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Information on EC 3.1.21.1 - deoxyribonuclease I and Organism(s) Homo sapiens and UniProt Accession P24855

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyribonuclease I
-
deoxyribonuclease-1
-
type I DNAse I
-
deoxyribonuclease
-
-
-
-
deoxyribonuclease A
-
-
-
-
deoxyribonuclease I
-
-
deoxyribonucleic phosphatase
-
-
-
-
desoxyribonuclease
-
-
-
-
DNA endonuclease
-
-
-
-
DNase
-
-
-
-
DNase 1
-
-
DNase I
Dnase1
-
-
DNase1-like 3
-
-
DNase1/3
-
-
Dornase alfa
-
-
-
-
dornase alpha
-
-
endodeoxyribonuclease I
-
-
-
-
EndoDNase
-
-
Escherichia coli endonuclease I
-
-
-
-
hDNase I
-
-
lactoferrin
-
-
nuclease, deoxyribo-
-
-
-
-
nuclease, Escherichia coli endo-, I
-
-
-
-
pancreatic deoxyribonuclease
-
-
-
-
pancreatic DNase
-
-
-
-
pulmozyme, rhDNaseI
-
-
streptodornase
-
-
-
-
tear lipocalin
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
hydrolysis of phosphoric ester
CAS REGISTRY NUMBER
COMMENTARY hide
9003-98-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
double-stranded DNA + H2O
?
show the reaction diagram
-
-
-
?
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
salmon testis DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
supercoiled DNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
in presence of Mg2+ and Ca2+ under neutral conditions
production of 3'-OH and 5'-phosphate ends
?
(pC)10 + H2O
?
show the reaction diagram
-
-
-
-
?
190mer DNA fragment + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
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
-
-
-
-
?
DNA + H2O
5'-phosphodinucleotides + 5'-phosphooligonucleotides
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
predominant single-strand nicking in presence of Mg2+ and Ca2+
-
?
dsDNA + H2O
?
show the reaction diagram
-
-
-
?
heat-denatured DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
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
p-nitrophenyl phenylphosphonate + H2O
p-nitrophenol + phenylphosphoric acid
show the reaction diagram
poly(dA) + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
poly(dT) + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
relaxed circular plasmid DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
?
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
dsDNA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Co2+
activates
Mg2+
activates, DNase I is a Ca2+/Mg2+-dependent enzyme, synergism
Mn2+
activates
Cu2+
-
highest activity at 5 mM, but only 40% activtiy compared to Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
actin
inhibits the DNA-nicking activity of DNAse I/CdtB chimera
aurintricarboxylic acid
i.e ATA, a general inhibitor of nucleases, weak inhibition
G-actin
specific, strong inhibition
-
gamma-actin
-
-
2-(4-amidinophenyl)-6-indolecarbamidine
-
significantly inhibits DNase I activity
2-mercaptoethanol
-
inhibition after treatment with EGTA
Ca2+
-
80% inhibition at 0.1 mM
G-actin
-
gamma-actin
-
-
-
heparin
-
directly inhibits recombinant DNase1/3
iodoacetate
-
complete inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
(pC)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0042
d(pA)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0053
d(pApCpTpApCpApGpTpCpTpApCpA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0072
d(pGpGpCpApCpTpTpApC)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0056
d(pT)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0037
d(pTpApGpApApGpApTpCpApApA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167 - 493.3
(pC)10
106.6
d(pA)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
703.3
d(pApCpTpApCpApGpTpCpTpApCpA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
0.0492 - 453.3
d(pGpGpCpApCpTpTpApC)
713
d(pT)10
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
136.6
d(pTpApGpApApGpApTpCpApApA)
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000013
gamma-actin
-
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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+
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
DNase I
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
6.75
-
DNase I type-1 enzyme
7.2 - 7.6
-
in 33 mM Tris-HCl buffer
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
-
-
5 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
stable up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
pI values vary from 3.5-4.3 due to single nucleotide polymorphism
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
blood plasma of 40 non-pregnant women, 40 healthy pregnant women (over 37 weeks) and 40 pregnant women with a diagnosis of intrauterine growth restriction
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
-
leukemic cells
Manually annotated by BRENDA team
-
multi-drug resistant cell line
Manually annotated by BRENDA team
-
enzyme secretion
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNAS1_HUMAN
282
1
31434
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32498
x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation
37000
x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation
30000
33000 - 38000
-
for serum and pancreas DNase I, gel filtration
34000
38000
-
gel filtration
41000
-
SDS-PAGE, gel filtration
80000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, recombinant secreted enzyme, SDS-PAGE, x * 32498, sequence calculation
heterotrimer
CdtB/DNAse I, but not DNAseI/CdtB
monomer
-
1 * 34000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
enzyme contains 2 potential N-glycosylation sites
proteolytic modification
enzyme sequence contains a precursor peptide
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A224del
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.69, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.52
A224P
also naturally occuring mutation, ID number (NCBI database): rs8176939, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.23, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.36
C209Y
also naturally occuring mutation, ID number (NCBI database): rs8176939, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.24, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.23
E13D
also naturally occuring mutation, ID number (NCBI database): rs34907394, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.35, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
G105A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.05, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.68
G105K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 3.27, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.64
G105R
also naturally occuring mutation, ID number (NCBI database): rs176919, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 3.22, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.63
G240D
also naturally occuring mutation, ID number (NCBI database): rs8176924, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.46, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.56
G55R
adds DNA contact residues, increases the specific activity of the hybrid protein
K18Term
termination codon at triplet 18, also naturally occuring mutation, no activity detected
L186L
also naturally occuring mutation, ID number (NCBI database): rs8176920, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.8, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
L62E
added a metal ion-binding residue, increases the specific activity of the hybrid protein
N106Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q
enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin
N18Q/N106Q
enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin
N7A
complete loss of activity
N7S
complete loss of activity
P132A
also naturally occuring mutation, ID number (NCBI database): rs1799891, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 2.10, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.93
P197A
also naturally occuring mutation, ID number (NCBI database): rs34186031
P197S
also naturally occuring mutation, ID number (NCBI database): rs34186031, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 2.03, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.75
Q222E
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.26, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
Q222K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.71, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.0
Q222L
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.17, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.81
Q222R
also naturally occuring mutation, ID number (NCBI database): rs1053874, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.48, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 1.2
Q35A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.39, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.55
Q35E
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.79, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.53
Q35H
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.60, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.60
Q38H
naturally occuring mutation, ID number (NCBI database): rs4554238
Q9E
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) about 0.35
R100E
adds a residue that hydrogen bonds to the catalytic H160 in DNAse I, increases the specific activity of the hybrid protein
R185C
naturally occuring mutation
R21S
also naturally occuring mutation, ID number (NCBI database): rs8176927, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.75, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.96
R85A
no activity detected
R85G
also naturally occuring mutation, ID number (NCBI database): rs8176928, no activity detected
R85K
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.87, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.56
S99Y
adds DNA contact residues, increases the specific activity of the hybrid protein
V134R
adds DNA contact residues, increases the specific activity of the hybrid protein
V82M
also naturally occuring mutation
V89A
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.21, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.53
V89L
relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.55, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.33
V89M
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 0.24, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.20
V92M
also naturally occuring mutation, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) about 1.0
Y95S
also naturally occuring mutation, ID number (NCBI database): rs34923865, relative activity secreted from transiently transfected COS-7 cells assayed by the single radial enzyme diffusion method (wild type activity = 1.0) 1.32, relative thermal stability (activity measured after incubation of the cells for 20 min at 50°C) 0.67
E128W
-
point mutation by sequential PCR steps, altered secondary structure, 80% reduced activity compared to the wild-type enzyme
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
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
Q244R
-
polymorphism of DNase 1, is associated with systemic lupus erythematosus susceptibility but is not correlated with DNase 1 activity
Q9R/E13R/N74K
-
most hyperactive variant, 35fold more active than wild type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
stable within the range for 24 h at 4°C
134214
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
-
stable for 1 month
0
-
stable for 7 days
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance
less active in phosphate buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HCl, pH 7.5, 5 mM CaCl2, 30% polyethylene glycol, more than 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from 293 cells
2 chromatography steps to homogeneity
-
near homogeneity
-
near homogeneity by fractionation steps
-
one chromatographic step to homogeneity
-
overexpressed DNaseI-Fc fusion protein
-
to homogeneity by 6step chromatography
-
to homogeneity by chromatography techniques for serum and pancreas DNase I
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 of wild-type and mutants in COS-7 cells
transient ectopic expression in HeLa S3 cells, no toxic effect on host cells, expression in human embryonic kidney 293 cells as His-tagged enzyme
transient expression in COS-7 cell
DNase I cDNA, derived from genes DNASE1-1 and DNASE1-2 ligated into a pcDNA3.1 (+) vector and expressed in COS-7 cells
-
expression in Escherichia coli
-
expression in human 293 cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
overexpression in chinese hamster ovary cells
-
overexpression in Sf9 cells as a DNaseI-Fc fusion- and a non-fusion protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
significant increase of DNase I activity in cases of intrauterine growth restriction. Increase in DNase I activity over a certain threshold indicates presence of pathological processes in the organism
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
cell-free DNA circulating in blood cannot be a reliable marker of increased cell death during pregnancy. Thus, assessment of the level of cell death during pregnancy should be done by simultaneous analysis of cell-free DNA level and DNase I activity
medicine
DNAse I/cdtB gene chimera has therapeutic applications for inhibiting the proliferation of cancer cells
analysis
diagnostics
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dwyer, A.A.; Huang, A.J.; Pan, C.Q.; Lazarus, R.A.
Expression and characterization of a DNase I-Fc fusion enzyme
J. Biol. Chem.
274
9738-9743
1999
Homo sapiens
Manually annotated by BRENDA team
Felten, C.; Quan, C.P.; Chen, A.B.; Canova-Davis, E.; McNerney, T.; Goetzinger, W.K.; Karger, B.L.
Use of acidic and basic pH and calcium ion addition in the capillary zone electrophoretic characterization of recombinant human deoxyribonuclease, a complex phosphoglycoprotein
J. Chromatogr.
853
295-308
1999
Homo sapiens
Manually annotated by BRENDA team
Takeshita, H.; Yasuda, T.; Nakajima, T.; Hosomi, O.; Nakashima, Y.; Kishi, K.
Mouse deoxyribonuclease I (DNase I): biochemical and immunological characterization, cDNA structure and tissue distribution
Biochem. Mol. Biol. Int.
42
65-75
1997
Homo sapiens, Mus musculus, Rattus sp.
Manually annotated by BRENDA team
Pan, C.Q.; Lazarus, R.A.
Engineering hyperactive variants of human deoxyribonuclease I by altering its functional mechanism
Biochemistry
36
6624-6632
1997
Homo sapiens
Manually annotated by BRENDA team
Yasuda, T.; Awazu, S.; Sato, W.; Iida, R.; Tanaka, Y.; Kishi, K.
Human gentically polymorphic deoxyribonuclease: purification, characterization, and multiplicity of urine deoxyribonuclease I
J. Biochem.
108
393-398
1990
Homo sapiens
Manually annotated by BRENDA team
Ito, K.; Minamiura, N.; Yamamato, T.
Human urine DNase I: Immunological identity with human pancreatic DNase I, and enzyme and proteochemical properties of the enzyme
J. Biochem.
95
1399-1406
1984
Homo sapiens
Manually annotated by BRENDA team
Love, J.D.; Hewitt, R.R.
The realtionship between human serum and human pancreatic DNase I
J. Biol. Chem.
254
12588-12594
1979
Homo sapiens
Manually annotated by BRENDA team
Murai, K.; Yamanaka, M.; Akagi, K.; Anai, M.; Mukai, T.; Omae, T.
Purification and properties of deoxyribonuclease from human urine
Biochim. Biophys. Acta
517
186-194
1978
Homo sapiens
Manually annotated by BRENDA team
Funakoshi, A.; Tsubota, Y.; Wakasugi, H.; Ibayashi, H.; Takagi, Y.
Purification and properties of human pancreatic deoxyribonuclease I
J. Biochem.
82
1771-1777
1977
Homo sapiens
Manually annotated by BRENDA team
Yusifov, T.N.; Abduragimov, A.R.; Gasymov, O.K.; Glasgow, B.J.
Endonuclease activity in lipocalins
Biochem. J.
347
815-819
2000
Homo sapiens
-
Manually annotated by BRENDA team
Shiokawa, D.; Tanuma, S.
Characterization of human DNase I family endonucleases and activation of DNase gamma during apoptosis
Biochemistry
40
143-152
2001
Homo sapiens (P24855), Homo sapiens
Manually annotated by BRENDA team
Yatouji, S.; Liautaud-Roger, F.; Dufer, J.
Nuclear chromatin texture and sensitivity to DNase I in human leukaemic CEM cells incubated with nanomolar okadaic acid
Cell Prolif.
33
51-62
2000
Homo sapiens
Manually annotated by BRENDA team
Tsutsumi, S.; Kaneko, Y.; Asao, T.; Kuwano, H.; Kudo, S.; Takeshita, H.; Yasuda, T.; Kishi, K.
DNase I is present in the chief cells of human and rat stomachs
Histochem. J.
33
531-535
2002
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Babina, S.E.; Kanyshkova, T.G.; Buneva, V.N.; Nevinsky, G.A.
Lactoferrin is the major deoxyribonuclease of human milk
Biochemistry (Moscow)
69
1006-1015
2004
Homo sapiens
Manually annotated by BRENDA team
Baranovskii, A.G.; Buneva, V.N.; Nevinsky, G.A.
Human deoxyribonucleases
Biochemistry (Moscow)
69
587-601
2004
Homo sapiens
Manually annotated by BRENDA team
Kawai, Y.; Yoshida, M.; Arakawa, K.; Kumamoto, T.; Morikawa, N.; Masamura, K.; Tada, H.; Ito, S.; Hoshizaki, H.; Oshima, S.; Taniguchi, K.; Terasawa, H.; Miyamori, I.; Kishi, K.; Yasuda, T.
Diagnostic use of serum deoxyribonuclease I activity as a novel early-phase marker in acute myocardial infarction
Circulation
109
2398-2400
2004
Homo sapiens
Manually annotated by BRENDA team
Fujihara, J.; Hieda, Y.; Xue, Y.; Nakagami, N.; Imamura, S.; Takayama, K.; Kataoka, K.; Takeshita, H.
Actin-inhibition and folding of vertebrate deoxyribonuclease I are affected by mutations at residues 67 and 114
Comp. Biochem. Physiol. B
143
70-75
2006
Gloydius blomhoffii, Elaphe quadrivirgata, Xenopus laevis, Sus scrofa (P11936), Sus scrofa, Homo sapiens (P24855), Homo sapiens
Manually annotated by BRENDA team
Oliveri, M.; Daga, A.; Lunardi, C.; Navone, R.; Millo, R.; Puccetti, A.
DNase I behaves as a transcription factor which modulates fas expression in human cells
Eur. J. Immunol.
34
273-279
2004
Homo sapiens
Manually annotated by BRENDA team
Chhabra, D.; Nosworthy, N.J.; dos Remedios, C.G.
The N-terminal fragment of gelsolin inhibits the interaction of DNase I with isolated actin, but not with the cofilin-actin complex
Proteomics
5
3131-3136
2005
Homo sapiens
Manually annotated by BRENDA team
Lichtinghagen, R.
Determination of Pulmozyme (dornase alpha) stability using a kinetic colorimetric DNase I activity assay
Eur. J. Pharm. Biopharm.
63
365-368
2006
Homo sapiens
Manually annotated by BRENDA team
Cherepanova, A.; Tamkovich, S.; Pyshnyi, D.; Kharkova, M.; Vlassov, V.; Laktionov, P.
Immunochemical assay for deoxyribonuclease activity in body fluids
J. Immunol. Methods
325
96-103
2007
Homo sapiens
Manually annotated by BRENDA team
Fujihara, J.; Takatsuka, H.; Kataoka, K.; Xue, Y.; Takeshita, H.
Two deoxyribonuclease I gene polymorphisms and correlation between genotype and its activity in Japanese population
Leg. Med.
9
233-236
2007
Homo sapiens
Manually annotated by BRENDA team
Fukano, H.; Suzuki, Y.
Enzymatic conversion of long DNA to small DNA fragments for the construction of short hairpin RNA expression libraries
Anal. Biochem.
385
80-84
2009
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Takeshita, H.; Soejima, M.; Koda, Y.; Yasuda, T.; Takatsuka, H.; Fujihara, J.
Gln222Arg (A2317G) polymorphism in the deoxyribonuclease I gene exhibits ethnic and functional differences
Clin. Chem. Lab. Med.
47
51-55
2009
Homo sapiens
Manually annotated by BRENDA team
Napirei, M.; Ludwig, S.; Mezrhab, J.; Klckl, T.; Mannherz, H.G.
Murine serum nucleases - contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1/3)
FEBS J.
276
1059-1073
2009
Homo sapiens, Mus musculus (O55070), Mus musculus, Mus musculus C57BL/6 (O55070)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Boyano, M.D.; Andollo, N.; Zalduendo, M.M.; Archaga, J.
Association between practice patterns and body mass index percentile in infants and young children with cystic fibrosis
J. Cyst. Fibros.
7
385-390
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zhao, W.; Lam, J.C.; Chiuman, W.; Brook, M.A.; Li, Y.
Enzymatic cleavage of nucleic acids on gold nanoparticles: a generic platform for facile colorimetric biosensors
Small
4
810-816
2008
Homo sapiens
Manually annotated by BRENDA team
Wahlberg, K.; Jiang, J.; Rooks, H.; Jawaid, K.; Matsuda, F.; Yamaguchi, M.; Lathrop, M.; Thein, S.L.; Best, S.
The HBS1L-MYB intergenic interval associated with elevated HbF levels shows characteristics of a distal regulatory region in erythroid cells
Blood
114
1254-1262
2009
Homo sapiens
Manually annotated by BRENDA team
Yasuda, T.; Ueki, M.; Takeshita, H.; Fujihara, J.; Kimura-Kataoka, K.; Iida, R.; Tsubota, E.; Soejima, M.; Koda, Y.; Kato, H.; Panduro, A.
A biochemical and genetic study on all non-synonymous single nucleotide polymorphisms of the gene encoding human deoxyribonuclease I potentially relevant to autoimmunity
Int. J. Biochem. Cell Biol.
42
1216-1225
2010
Homo sapiens (P24855), Homo sapiens
Manually annotated by BRENDA team
Dou, Y.; Yang, X.
Novel high-sensitive fluorescent detection of deoxyribonuclease I based on DNA-templated gold/silver nanoclusters
Anal. Chim. Acta
784
53-58
2013
Homo sapiens
Manually annotated by BRENDA team
Parsiegla, G.; Noguere, C.; Santell, L.; Lazarus, R.A.; Bourne, Y.
The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily
Biochemistry
51
10250-10258
2012
Homo sapiens (P24855), Homo sapiens
Manually annotated by BRENDA team
Skiljevic, D.; Jeremic, I.; Nikolic, M.; Andrejevic, S.; Sefik-Bukilica, M.; Stojimirovic, B.; Bonaci-Nikolic, B.
Serum DNase I activity in systemic Lupus erythematosus: correlation with immunoserological markers, the disease activity and organ involvement
Clin. Chem. Lab. Med.
51
1083-1091
2013
Homo sapiens
Manually annotated by BRENDA team
Zhu, B.; Gong, Y.; Chen, P.; Zhang, H.; Zhao, T.; Li, P.
Increased DNase I activity in diabetes might be associated with injury of pancreas
Mol. Cell. Biochem.
393
23-32
2014
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ershova, E.; Sergeeva, V.; Klimenko, M.; Avetisova, K.; Klimenko, P.; Kostyuk, E.; Veiko, N.; Veiko, R.; Izevskaya, V.; Kutsev, S.; Kostyuk, S.
Circulating cell-free DNA concentration and DNase I activity of peripheral blood plasma change in case of pregnancy with intrauterine growth restriction compared to normal pregnancy
Biomed. Rep.
7
319-324
2017
Homo sapiens (P24855), Homo sapiens
Manually annotated by BRENDA team