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Information on EC 3.1.21.1 - deoxyribonuclease I and Organism(s) Bos taurus and UniProt Accession P00639
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3.1.21.1 deoxyribonuclease ISpecify your search results
Word Map
- 3.1.21.1
-
footprint
- polymerases
- chromatin
- strand
- milk
- neutrophil
-
single-stranded
- lysozyme
-
exonuclease
- herpes
- bacteriophage
- viruses
- phage
- histone
- triphosphate
- simplex
- transferrin
- polymerization
- infant
- transcriptase
- immunoglobulin
- actin
-
fidelity
- nucleosome
- duplex
- myeloperoxidase
- mismatch
- thymidine
- cytomegalovirus
- dntp
-
protein-dna
- fork
-
sequence-specific
- pcna
- sp1
- endonucleases
- herpesvirus
- iga
-
dna-protein
-
micrococcal
- nucleases
- ganciclovir
- whey
- beta-globin
-
supercoiled
-
exotoxin
-
dna-dependent
- ssdna
- medicine
- diagnostics
- streptokinase
- molecular biology
- analysis
- lamivudine
- pharmacology
- degradation
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lactoferrin, dna polymerase, dnase i, colicin, diphtheria toxin, dnaase, deoxyribonuclease, dnasei, deoxyribonuclease i, crm197, 
more
topSYNONYM 
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
-
-
-
-
deoxyribonuclease A
-
-
-
-
deoxyribonucleic phosphatase
-
-
-
-
DNA endonuclease
-
-
-
-
DNase
-
-
-
-
DNase I
-
-
-
-
DNase I
-
-
Escherichia coli endonuclease I
-
-
-
-
pancreatic deoxyribonuclease
-
-
-
-
pancreatic DNase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
preference for double-stranded DNA
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9003-98-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
5'-phosphooligonucleotides + ?
DNAse I converts 100% of 1 microg of supercoiled plasmid DNA to relaxed form in 1 h at 37°C. A 10fold higher concentration of DNAse I converts 98% of 1 microg of supercoiled DNA to linear form and a 100fold higher concentration of the nuclease completely digests the DNA into small fragments
-
-
?
crab d(A-T) polymer + H2O
5'-hexanucleotides + ?
-
unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure
enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage
?
DNA + H2O
5'-phosphotrinucleotides + ?
-
no preference for any nucleotide
as the main products
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
-
wild-type enzyme and mutant D99A perform double scission on duplex DNA in presence of Mg2+ and Ca2+, not mutant D201A
-
?
Fc-oligo-SH + H2O
?
-
degradation of a thiolated ferrocenyloligonucleotide, efficiency of DNase I reaction on the electrode is 48, 72, or 73% when treated with 1 microl of 2, 1, or 0.5 micromol ferrocenyloligonucleotide, respectively. DNase I can cleave the oligonucleotide on the gold surface and does not show a nonspecific surface absorption
-
-
?
NO2-Ph-pdTp-NO2Ph + H2O
p-nitrophenol + NO2-Ph-pdT-3'-phosphate
-
rapidly hydrolyzed at a single bond
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
-
-
superhelical form converted to circular-relaxed and linear forms
?
DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for native DNA
produces nicks on one strand in preference to scission of both strands, autoretardation causes the continuous formation of products which are poorer substrates than those from which they are derived
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
immobilized DNase I is used in a bioreactor
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
DNase I-DNA interaction alters protein secondary structure, with a major reduction in alpha helix and an increase in beta sheet and random structures, and reveals a partial B-to-A DNA conformational change. No DNA digestion upon protein-DNA complexation
-
-
?
plasmid DNA + H2O
?
-
depending on metal ions, duplex DNA is hydrolyzed by DNase I in a single or double scission mode
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
preference for double-stranded DNA
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
major function is to inflict nicks during early stages of hydrolytic attack on DNA, participation in repair phenomena
differences in the composition of digests obtained in the presence of Mn2+ or Mg2+, differences between the early and terminal stages of the reaction, with DNA as substrate early cleavages are directed towards the center of the molecule and are predominantly single-strand nicks, in the latter part of the reaction the purine-p-pyrimidine bond is preferentially cleaved
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+
in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
cutting one of the two strands by a nucleophilic attack on the O-3'-P-bond
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
-
hydrolysis of both double- and single-stranded DNA
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
Sr2+
additional information
-
metal binding and influence on activity, wild-type and mutant enzymes, overview
Ca2+
-
addition of Ca2+ stabilizes the enzyme, facilitates second cut in double-stranded DNA
Ca2+
-
no lag phase in the reaction obtained, if only Ca2+ is present or both Mg2+ and Ca2+ are present, double strand digestion preferred
Ca2+
-
Ca2+-binding causes a conformational change that maintains a more active structure of the enzyme
Ca2+
-
dependent on, D201 and D99 are involved in binding, conformation, protects wild-type and mutant D99A enzymes against trypsin inactivation, not mutant D201A
Ca2+
-
in the absence of Ca2+, but with Mg2+ the DNase cleaved the substrate DNA in a single nicking mode
Ca2+
-
in the presence of Ca2+, native (0.2 U) and inactivated DNase I of 5fold greater enzyme units applied (1.0 U) hydrolyze the Mg2+-DNA substrate forming some linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission, while 0.2 U of 2-nitro-5-thiosulfobenzoic acid-treated DNase I can only cleave the Mg2+-DNA substrate in a single nicking mode
Ca2+
-
two Ca2+ ions that stabilize surface loops as well as an additional metal ion binding site at the active site
Ca2+
-
4 ion-binding pockets, two of them strongly bind Ca2+ while the other two sites coordinate Mg2+
Co2+
-
reaction performs mainly double strand scissions, Co2+ is a better activator than other divalent metals
Mg2+
-
only single strand cleavage occurs during the lag period of the reaction if only Mg2+ is present
Mg2+
-
enzyme about 99.5% inactive if Ca2+ contamination is reduced to a minimum, must bind to the substrate, whereas Ca2+ must bind to the enzyme
Mg2+
-
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+
Mn2+
-
in the presence of Mn2+, native and 2-nitro-5-thiosulfobenzoic acid-treated DNase I of two different enzyme units used are all able to hydrolyze the plasmid DNA substrate in a double scission mode
Mn2+
-
in the presence of Mn2+, the wild-type is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
-
2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
-
2-mercaptoethanol
-
inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
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
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
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
-
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
Trypsin
-
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
-
2-Nitro-5-thiocyanobenzoic acid
-
inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135
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
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
-
iodoacetate
-
formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
N-bromosuccinimide
-
modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
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
-
DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
-
additional information
-
thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.106
2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.134
2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.148
2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
Bos taurus
pH and temperature not specified in the publication
0.148
2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.128
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.156
2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
0.197
2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
Bos taurus
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
975
0.1 M Tris-HCl pH 7.0, 10 mM CaCl2, 10 mM MnCl2, 0.05 mg/ml calf thymus DNA
additional information
additional information
-
specificity in DNA-DNase I interaction is mediated by DNA flexibility, which influences the induced-fit transitions required to form productive complexes. Productive DNA-DNase I interactions appear to be governed by one main DNA structural element: the minor groove width. Minor groove dimension results from various molecular mechanisms. For unbent DNA the local flexibility favors a wide minor groove. Since DNA flexibility is highly sequence dependent, base sequence influences the induced-fit transitions required to form DNA-DNase I complexes
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DNAS1_BOVIN
282
1
31346
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
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 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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
DNAse I DNA nicking-activity is less than 50% of the control after 5 min of heating
additional information
additional information
-
both N-linked glycosylation sites N18 and N106 are required for heat stability
additional information
-
thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ is able to protect DNase completely against inactivation by trypsin
-
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 5 mM CaCl2, 30% polyethylene glycol, 4 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
conconavalin A-agarose as an effective step for DNases with neutral carbohydrate side-chains, preparing a protease free DNase I
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
degradation
the degradation of extracellular DNA with enzymes such as DNase I is a rapid method to remove Campylobacter jejuni biofilms, and is likely to potentiate the activity of antimicrobial treatments and thus synergistically aid disinfection treatments
pharmacology
analysis
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
molecular biology
-
a DNase bioreactor can be used to remove DNA from RNA samples prior to reverse transcription followed by PCR
pharmacology
bacterial biofilm infections are highly prevalent and are a significant cause of morbidity and mortality. With the rapid emergence of resistance to conventional antibiotic therapies and intrinsic biofilm resistance to antibiotic penetration, Pseudomonas aeruginosa biofilm treatment options are limited. Consequently, novel anti-biofilm strategies to prevent biofilm formation and remove existing biofilms are being sought. Glutathione enhances antibiotic efficiency and effectiveness of DNase I in disrupting Pseudomonas aeruginosa biofilms while also inhibiting pyocyanin activity, Thus facilitating restoration of cell enzymatic activity, confluence and viability
pharmacology
DNase I has a cytotoxic effect on B16 melanoma cells. DNase I inhibits the migratory activity of melanoma cells in vitro, causing a decrease in the distance of cell front migration and in the area of scratch healing 48 h after the enzyme addition, as well as reducing the rate of cell migration. In mice with B16 metastatic melanoma, intramuscular administration of DNase I in the dose range of 0.12-1.20 mg/kg results in a two- to threefold decrease in the number of surface lung metastases and causes nonspecific antigenic immune stimulation. The pronounced antimetastatic effect of DNase I observed in the in vivo model of metastatic B16 melanoma may be due to both the inhibitory activity of the enzyme on the molecular level (i.e., exDNA degradation) and to its systemic effect on the immune system
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 37°C for 30 min, a quantitative analysis can be achieved in the range of 0.0001-0.01 units/microl of DNase I
analysis
-
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, C.Y.; Lu, S.C.; Liao, T.H.
Cloning, sequencing and expression of a cDNA encoding bovine pancreatic deoxyribonuclease I in Escherichia coli: purification and characterization of the recombinant enzyme
Gene
206
181-184
1998
Bos taurus
Bellard, M.; Dretzen, G.; Giangrande, A.; Ramain, P.
Nuclease digestion of transcriptionally active chromatin
Methods Enzymol.
170
317-346
1989
Bos taurus
Cobianchi, F.; Wilson, S.H.
Enzymes for modifying and labeling DNA and RNA
Methods Enzymol.
152
94-110
1987
Bos taurus
Suck, D.; Oefner, C.; Kabsch, W.
Three-dimensional structure of bovine pancreatic DNase I at 2.5 angstrm resolution
EMBO J.
3
2423-2430
1984
Bos taurus
Kreuder, V.; Dieckhoff, J.; Sittig, M.; Mannherz, H.G.
Isolation, characterization and crystallization of deoxyribonuclease I from bovine and rat parotid gland and its characterization with rabbit skeletal muscle actin
Eur. J. Biochem.
139
389-400
1984
Bos taurus, Rattus sp.
Weston, S.A.; Lahm, A.; Suck, D.
X-ray structure of the DNase I-d(GGTATACC)2 complex at 2.3 A resolution
J. Mol. Biol.
226
1237-1256
1992
Bos taurus
Moore, S.
Pancreatic DNase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
14
281-296
1981
Bos taurus
-
Funkakoshi, A.; Tsubota, Y.; Fujii, K.; Ibayashi, H.; Takagi, Y.
Simple purification and properties of bovine pancreatic deoxyribonuclease I
J. Biochem.
88
1113-1118
1980
Bos taurus
Sartin, J.L.; Hugli, T.E.; Liao, T.H.
Reactivity of the tryptophan residues in bovine pancreatic deoxyribonuclease with N-bromosuccinimide
J. Biol. Chem.
255
8633-8637
1980
Bos taurus
Hitchcock, S.E.
Actin-deoxyribonuclease I interaction
J. Biol. Chem.
255
5668-5673
1980
Bos taurus
Lizarraga, B.; Sanchez-Romero, D.; Gil, A.; Melgar, E.
The role of Ca2+ on pH-induced hydrodynamic changes of bovine pancreatic deoxyribonuclease A
J. Biol. Chem.
253
3191-3195
1978
Bos taurus
Catley, B.J.
Observations on the carbohydrate moiety of bovine pancreatic deoxyribonuclease A
Arch. Biochem. Biophys.
159
214-223
1973
Bos taurus
Junowicz, E.; Spencer, J.H.
Studies on bovine pancreatic deoxyribonuclease A 1. Generel properties and activation with different bivalent metals
Biochim. Biophys. Acta
312
72-84
1973
Bos taurus
Poulos, T.L.; Price, P.A.
Some effects of calcium ions on the structure of bovine pancreatic deoxyribonuclease A
J. Biol. Chem.
247
2900-2904
1972
Bos taurus
Schabort, J.C.; Pitout, M.J.
The relationship between the chemical structure of aflatoxins and their effect on bovine pancreas deoxyribonuclease
Enzymologia
41
201-206
1970
Bos taurus
Laskowski, Sr., M.
Deoxyribonuclease I
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
289-311
1971
Bos taurus
-
Iwamori, M.; Suzuki, H.; Kimura, T.; Iwamori, Y.
Shedding of sulfated lipids into gastric fluid and inhibition of pancreatic DNase I by cholesterol sulfate in concert with bile acids
Biochim. Biophys. Acta
1487
268-274
2000
Bos taurus
Chen, C.Y.; Lu, S.C.; Liao, T.H.
The distinctive functions of the two structural calcium atoms in bovine pancreatic deoxyribonuclease
Protein Sci.
11
659-668
2002
Bos taurus
Chen, W.J.; Huang, P.T.; Liu, J.; Liao, T.H.
Involvement of the N- and C-terminal fragments of bovine pancreatic deoxyribonuclease in active protein folding
Biochemistry
43
10653-10663
2004
Bos taurus (P00639), Bos taurus
Bencina, M.; Bencina, K.; Strancar, A.; Podgornik, A.
Immobilization of deoxyribonuclease via epoxy groups of methacrylate monoliths
J. Chromatogr. A
1065
83-91
2005
Bos taurus
De Maria, A.; Arruti, C.
DNase I and fragmented chromatin during nuclear degradation in adult bovine lens fibers
Mol. Vis.
10
74-82
2004
Bos taurus
Chen, W.J.; Lee, I.S.; Chen, C.Y.; Liao, T.H.
Biological functions of the disulfides in bovine pancreatic deoxyribonuclease
Protein Sci.
13
875-883
2004
Bos taurus
Chen, W.J.; Lo, T.; Lai, Y.S.; Huang, P.T.; Lin, C.C.; Liao, T.H.
Construction and characterization of a bifunctional enzyme with deoxyribonuclease I and thioredoxin-like activities
Biochem. Biophys. Res. Commun.
356
750-755
2007
Bos taurus (P00639), Bos taurus
Sato, S.; Fujita, K.; Kanazawa, M.; Mukumoto, K.; Ohtsuka, K.; Waki, M.; Takenaka, S.
Electrochemical assay for deoxyribonuclease I activity
Anal. Biochem.
381
233-239
2008
Bos taurus
Martnez Valle, F.; Balada, E.; Ordi-Ros, J.; Vilardell-Tarres, M.
DNase 1 and systemic lupus erythematosus
Autoimmun. Rev.
7
359-363
2008
Bos taurus, Homo sapiens, Mus musculus
N'soukpo-Kossi, C.N.; Diamantoglou, S.; Tajmir-Riahi, H.A.
DNase I - DNA interaction alters DNA and protein conformations
Biochem. Cell Biol.
86
244-250
2008
Bos taurus
Mannherz, H.G.; Ballweber, E.; Hegyi, G.; Goody, R.S.
Cross-linked long-pitch actin dimer forms stoichiometric complexes with gelsolin segment 1 and/or deoxyribonuclease I that nonproductively interact with myosin subfragment 1
Biochemistry
47
9335-9343
2008
Bos taurus
Fujihara, J.; Yasuda, T.; Kunito, T.; Fujii, Y.; Takatsuka, H.; Moritani, T; Takeshita, H.
Two N-linked glycosylation sites (Asn18 and Asn106) are both required for full enzymatic activity, thermal stability, and resistance to proteolysis in mammalian deoxyribonuclease I
Biosci. Biotechnol. Biochem.
72
3197-3205
2008
Bos taurus, Homo sapiens (P24855), Homo sapiens, Equus caballus (Q4AEE3), Equus caballus
Elkordy, A.A.; Forbes, R.T.; Barry, B.W.
Study of protein conformational stability and integrity using calorimetry and FT-Raman spectroscopy correlated with enzymatic activity
Eur. J. Pharm. Sci.
33
177-190
2008
Bos taurus
DiRienzo, J.M.; Cao, L.; Volgina, A.; Bandelac, G.; Korostoff, J..
Functional and structural characterization of chimeras of a bacterial genotoxin and human type I DNAse
FEMS Microbiol. Lett.
291
222-231
2009
Bos taurus (P00639), Homo sapiens (P24855), Homo sapiens
Krasnorutskii, M.A.; Buneva, V.N.; Nevinsky, G.A.
Immunization of rabbits with DNase I produces polyclonal antibodies with DNase and RNase activities
J. Mol. Recognit.
21
233-242
2008
Bos taurus, Homo sapiens
N'soukpoe-Kossi, C.N.; Tajmir-Riahi, H.A.
DNase I-tRNA interaction
Oligonucleotides
18
65-72
2008
Bos taurus
Chen, W.J.; Liao, T.H.
2-Nitro-5-thiosulfobenzoic acid as a novel inhibitor specific for deoxyribonuclease I
Protein J.
27
240-246
2008
Bos taurus, Rattus norvegicus
Chen, W.J.; Huang, P.T.; Cheng, Y.C.; Liao, T.H.
Putative secondary active site of bovine pancreatic deoxyribonuclease I
Protein Pept. Lett.
15
640-646
2008
Bos taurus
Heddi, B.; Abi-Ghanem, J.; Lavigne, M.; Hartmann, B.
Sequence-dependent DNA flexibility mediates DNase I cleavage
J. Mol. Biol.
395
123-133
2010
Bos taurus
Gueroult, M.; Picot, D.; Abi-Ghanem, J.; Hartmann, B.; Baaden, M.
How cations can assist DNase I in DNA binding and hydrolysis
PLoS Comput. Biol.
6
e1001000
2010
Bos taurus
Zhou, Z.; Zhu, C.; Ren, J.; Dong, S.
A graphene-based real-time fluorescent assay of deoxyribonuclease I activity and inhibition
Anal. Chim. Acta
740
88-92
2012
Bos taurus
Nguyen, U.T.; Burrows, L.L.
DNase I and proteinase K impair Listeria monocytogenes biofilm formation and induce dispersal of pre-existing biofilms
Int. J. Food Microbiol.
187
26-32
2014
Bos taurus
Ts Mavrova, A.; Dimov, S.; Yancheva, D.; Kolarevic, A.; Ilic, B.S.; Kocic, G.; Smelcerovic, A.
Synthesis and DNase I inhibitory properties of some 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidines
Bioorg. Chem.
80
693-705
2018
Bos taurus (P00639), Bos taurus
Brown, H.L.; Hanman, K.; Reuter, M.; Betts, R.P.; van Vliet, A.H.
Campylobacter jejuni biofilms contain extracellular DNA and are sensitive to DNase I treatment
Front. Microbiol.
6
699
2015
Bos taurus (P00639)
Das, T.; Simone, M.; Ibugo, A.I.; Witting, P.K.; Manefield, M.; Manos, J.
Glutathione enhances antibiotic efficiency and effectiveness of DNase I in disrupting Pseudomonas aeruginosa biofilms while also inhibiting pyocyanin activity, thus facilitating restoration of cell enzymatic activity, confluence and viability
Front. Microbiol.
8
2429
2017
Bos taurus (P00639)
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