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Information on EC 3.1.21.1 - deoxyribonuclease I and Organism(s) Oreochromis mossambicus and UniProt Accession O42446

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This record set is specific for:
Oreochromis mossambicus
UNIPROT: O42446 not found.
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Word Map
The taxonomic range for the selected organisms is: Oreochromis mossambicus
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
-
-
-
-
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
-
-
-
-
additional information
enzyme belongs to the piscine DNase I family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
show the reaction diagram
preference for double-stranded DNA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
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
double-stranded DNA + H2O
5'-phosphooligonucleotides + ?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
highest activity at 10 mM, doubled activity upon addition of 1 mM Ca2+
Mn2+
-
highest activity at 1 mM, addition of Ca2+ doesn't change activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
-
50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
about, 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
8.5
-
in the presence of Mg2+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
tilapia
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNAS1_OREMO
284
1
32216
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
gel filtration, SDS-PAGE, thin-layer IEF, MS analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 30000, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
carbohydrate-chain at Asn 18
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
inactivation after 10 min incubation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
14000fold from hepatopancreas
to homogeneity by 4step chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
deducing amino acid composition from cDNA
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hsiao, Y.M.; Ho, H.C.; Wang, W.Y.; Tam, M.F.; Liao, T.H.
Purification and characterization of tilapia (Oreochromis mossambicus) deoxyribonuclease I. Primary structure and cDNA sequence
Eur. J. Biochem.
249
786-791
1997
Oreochromis mossambicus
Manually annotated by BRENDA team
Yasuda, T.; Takeshita, H.; Iida, R.; Ueki, M.; Nakajima, T.; Kaneko, Y.; Mogi, K.; Kominato, Y.; Kishi, K.
A single amino acid substitution can shift the optimum pH of DNase I for enzyme activity: biochemical and molecular analysis of the piscine DNase I family
Biochim. Biophys. Acta
1672
174-183
2004
Takifugu rubripes, Oreochromis mossambicus (O42446), Oreochromis mossambicus, Pagrus major (Q5KTT0), Pagrus major, Anguilla japonica (Q5KTT1), Anguilla japonica, Cyprinus carpio (Q8JIP7)
Manually annotated by BRENDA team