCl dissociation
-
2479fold from pancreas, isozymes A and B to homogeneity
Q9YGI5
affinity chromatography
-
three chromatographic steps
Q5R2I2
2 chromatography steps to homogeneity
-
near homogeneity
-
near homogeneity by fractionation steps
-
one chromatographic step to homogeneity
-
overexpressed DNaseI-Fc fusion protein
-
recombinant His-tagged enzyme from 293 cells
P24855
to homogeneity by 6step chromatography
-
to homogeneity by chromatography techniques for serum and pancreas DNase I
-
to homogeneity by chromatography steps
-
DNase1/3-like nuclease, by affinity chromatography
O55070
to homogeneity by 2step chromatography
-
14000fold from hepatopancreas
O42446
to homogeneity by 4step chromatography
-
one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column
-
to homogeneity by conconavalin A-agarose
-
10000fold from hepatopancreas
Q5KTT0
to homogeneity by chromatography techniques, isoelectric focusing, gel filtration
-
affinity chromatography and gel filtration, highly pure protein was used for assays
Potyvirus sp.
-
1800fold from pancreas
Q90WM1
one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column
-
high homogeneity by chromatography steps
-
to homogeneity by affinity chromatography
-
recombinant wild-type and deletion mutants from Escherichia coli, to homogeneity
-
26500fold from pancreas, to homogeneity
-
one-step purification by lectin affinity chromatography using a combined concanavalin A and wheat germ agglutinin column
-
to homogeneity by chromatography steps
-
three chromatographic steps
Q5R2I3
1800fold from pancreas
Q90W31
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the pET28a expression vector and overexpressed in Escherichia coli BL21 (DE3). His-tagged OmpA expressed in HEp-2 cells
-
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in COS-7 cells
Q5KTT1
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type and mutants in COS-7 cells
-
into vector pET15b and expressed in Escherichia coli strain BL21(DE3)pLysE
-
overexpression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression in COS-7 cells
Bufo vulgaris japonicus
Q90WM0
DNA and amino acid sequence determination and analysis, expression in COS-7 cells
Q767J3
mutant G52E (CRM197) is expressed in Escherichia coli BL21AI 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
Q8JIP7
expression in COS-7 cells
-
expression in COS-7 cell
-
expression of wild-type and mutants in COS-7 cells
-
DNA and amino acid sequences determination and analysis, expression in Escherichia coli BL21(DE3) in the insoluble fraction
Q9YGI5
expression in COS-7 cells
-
expression in Escherichia coli as His-tag fusion construct
-
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-7 cells
-
expression in Escherichia coli
-
expression in human 293 cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type and mutants in COS-7 cells
-
overexpression in chinese hamster ovary cells
-
overexpression in Sf9 cells as a DNaseI-Fc fusion- and a non-fusion protein
-
transient ectopic expression in HeLa S3 cells, no toxic effect on host cells, expression in human embryonic kidney 293 cells as His-tagged enzyme
P24855
transient expression in COS-7 cell
-
deducing amino acid composition from cDNA
-
expression in MCF-7 cell
P49183
expression in NIH-3T3 fibroblasts
-
NIH-3T3 cells with expression vectors for murine DNase1 and DNase1/3 cDNA
O55070
deducing amino acid composition from cDNA
-
DNA and amino acid sequence determination and analysis, expression in COS-7 cells
Q5KTT0
expression in Escherichia coli
Potyvirus sp.
-
DNA and amino acid sequence determination and analysis, expression in COS-7 cells as His-tagged enzyme
Q90WM1
expression in NIH-3T3 fibroblasts
P21704
quantification of gene transcript in somatostatin treated animals
P21704
expression in COS cells
-
expression of wild-type and deletion mutants in Escherichia coli BL21 (DE3)
-
DNA 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
Q90W31
expression in COS-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose induces both DNase I and caspase-3
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D44H
Q5KTT1
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
Q5KTT1
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
M118R
Q5KTT1
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
M236Q
Q5KTT1
pH profile remains similar to the wild-type enzyme with an optimum around pH 8.0
Q134L
Q5KTT1
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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 1.0
N106Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q
-
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q/N106Q
-
enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin
N7A
-
complete loss of activity
N7S
-
complete loss of activity
P132A
-
also naturally occuring mutation, ID number (NCBI database): rs1799891, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 2.10, relative thermal stability (activity measured after incubation of the cells for 20 min at 50C) 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 50C) 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 50C) 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 50C) 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 50C) 0.81
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 50C) 1.2
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 50C) 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 50C) 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 50C) 0.60
Q38H
-
naturally occuring mutation, ID number (NCBI database): rs4554238
Q9E
-
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) about 0.35
Q9R/E13R/N74K
-
most hyperactive variant, 35fold more active than wild type enzyme
R100E
-
adds a residue that hydrogen bonds to the catalytic H160 in DNAse I, increases the specific activity of the hybrid protein
R185C
-
naturally occuring mutation
R21S
-
also naturally occuring mutation, ID number (NCBI database): rs8176927, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.75, relative thermal stability (activity measured after incubation of the cells for 20 min at 50C) 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 50C) 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 50C) 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 50C) 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 50C) 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 50C) 0.67
C151A
Potyvirus sp.
-
activity similar to wild type
D81G
Potyvirus sp.
-
no activity
D81N
Potyvirus sp.
-
50% activity compared to wild type
H46A
Potyvirus sp.
-
activity similar to wild type
R334A/E74A
-
inactive
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
L62E
-
added a metal ion-binding residue, increases the specific activity of the hybrid protein
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
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
A144Y
P49183
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
additional information
O55070
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
-
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
H371A
-
site-directed mutagenesis, exchange of a well-conserved His residue, loss of most of the nuclease activity, stilla ctive in DNA-binding
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
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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 37C for 30 min, a quantitative analysis can be achieved in the range of 0.0001-0.01 units/microl of DNase I
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
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
medicine
-
inhibition of viral synthesis by DNase I in cell cultures
medicine
-
usage of DNase 1 as a therapeutic agent in systemic lupus erythematosus
medicine
-
treatment of established 72 h biofilms with 100 microg per ml of DNase for 24 h induces incomplete Listeria monocytogenes biofilm dispersal, with about 25% biofilm remaining compared to control. Addition of proteinase K completely inhibits biofilm formation, and 72 h biofilms including those grown under stimulatory conditions are completely dispersed with 100 microg per ml proteinase K
molecular biology
-
a DNase bioreactor can be used to remove DNA from RNA samples prior to reverse transcription followed by PCR
analysis
-
enzymatic activity assay for determination of enzyme stability. Method bases on a colorimetric endpoint activity assay using degradation of a DNA/methyl green complex and is feasible on an automated analyzer system within a rather short time
analysis
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotynilated forward and fluorescein-labeled reverse primers. Urine samples give an activity of 1.49 U/ml, blood plasma of 0.36 U/ml
analysis
-
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
diagnostics
-
decrease in DNase activity in blood correlates with chronic pancreatitis, stomach cancer and glomerulonephritis, increase in DNase activity in blood was observed during development of breast cancer
diagnostics
-
increased DNase I activity in patient serum could be used as diagnostic marker for the early detection of acute myocardial infarction
medicine
-
inhaled DNase I into the airways reduces viscoelasticity of sputum, improves lung function of cystic fibrosis patients
medicine
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improvement of respiratory tract functioning in patients with cystic fibrosis
medicine
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analysis of genetic polymorphisms and correlation between genotype and its activity. Study on allele frequencies in DNase1 polymorphisms and polymorphisms in intron 4, designated HumDN1
medicine
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enzymatic activity assay for determination of enzyme stability. Method bases on a colorimetric endpoint activity assay using degradation of a DNA/methyl green complex and is feasible on an automated analyzer system within a rather short time. Application of method proves the reliability of enzyme during aerosolization with inhalation devices
medicine
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DNAse I/cdtB gene chimera has therapeutic applications for inhibiting the proliferation of cancer cells
medicine
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early use of dornase alpha provides nutritional benefits, thus is significantly associated with a higher body mass index percentile over time. Children who received dornase alpha before age two have an average body mass index percentile that is 10.2 percentiles greater than children who have not
medicine
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extracellular DNase 1 is implicated in the chromatin breakdown of necrotic cells in vitro. Connection between DNase 1 activity and the development of human systemic lupus erythematosus. Systemic lupus erythematosus patients have lower DNase 1 activity than patients with rheumatoid arthritis and scleroderma. Usage of DNase 1 as a therapeutic agent in systemic lupus erythematosus
medicine
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single nucleotide polymorphism in exon 8, is associated with several diseases
medicine
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DNase I activity activity in systemic Lupus erythematosus patients is lower than in healthy controls. DNase I activity is in positive correlation with systemic Lupus erythematosus activity index-2K, levels of antinuclear, anti-dsDNA, anti-nucleosome and anti-histone antibodies and in negative correlation with complement component C3 concentration. An increase of DNase I activity characterizes relapse in most SLE patients, although it does not reach the levels of healthy individuals
medicine
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patients with type 2 diabetes show a significant elevation of DNase I activity in serum, and increase in DNase I expression is observed in the pancreas of diabetic persons
medicine
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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
analysis
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use of DNase I pre-treatment significantly increases the reliability and sensitivity of immunodetection of CIP/KIP cyclin-dependent kinase inhibitors. Applications in developmental neurobiology and cancer diagnosis
medicine
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use of DNase I pre-treatment significantly increases the reliability and sensitivity of immunodetection of CIP/KIP cyclin-dependent kinase inhibitors. Applications in developmental neurobiology and cancer diagnosis
medicine
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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
molecular biology
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DNase-I hypersensitive sites may constitute a molecular marker to identify alleles and subsequently acquire the appropriate methylation imprint. This molecular identifier may be present or absent for a specific gene according to the sex of the gamete
additional information
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the gonadotrophin releasing hormone cGnRH II is pro-apoptotic to pyriform cells, exerting its effects by activating an alternative cell death pathway, probably involving calcium as first messenger and DNase I as first executioner