Information on EC 3.1.21.1 - deoxyribonuclease I

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.21.1
-
RECOMMENDED NAME
GeneOntology No.
deoxyribonuclease I
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
CAS REGISTRY NUMBER
COMMENTARY hide
9003-98-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC19606T
-
-
Manually annotated by BRENDA team
strain ATCC19606T
-
-
Manually annotated by BRENDA team
eel
SwissProt
Manually annotated by BRENDA team
multifunctional enzyme
-
-
Manually annotated by BRENDA team
Bufo vulgaris japonicus
-
SwissProt
Manually annotated by BRENDA team
strain N2
-
-
Manually annotated by BRENDA team
strain N2
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
spruce budworm
-
-
Manually annotated by BRENDA team
japanese quail
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
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
Mus musculus C57BL/6
C57BL/6 mice
Uniprot
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
sea urgin
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Potyvirus sp.
-
-
-
Manually annotated by BRENDA team
-
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
fungus
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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)
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
DNA + H2O
5'-phosphodinucleotides + 5'-phosphooligonucleotides
show the reaction diagram
-
-
-
?
DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
DNA + H2O
5'-phosphotrinucleotides + ?
show the reaction diagram
double-stranded circular DNA + H2O
?
show the reaction diagram
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
double-stranded DNA + H2O
?
show the reaction diagram
double-stranded linear DNA + H2O
?
show the reaction diagram
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
dsDNA + H2O
?
show the reaction diagram
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
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
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
phage M13 DNA + H2O
?
show the reaction diagram
-
endolytically cleavage generating single base nicks
-
?
plasmid DNA + H2O
?
show the reaction diagram
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
RNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
RNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
RNA + H2O
?
show the reaction diagram
-
low activity
-
?
salmon sperm DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
salmon sperm DNA + H2O
?
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
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
-
?
single-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
ssDNA + H2O
?
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
?
supercoiled plasmid DNA + H2O
linear DNA + ?
show the reaction diagram
supercoiled pUC18 DNA + H2O
?
show the reaction diagram
-
endolytically cleavage generating single base nicks
-
?
Xenopus laevis DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
dsDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
dsDNA + H2O
?
show the reaction diagram
-
-
-
?
ssDNA + H2O
5'-phosphodinucleotide + 5'-phosphooligonucleotide
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
-
Cu2+
-
highest activity at 5 mM, but only 40% activtiy compared to Mg2+
KCl
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
MgCl2
Potyvirus sp.
-
-
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(4-amidinophenyl)-6-indolecarbamidine
-
significantly inhibits DNase I activity
2-mercaptoethanol
2-Nitro-5-thiocyanobenzoic acid
2-nitro-5-thiosulfobenzoic acid
5'-deoxy-GMP
-
competitive, product inhibition
Aflatoxin B2a
-
non-competitive inhibitor
Aflatoxin G2
-
non-competitive inhibitor
Aflatoxin G2a
-
non-competitive inhibitor
Aflatoxin M1
-
non-competitive inhibitor
Aprotinin
inhibits DNase1 as a result of plasmin inhibition
aurintricarboxylic acid
i.e ATA, a general inhibitor of nucleases, weak inhibition
Bile acids
-
inhibit the enzyme in concert with cholesterol sulfate
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
dithiothreitol
-
-
DTT
-
80% inhibition at 1 mM
E2-immunity protein
-
complete inhibition of activity on plasmid DNA
-
G-actin
gamma-actin
guanidinium hydrochloride
-
over 80% inhibition at 0.5 M
heparin
iodoacetate
K+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
mannitol
methanesulfonylchloride
-
inactivation at pH 5.0
N-bromosuccinimide
Na+
-
no inhibition at 50 mM, 50% inhibition at 200 mM
oligonucleotides
-
competitive inhibition
phosphate
plasmin
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
-
protein Im9
-
an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell
-
RNA
-
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)
Tris-HCl buffer
Trypsin
Urea
-
20% inhibition at 4 M
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
aflatoxin B1
-
effective activator below 0.08 mM
Aflatoxin B2
-
effective activator below 0.08 mM
Aflatoxin M2
-
effective activator below 0.08 mM
Aprotinin
activates DNase1/3-like activity
Bile
-
bile from rat , reconstitution of activity of inhibited DNase I-actin complex
-
bovine serum albumin
-
0.01 mg/reaction volume stimulates about 50% at both pH 6.2 and 7.7
-
dithiothreitol
-
-
heparin
activates DNase1
mannitol
-
induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days
N-ethylmaleimide
-
stimulation about 10-20% at both pH 6.2 and 7.7
okadaic acid
-
10 nM, increases accessibility to DNA in chromatin of carcinoma cells, changes the chromatin supraorganization to a more homgenous and fine chromatin texture as compared to control cells, causes apoptosis after exposure longer than 6 h, no effect on CEM-VLB100 cells
Slx4
-
the Slx4 protein is essential for efficient processing of DNA substrates
-
additional information
-
His44 may play a critical role in substrate DNA binding in the putative secondary active site, and introduction of sulfhydryl groups at Thr14 and Ser43 may facilitate Mn2+-coordination and further contribute to the catalytic activity of DNase I
-
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, 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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167 - 493.3
(pC)10
106.6
d(pA)10
Homo sapiens
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
703.3
d(pApCpTpApCpApGpTpCpTpApCpA)
Homo sapiens
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
0.0492 - 453.3
d(pGpGpCpApCpTpTpApC)
713
d(pT)10
Homo sapiens
-
20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37C
136.6
d(pTpApGpApApGpApTpCpApApA)
Homo sapiens
-
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 hide
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
-
-
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+
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
in the presence of Mg2+, dependent on bivalent metal ions
6 - 8
Asp44 is responsible for the higher pH optimum compared to vertebrates, residue 44 might have been involved in the evolutionary change of pH optimum for activity from piscine, reptile and amphibia to vertebrates, who possess a His44 residue and a lower pH optimum
6.2
-
in 25 mM cacodylate hydrochlorid and 3 mM Co2+
6.4
-
in the presence of Co2+ in 50 mM cacodylate-HCl buffer
6.75
-
DNase I type-1 enzyme
6.8
DNase I
7 - 8
depending on the metal ion use