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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Danio rerio and UniProt Accession Q2TV65

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EC Tree
IUBMB Comments
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
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This record set is specific for:
Danio rerio
UNIPROT: Q2TV65
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
2
+
2
=
+
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
manganese superoxide dismutase
-
copper-zinc superoxide dismutase
-
-
-
-
Cu,Zn-SOD
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
cuprein
-
-
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
-
-
-
-
erythrocuprein
-
-
-
-
Fe-SOD
-
-
-
-
ferrisuperoxide dismutase
-
-
-
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
Mn-SOD
-
-
-
-
SOD
-
-
-
-
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
superoxide:superoxide oxidoreductase
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-89-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2- + H+
O2 + H2O2
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
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibitory: sodium dodecyl sulfate up to 4%
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2000
-
pH 10.2, 25°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.2 - 11.2
high enzyme activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.29
sequence calculation, MnSOD
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2TV65_DANRE
224
0
24978
TrEMBL
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24989
x * 24989, sequence calculation, MnSOD
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 24989, sequence calculation, MnSOD
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3 - 12
-
-
659841
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
purified recombinant enzyme, half-life is 48 min
80
purified recombinant enzyme, 48% remaining activity after 10 min
90
purified recombinant enzyme, inactivation after 10 min
70
-
10 min, 40% residual activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable in presence of 4% SDS
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain QC779
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, real-time RT-PCR expression analysis, sequence comparisons, expression in Escherichia coli strain QC779
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
soaking fish larva in enzyme solution protects fish from 100 ppm paraquat-induced oxidative injury
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ken, C.F.; Lin, C.T.; Shaw, J.F.; Wu, J.L.
Characterization of fish Cu/Zn-superoxide dismutase and its protection from oxidative stress
Mar. Biotechnol.
5
167-173
2003
Danio rerio
Manually annotated by BRENDA team
Lin, C.T.; Tseng, W.C.; Hsiao, N.W.; Chang, H.H.; Ken, C.F.
Characterization, molecular modelling and developmental expression of zebrafish manganese superoxide dismutase
Fish Shellfish Immunol.
27
318-324
2009
Danio rerio (Q2TV65), Danio rerio, Danio rerio AB (Q2TV65)
Manually annotated by BRENDA team