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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Arabidopsis thaliana and UniProt Accession O78310
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1.15.1.1 superoxide dismutaseIUBMB 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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Word Map
- 1.15.1.1
- catalase
- malondialdehyde
- gsh
- necrosis
- endothelial
- tnf
- wistar
- artery
- ascorbate
- gsh-px
- caspase-3
- cholesterol
- cardiac
-
reperfusion
-
neuroprotective
- sclerosis
-
tbars
-
anti-oxidant
- ischemia
-
thiobarbituric
- myocardial
- triglyceride
-
alt
-
amyotrophic
-
mime
-
sacrificed
- chlorophyll
-
neurotoxicity
- hippocampus
- myeloperoxidase
- infarct
- cerebral
- xanthine
-
hepatotoxicity
- streptozotocin
-
albino
-
sham
- creatinine
-
ischemia-reperfusion
- bcl-2
- s-transferase
- glutathione-s-transferase
-
hepatoprotective
- diagnostics
-
chemiluminescence
- synthesis
-
gavage
-
cardioprotective
- ceruloplasmin
- drug development
- oxygenase-1
-
endothelium-dependent
- peroxynitrite
- environmental protection
- analysis
- biotechnology
- medicine
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
-
-
-
-
Fe-SOD
-
-
-
-
SOD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
9054-89-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
-
one copper chaperone gene for superoxide dismutase is responsible for the activation of cytosolic, peroxisomal and chloroplast enzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
additional information
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated
physiological function
superoxide dismutases (SODs) are key enzymes functioning as the first line of antioxidant defense by virtue of the ability to convert highly reactive superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a central role in protecting plants against the toxic effects of reactive oxygen species generated during normal cellular metabolic activity or as a result of various environmental stresses, regulation mechanisms and functional role(s) during development and in response to biotic or abiotic stresses, overview. The effect of a particular stress on SOD gene expression is likely governed by the subcellular sites at which oxidative stress is generated. Molecular mechanisms of GTACT motif-dependent transcriptional suppression by Cu2+ are conserved in land plants
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
-
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
additional information
distribution, subcellular location, and physicochemical properties of the Mn-, Fe-, Cu/Zn-, and Ni-SODs, and molecular mechanism of regulation of SOD gene expression, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SODC2_ARATH
216
0
22244
Swiss-Prot
Chloroplast (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
additional information
-
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
additional information
posttranscriptional regulation of SODs, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
microRNA miR398, conserved in several plant species, targets two of the three Cu/Zn-SODs of Arabidopsis thaliana (CSD1 and CSD2) by triggering cleavage or inhibiting translation of their mRNAs
overexpression of yeast transcription factor ACE1 in Arabidopsis thaliana increases the activities of Cu/Zn-SOD, indicating that ACE1 plays an important role in the regulation of SOD gene expression. The Cu/ZnSOD gene is remarkably activated by ginsenoside Rb2 through transcription factor AP2 binding sites and its induction
regulation of the expression of miR398, overview. Effects of abiotic and biotic stresses on SOD expression, overview
effects of abiotic and biotic stresses on SOD expression, overview
microRNA miR398, conserved in several plant species, targets two of the three Cu/Zn-SODs of Arabidopsis thaliana (CSD1 and CSD2) by triggering cleavage or inhibiting translation of their mRNAs
overexpression of yeast transcription factor ACE1 in Arabidopsis thaliana increases the activities of Cu/Zn-SOD, indicating that ACE1 plays an important role in the regulation of SOD gene expression. The Cu/ZnSOD gene is remarkably activated by ginsenoside Rb2 through transcription factor AP2 binding sites and its induction
regulation of the expression of miR398, overview. Effects of abiotic and biotic stresses on SOD expression, overview
the Arabidopsis thaliana Fe-SOD gene promoter containing the GTACT motif is repressed by Cu2+. Molecular mechanisms of GTACT motif-dependent transcriptional suppression by Cu2+ are conserved in land plants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chu, C.C.; Lee, W.C.; Guo, W.Y.; Pan, S.M.; Chen, L.J.; Li, H.M.; Jinn, T.L.
A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis
Plant Physiol.
139
425-436
2005
Arabidopsis thaliana
Wang, W.; Xia, M.X.; Chen, J.; Yuan, R.; Deng, F.N.; Shen, F.F.
Gene expression characteristics and regulation mechanisms of superoxide dismutase and its physiological roles in plants under stress
Biochemistry (Moscow)
81
465-480
2016
Arabidopsis thaliana, Arabidopsis thaliana (O78310), Arabidopsis thaliana (P24704), Glycine max, Nicotiana tabacum, Pleurotus ostreatus, Populus trichocarpa, Zea mays, Nicotiana benthamiana, Raphanus sativus var. raphanistroides, Gypsophila oblanceolata, Rhodobacter capsulatus (O30970), Rattus norvegicus (P07632), Rattus norvegicus (P07895), Pseudomonas putida (P09223), Nicotiana plumbaginifolia (P11796), Nicotiana plumbaginifolia (P22302), Nicotiana plumbaginifolia (P27082), Nostoc sp. PCC 7120 = FACHB-418 (Q8YSZ1)
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