Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.22.1 - deoxyribonuclease II and Organism(s) Homo sapiens and UniProt Accession O00115

for references in articles please use BRENDA:EC3.1.22.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: O00115 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
dnase ii, nuc-1, acid dnase, deoxyribonuclease ii, l-dnase ii, acid deoxyribonuclease, lei/l-dnase ii, dnase iialpha, dnase iibeta, dnase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyribonuclease II
-
DNase IIalpha
-
acid deoxyribonuclease
-
-
-
-
acid DNase
deoxyribonuclease IIalpha
-
deoxyribonuclease IIbeta
-
deoxyribonucleate 3'-nucleotidohydrolase
-
-
-
-
DNase 2
-
-
DNase 2a
-
-
DNase II
DNase IIalpha
-
DNase IIbeta
-
L-DNase II
-
-
LEI-derived DNase II
-
-
LEI/L-DNase II
-
-
leukocyte elastase inhibitor-derived DNase II
-
-
lysosomal DNase II
-
-
-
-
pancreatic DNase II
-
-
-
-
R31240_2
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-64-3
-
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
oligonucleotides + ?
show the reaction diagram
induces DNA digestion during apoptosis
-
?
salmon testicular DNA + H2O
?
show the reaction diagram
-
-
-
?
DNA + H2O
3' phosphooligonucleotides
show the reaction diagram
-
-
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
show the reaction diagram
DNA + H2O
oligonucleotides + ?
show the reaction diagram
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
show the reaction diagram
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
DNA + H2O
oligonucleotides + ?
show the reaction diagram
induces DNA digestion during apoptosis
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
show the reaction diagram
-
ethanol stress on ARPE-19 cells can induce a pathway which is a form of programmed cell death with characteristics of both apoptosis and necrosis, possibly by triggering conversion of leukocyte elastase inhibitor LEI to L-DNase II
-
-
?
DNA + H2O
oligonucleotides + ?
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
strong inhibition
Co2+
-
complete inhibition
Cu2+
-
complete inhibition
Fe3+
-
complete inhibition at 0.1 mM
Mg2+
-
strong inhibition
Mn2+
-
strong inhibition
tunicamycin
Zn2+
-
strong inhibition
additional information
-
caspases inhibitors have no effect on acid endonucleases, and no effect on apoptosis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AP-24
-
apoptotic protease of 24 kDa, is activated during apoptosis and is able to activate L-DNase II
-
cathepsin D
-
an acid protease, can transform LEI into L-DNase II
-
EDTA
-
slight activation
intracellular elastase
-
a neutral protease, can transform LEI into L-DNase II
-
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.42 - 0.51
-
-
additional information
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotynilated forward and fluorescein-labeled reverse primers
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5
-
-
5.1 - 5.3
-
in acetate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
during lens cell differentiation
Manually annotated by BRENDA team
low levels
Manually annotated by BRENDA team
low levels
Manually annotated by BRENDA team
low levels
Manually annotated by BRENDA team
low levels
Manually annotated by BRENDA team
low levels
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
LEI is concentrated around the nucleus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
DNase II gene shows relatively low genetic diversity with regard to the non-synonymous single nucleotide polymorphisms, suggesting that the enzyme has been well conserved
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNS2A_HUMAN
360
0
39581
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
gel filtration
32000
-
1 * 8000-10000 + 1 * 32000 + 1 * ?, cDNA and protein sequence analysis
36000
-
gel filtration
37000
-
unglycosylated form of wild-type enzyme and N69Q mutant upon tunicamycin treatment
38030
-
calculation from cDNA sequence
42000 - 44000
-
SDS-PAGE, mature protein
43000
-
mutants N86Q, N212Q, N266Q, N290Q. It appears that the four sites each contribute to glycosylation and no additional glycosylation sites are responsible for the observed size
45000
47000
-
D107N mutant, addition of glycosylation site
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
1 * 8000-10000 + 1 * 32000 + 1 * ?, cDNA and protein sequence analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structural model of protein. DNase IIalpha is a monomeric enzyme with pseudodimeric fold. It contains two requisite PLD-signature motifs in the N-terminal subdomains which together form a single active site
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A335Term
does not eliminate DNase II activity
A58del
in Japanese, African, Korean and Caucasian subjects, homozygous for the G292 allele. Shows almost no DNase II activity
H188A
shows similar levels of activity to that of the wild-type
H188K
shows similar levels of activity to that of the wild-type
H188R
in Japanese, African, Korean and Caucasian subjects, homozygous for the A683 allele. DNase II activity is similar to that of the wild-type
Q322Term
Q329Term
eliminates DNase II activity
R23A
exerts no effect on the DNase II activity
R23H
exerts no effect on the DNase II activity
R23I
in Japanese, African, Korean and Caucasian subjects, homozygous for the G188 allele. DNase II activity is similar to that of the wild-type
R298A
drastically abrogates DNase II activity
R298H
drastically abrogates DNase II activity
R298K
drastically abrogates DNase II activity
R298L
in Japanese, African, Korean and Caucasian subjects, homozygous for the G1013 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
V190I
in Korean subjects,heterozygous for the G688 and A688 alleles. In Japanese, homozygous for the G688 allele. DNase II activity is similar to that of the wild-type
V284A
activity remains low
V284L
activity remains low
V284M
in Japanese, African, Korean and Caucasian subjects, homozygous for the G970 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
C11A
-
the mutation decreases the activity
C159A
-
complete loss of activity
C19A
-
complete loss of activity
C267A
-
complete loss of activity
C299A
-
the mutation increases the activity
C308A
-
complete loss of activity
C327A
-
complete loss of activity
C347A
-
complete loss of activity
D107N
-
although the mutant is capable of even greater glycosylation, this mutant results in some loss of activity
H295A
N212Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N266Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N290Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N69Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N86Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
additional information
-
mutation of the histidine moiety of His 368 completely abolishes endonuclease activity of L-DNase II
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
irreversible loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 1 mM PMSF, 50% glycerol v/v, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
near homogeneity by 3step chromatography techniques
-
near homogeneity by 5step chromatography techniques
-
to homogeneity by 6step chromatography techniques
-
to homogeneity by chromatography steps and isoelectric focusing
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA fragment containing the entire coding sequence of DNase II cDNA amplified and ligated into pcDNA3.1(+). Mutants corresponding to each single nucleotide polymorphism expressed in COS-7 cell
expression in Chinese hamster ovary cells
expression in COS-7 cells
-
expression in human embryonic kidney 293 cells
-
MEF-/- cells null for enzyme expression and activity are transiently transfected with plasmid-expression constructs encoding wild-type human DNase IIalpha, pD2, or mutant forms
-
Sp1 and Sp3 play a pivotal role in the transcriptional activation of DNase II in HL-60 cells during phorbol 12-myristate-13-acetate induced differentiation
-
the gene encoding DNase IIbeta has identical splice sites to DNase IIalpha
the wild-type and mutant enzyme cDNA plasmid are transiently transfected in HCT116 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
non-synonymous single nucleotide polymorphisms in the DNase II gene may have clinical implications in relation to the prevalence of autoimmune diseases
analysis
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotinylated forward and fluorescein-labeled reverse primers
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, K.P.; Baron, W.F.; Henzel, W.J.; Spencer, S.A.
Molecular cloning and characterization of human and murine DNase II
Gene
215
281-289
1998
Homo sapiens, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Krieser, R.J.; Eastman, A.
The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis
J. Biol. Chem.
273
30909-30914
1998
Homo sapiens (O00115), Homo sapiens
Manually annotated by BRENDA team
Takeshita, H.; Yasuda, T.; Iida, R.; Nakajima, T.; Hosomi, O.; Nakashima, Y.; Mori, S.; Nomoto, H.; Kishi, K.
Identification of the three non-identical subunits cnstituting human deoxyribonuclease II
FEBS Lett.
440
239-242
1998
Homo sapiens
Manually annotated by BRENDA team
Yasuda, T.; Nadano, D.; Awazu, S.; Kishi, K.
Human urine deoxyribonuclease II (DNase II) isoenzymes: a novel immunoaffinity purification, biochemical multiplicity, genetic heterogeneity and broad distribution among tissues and body fluids
Biochim. Biophys. Acta
1119
185-193
1992
Homo sapiens
Manually annotated by BRENDA team
Harosh, I.; Binninger, D.M.; Harris, P.V.; Mezzina, M.; Boyd, J.B.
Mechanism of action of deoxyribonuclease II from human lymphoblasts
Eur. J. Biochem.
202
479-484
1991
Homo sapiens
Manually annotated by BRENDA team
Murai, K.; Yamanaka, M.; Akagi, K.; Anai, M.
Purification and properties of deoxyribonuclease II from human urine
J. Biochem.
87
1097-1103
1980
Homo sapiens
Manually annotated by BRENDA team
Slor, H.
Purification of 14C-labelled deoxyribonuclease II from HeLa S3 lysosomes and its use as a marker for the study of nuclear deoxyribonuclease II
Biochem. J.
136
83-87
1973
Homo sapiens
Manually annotated by BRENDA team
Schroeder, W.A.; Shelton, R.J.; Shelton, J.B.; Robberson, B.; Apell, G.
DNase II inhibitor in tissues and urine - pH and salt artifacts
Arch. Biochem. Biophys.
131
652-658
1969
Homo sapiens
Manually annotated by BRENDA team
MacLea, K.S.; Krieser, R.J.; Eastman, A.
Revised structure of the active form of human deoxyribonuclease IIalpha
Biochem. Biophys. Res. Commun.
292
415-421
2002
Homo sapiens (Q8WZ79), Homo sapiens
Manually annotated by BRENDA team
MacLea, K.S.; Krieser, R.J.; Eastman, A.
Structural requirements of human DNase II alpha for formation of the active enzyme: the role of the signal peptide, N-glycosylation, and disulphide bridging
Biochem. J.
371
867-876
2003
Homo sapiens
Manually annotated by BRENDA team
Chou, S.F.; Chen, H.L.; Lu, S.C.
Sp1 and Sp3 are involved in up-regulation of human deoxyribonuclease II transcription during differentiation of HL-60 cells
Eur. J. Biochem.
270
1855-1862
2003
Homo sapiens
Manually annotated by BRENDA team
Krieser, R.J.; MacLea, K.S.; Park, J.P.; Eastman, A.
The cloning, genomic structure, localization, and expression of human deoxyribonuclease IIbeta
Gene
269
205-216
2001
Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus
Manually annotated by BRENDA team
MacLea, K.S.; Krieser, R.J.; Eastman, A.
A family history of deoxyribonuclease II: surprises from Trichinella spiralis and Burkholderia pseudomallei
Gene
305
1-12
2003
Bos taurus (P56541), Caenorhabditis elegans (P34387), Caenorhabditis elegans (P34508), Caenorhabditis elegans (Q17778), Caenorhabditis elegans, Caenorhabditis elegans F09G8.2 (P34387), Caenorhabditis elegans K04H4.6 (P34508), Caenorhabditis elegans NUC-1 (Q17778), Drosophila melanogaster (Q7JYM9), Homo sapiens (O00115), Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus (P56542), Mus musculus (Q9QY48), Rattus norvegicus (Q9QZK8), Rattus norvegicus (Q9QZK9), Sus scrofa (O62855)
Manually annotated by BRENDA team
Evans, C.J.; Aguilera, R.J.
DNase II: genes, enzymes and function
Gene
322
1-15
2003
Caenorhabditis elegans, Caenorhabditis elegans NUC-1, Drosophila melanogaster, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Cymerman, I.A.; Meiss, G.; Bujnicki, J.M.
DNase II is a member of the phospholipase D superfamily
Bioinformatics
21
3959-3962
2005
Homo sapiens
Manually annotated by BRENDA team
Shin, H.D.; Park, B.L.; Cheong, H.S.; Lee, H.S.; Jun, J.B.; Bae, S.C.
DNase II polymorphisms associated with risk of renal disorder among systemic lupus erythematosus patients
J. Hum. Genet.
50
107-111
2005
Homo sapiens
Manually annotated by BRENDA team
Brossas, J.Y.; Tanguy, R.; Brignole-Baudouin, F.; Courtois, Y.; Torriglia, A.; Treton, J.
L-DNase II associated with active process during ethanol induced cell death in ARPE-19
Mol. Vis.
10
65-73
2004
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
Schaefer, P.; Cymerman, I.A.; Bujnicki, J.M.; Meiss, G.
Human lysosomal DNase IIalpha contains two requisite PLD-signature (HxK) motifs: evidence for a pseudodimeric structure of the active enzyme species
Protein Sci.
16
82-91
2007
Homo sapiens
Manually annotated by BRENDA team
Torriglia, A.; Lepretre, C.; Padron-Barthe, L.; Chahory, S.; Martin, E.
Molecular mechanism of L-DNase II activation and function as a molecular switch in apoptosis
Biochem. Pharmacol.
76
1490-1502
2008
Gallus gallus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Lepretre, C.; Fleurier, Y.; Martin, E.; Torriglia, A.
Nuclear export of LEI/L-DNase II by Crm1 is essential for cell survival
Biochim. Biophys. Acta
1783
1068-1075
2008
Cricetulus griseus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Liu, M.F.; Wu, X.P.; Wang, X.L.; Yu, Y.L.; Wang, W.F.; Chen, Q.J.; Boireau, P.; Liu, M.Y.
The functions of Deoxyribonuclease II in immunity and development
DNA Cell Biol.
27
223-228
2008
Acanthaster planci, Drosophila sp. (in: flies), Haemonchus contortus, Homo sapiens, Mus musculus, Sus scrofa, Trichinella spiralis
Manually annotated by BRENDA team
Ueki, M.; Takeshita, H.; Fujihara, J.; Kimura-Kataoka, K.; Iida, R.; Yuasa, I.; Nakajima, T.; Kominato, Y.; Yasuda, T.
Genetic and expression analysis of all 7 non-synonymous single nucleotide polymorphisms in the human deoxyribonuclease II gene, with potential relevance to autoimmunity
Clin. Chim. Acta
411
92-98
2010
Homo sapiens (O00115), Homo sapiens
Manually annotated by BRENDA team
Fischer, H.; Scherz, J.; Szabo, S.; Mildner, M.; Benarafa, C.; Torriglia, A.; Tschachler, E.; Eckhart, L.
DNase 2 is the main DNA-degrading enzyme of the stratum corneum
PLoS ONE
6
e17581
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Jaadane, I.; Nagbou, A.; Behar-Cohen, F.; Torriglia, A.
Interaction of leukocyte elastase inhibitor/L-DNase II with BCL-2 and BAX
Biochim. Biophys. Acta
1843
2807-2815
2014
Homo sapiens
Manually annotated by BRENDA team