3.1.21.1: deoxyribonuclease I
This is an abbreviated version!
For detailed information about deoxyribonuclease I, go to the full flat file.
Word Map on EC 3.1.21.1
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3.1.21.1
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footprint
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polymerases
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chromatin
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strand
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milk
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neutrophil
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single-stranded
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lysozyme
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exonuclease
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herpes
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bacteriophage
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viruses
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phage
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histone
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triphosphate
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simplex
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transferrin
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polymerization
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infant
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transcriptase
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immunoglobulin
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actin
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fidelity
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nucleosome
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duplex
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myeloperoxidase
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mismatch
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thymidine
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cytomegalovirus
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dntp
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protein-dna
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fork
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sequence-specific
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pcna
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sp1
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endonucleases
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herpesvirus
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iga
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dna-protein
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micrococcal
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nucleases
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ganciclovir
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whey
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beta-globin
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supercoiled
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exotoxin
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dna-dependent
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ssdna
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medicine
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diagnostics
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streptokinase
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molecular biology
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analysis
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lamivudine
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pharmacology
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degradation
- 3.1.21.1
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footprint
- polymerases
- chromatin
- strand
- milk
- neutrophil
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single-stranded
- lysozyme
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exonuclease
- herpes
- bacteriophage
- viruses
- phage
- histone
- triphosphate
- simplex
- transferrin
- polymerization
- infant
- transcriptase
- immunoglobulin
- actin
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fidelity
- nucleosome
- duplex
- myeloperoxidase
- mismatch
- thymidine
- cytomegalovirus
- dntp
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protein-dna
- fork
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sequence-specific
- pcna
- sp1
- endonucleases
- herpesvirus
- iga
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dna-protein
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micrococcal
- nucleases
- ganciclovir
- whey
- beta-globin
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supercoiled
-
exotoxin
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dna-dependent
- ssdna
- medicine
- diagnostics
- streptokinase
- molecular biology
- analysis
- lamivudine
- pharmacology
- degradation
Reaction
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products =
Synonyms
alkaline deoxyribonuclease, alkaline DNase, alkaline nuclease, bovine pancreatic deoxyribonuclease I, bovine pancreatic DNase, bp-DNase I, bpDNase, carp liver DNase, ColE7, ColE9, colicin, colicin E2, Colicin E9, CRM197, deoxyribonuclease, deoxyribonuclease (pancreatic), deoxyribonuclease 1, deoxyribonuclease 1-like 3, deoxyribonuclease A, deoxyribonuclease I, deoxyribonuclease I-like enzyme, deoxyribonuclease-1, deoxyribonucleic phosphatase, desoxyribonuclease, diphtheria toxin, DNA endonuclease, DNA nuclease, DNA polymerase, DNAase, DNase, DNase 1, DNase A, DNase B, DNase C, DNase D, DNase I, DNase I-like enzyme, Dnase Y, DNase-I, Dnase1, DNase1-like 3, DNase1/3, DNASE1L3, DNaseI, domase, Dornase alfa, dornase alpha, dornava, dornavac, DTx, E9 Dnase, EC 3.1.4.5, endodeoxyribinuclease I, endodeoxyribonuclease I, EndoDNase, Escherichia coli endonuclease I, extracellular nuclease, hDNase I, lactoferrin, More, neutral DNase, neutral nuclease, nuclease Bh1, nuclease Stn beta, nuclease, deoxyribo-, nuclease, Escherichia coli endo-, I, NucT, OmpA, outer membrane protein A, pancreatic deoxyribonuclease, pancreatic DNase, pancreatic DNase I, pancreatic dornase, Potyviral Ia Proeinase, pulmozyme, rhDNaseI, PVBV proteinase, SdaD2, Slx1, Spd, Spd3, SsnA, streptodornase, tear lipocalin, thymonuclease, type I DNAse I, Vvn
ECTree
3.1.21.1 deoxyribonuclease IAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.1.21.1 - deoxyribonuclease I
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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
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2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
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2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
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2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-(4-amidinophenyl)-6-indolecarbamidine
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significantly inhibits DNase I activity
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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aurintricarboxylic acid
i.e ATA, a general inhibitor of nucleases, weak inhibition
calf spleen inhibitor protein II
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molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7
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calf thymus inhibitor protein
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molecular weight: 49000 Da, maximum stability at pH 6
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Cholesterol sulfate
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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
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at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min
plasmin
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
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protein Im9
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an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell
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RNA
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enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA
Somatostatin
2 enzyme forms: a somatostatin-sensitive and a somatostatin-resistant, controls the enzyme level in the lower gut, in vivo transient down-regulation of gene expression of the sensitive enzyme form
Tris
increasing concentrations of Tris (approximately half activity in the presence of 80 mM Tris) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (no inhibitory influence of Tris)
2-mercaptoethanol
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inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
2-Nitro-5-thiocyanobenzoic acid
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inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135
2-nitro-5-thiosulfobenzoic acid
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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
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is a novel inhibitor specific for DNase I
actin
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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
inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage
EDTA
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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
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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
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G-actin
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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
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iodoacetate
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formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
iodoacetate
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50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min
mannitol
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inhibition of enzyme activity during the entire growth period of seedlings
mannitol
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induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days
N-bromosuccinimide
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modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
NaCl
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50% inhibition at 60 mM, mutated enzyme less sensitive against increased salt concentrations
NaCl
increasing concentrations of NaCl (approximately half activity in the presence of 50 mM NaCl) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (approximately half activity in the presence of 150 mM NaCl)
Trypsin
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is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
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Trypsin
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
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additional information
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the phosphate residue is responsible for the inhibitory effect of guanosine 5'-nucleotides
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additional information
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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
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additional information
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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
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additional information
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DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
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additional information
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no inhibition by G-actin; no inhibition by G-actin
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additional information
no inhibition by G-actin; no inhibition by G-actin
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additional information
resistant to trypsin inactivation in absence of Ca2+
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additional information
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resistant to trypsin inactivation in absence of Ca2+
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additional information
G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
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additional information
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G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
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additional information
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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
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additional information
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
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additional information
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DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
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additional information
no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
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additional information
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no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
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