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Literature summary extracted from
- Sources of marine superoxide dismutases characteristics and applications (2015), Int. J. Biol. Macromol., 79, 627-637 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | diagnostics | Cu/Zn-SOD might be used as a bioindicator of the aquatic environmental pollution and cellular stress in pearl oyster | Pinctada fucata |
| 1.15.1.1 | diagnostics | the SOD in the cosmopolitan sponge Cliona celata is described as a useful biomarker for marine pollution in other marine invertebrates | Cliona celata |
| 1.15.1.1 | diagnostics | the variations of SOD expression pattern in yrtilus. edulis can be used as a tool for the marine environment monitoring | Mytilus edulis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | Cu/Zn-SOD, DNA and amino acid sequence determination and analysis, semi-quantitative and/or real-time RT-PCR enzyme expression analysis | Haliotis discus discus |
| 1.15.1.1 | cytoplasmic manganese SOD, DNA and amino acid sequence determination and analysis | Penaeus vannamei |
| 1.15.1.1 | DNA and amino acid sequence determination and analysis | Bruguiera gymnorhiza |
| 1.15.1.1 | gene dhsod-1, DNA and amino acid sequence determination and analysis, sequence comparisons | Debaryomyces hansenii |
| 1.15.1.1 | gene Sod1, a single copy, expression analysis, recombinant expression in transgenic Oryza sativa plants, plants are more tolerant to methyl viologen mediated oxidative stress in comparison to the untransformed control plants and also withstand salinity stress | Avicennia marina |
| 1.15.1.1 | Mn-SOD, DNA and amino acid sequence determination and analysis, semi-quantitative and/or real-time RT-PCR enzyme expression analysis | Haliotis discus discus |
| 1.15.1.1 | recombinant expression in in a copper-tolerant yeast, Cryptococcus sp. strain N6, two distinct bands exhibiting SOD activity appear on native PAGE: one band, with higher mobility, appears when the cells are grown without CuSO4, and the other band appears when the cells are grown with 10 mM CuSO4. Cells grown with 3 mM CuSO4 produce both SOD isoforms | Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | SaFe-SOD, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis, functional recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami | Sonneratia alba |
| 1.15.1.1 | semi-quantitative enzyme expression analysis | Pinctada fucata |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | additional information | the enzyme is not significantly modified in light mitochondrial (LMF) fractions by any treatment | Sparus aurata |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.15.1.1 | a stable SOD in a broad pH range from 4 to 12, higher temperature, and in the presence of proteases | Conticribra weissflogii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.15.1.1 | azide | causes 50% inhibition at 20 mM | Porphyridium purpureum |  |
| 1.15.1.1 | diethyldithiocarbamate | strong inhibition | Gadus morhua | |
| 1.15.1.1 | H2O2 | - |
Ulva linza | |
| 1.15.1.1 | additional information | UV-B radiation decreases the SOD activity | Cylindrotheca closterium | |
| 1.15.1.1 | additional information | the enzyme shows good tolerance to some inhibitors, detergents, and denaturants | Geobacillus sp. EPT3 | |
| 1.15.1.1 | additional information | cyanide at 5 mM and H2O2 at 3 mM have no effect on the activity of the enzyme | Porphyridium purpureum | |
| 1.15.1.1 | additional information | the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE); the enzyme is insensitive to malondialdehyde (MDA) or 4-hydroxy-2-nonenal (HNE). Enzyme Mn-SOD is insensitive to cyanide | Sparus aurata | |
| 1.15.1.1 | additional information | the enzyme is insensitive to potassium cyanide | Ulva linza |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.15.1.1 | chloroplast | - |
Ulva linza | 9507 | - |
| 1.15.1.1 | cytoplasm | - |
Penaeus vannamei | 5737 | - |
| 1.15.1.1 | cytosol | - |
Bruguiera gymnorhiza | 5829 | - |
| 1.15.1.1 | cytosol | - |
Sparus aurata | 5829 | - |
| 1.15.1.1 | cytosol | - |
Schwanniomyces vanrijiae var. vanrijiae | 5829 | - |
| 1.15.1.1 | cytosol | no signal peptide is identified at the N-terminal amino acid sequence of Cu/Zn-SOD indicating that this pfSOD encodes a cytoplasmic Cu/Zn-SOD | Pinctada fucata | 5829 | - |
| 1.15.1.1 | cytosol | three isoforms of Cu/Zn-SOD | Mytilus edulis | 5829 | - |
| 1.15.1.1 | extracellular | - |
Crassostrea gigas | - |
- |
| 1.15.1.1 | mitochondrion | in the light mitochondrial fraction | Sparus aurata | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Mytilus edulis | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Crassostrea gigas | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Bruguiera gymnorhiza | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Haliotis discus discus | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Sparus aurata | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Schwanniomyces vanrijiae var. vanrijiae | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Lampanyctus crocodilus | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD | Xiphias gladius | |
| 1.15.1.1 | Cu2+ | a Cu-Zn-SOD | Debaryomyces hansenii | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc | Pinctada fucata | |
| 1.15.1.1 | Cu2+ | a Cu/Zn-SOD. The isolated enzyme has 30% of its copper in the reduced state | Prionace glauca | |
| 1.15.1.1 | Fe2+ | a Fe-SOD | Lingulodinium polyedra | |
| 1.15.1.1 | Fe2+ | a Fe-SOD | Nodularia sp. (in: Bacteria) | |
| 1.15.1.1 | Fe2+ | a Fe-SOD | Ulva linza | |
| 1.15.1.1 | Fe2+ | a Fe-SOD, all iron-binding sites (His 27, His 80, Asp 164 and His 168) of SaFe-SOD are conserved | Sonneratia alba | |
| 1.15.1.1 | Fe2+ | a Fe-SOD, the dimeric enzyme contains one iron atom/subunit | Photobacterium leiognathi | |
| 1.15.1.1 | Mn2+ | a Mn-SOD | Penaeus vannamei | |
| 1.15.1.1 | Mn2+ | a Mn-SOD | Haliotis discus discus | |
| 1.15.1.1 | Mn2+ | a Mn-SOD | Geobacillus sp. EPT3 | |
| 1.15.1.1 | Mn2+ | a Mn-SOD | Sparus aurata | |
| 1.15.1.1 | Mn2+ | a Mn-SOD, Mn2+ constitutes 0.13% of the enzyme, equivalent to one manganese atom per molecule of enzyme | Porphyridium purpureum | |
| 1.15.1.1 | additional information | exposure to a pH of 3.8 in the presence of 8.0 M urea labilizes the manganese and allows the preparation of a colorless and inactive apoenzyme, that can be reconstituted by subsequent treatment with MnCl2 | Porphyridium purpureum | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Mytilus edulis | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Crassostrea gigas | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Bruguiera gymnorhiza | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Haliotis discus discus | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Sparus aurata | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Schwanniomyces vanrijiae var. vanrijiae | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Lampanyctus crocodilus | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Xiphias gladius | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD | Prionace glauca | |
| 1.15.1.1 | Zn2+ | a Cu-Zn-SOD | Debaryomyces hansenii | |
| 1.15.1.1 | Zn2+ | a Cu/Zn-SOD, conserved amino acids required for binding copper and zinc | Pinctada fucata | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | additional information | - |
two distinct bands exhibiting SOD activity appear on native PAGE: one band, with higher mobility, appears when the cells are grown without CuSO4, and the other band appears when the cells are grown with 10 mM CuSO4. Cells grown with 3 mM CuSO4 produce both SOD isoforms | Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | 46000 | - |
gel filtration | Ulva linza |
| 1.15.1.1 | 130000 | - |
isozyme 3, native PAGE | Mytilus edulis |
| 1.15.1.1 | 155000 | - |
isozyme 2, native PAGE | Mytilus edulis |
| 1.15.1.1 | 205000 | - |
isozyme 1, native PAGE | Mytilus edulis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.15.1.1 | 2 superoxide + 2 H+ | Photobacterium leiognathi | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Porphyridium purpureum | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Mytilus edulis | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Crassostrea gigas | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Gadus morhua | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Penaeus vannamei | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Debaryomyces hansenii | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Lingulodinium polyedra | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Tetraselmis subcordiformis | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Conticribra weissflogii | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Avicennia marina | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Bruguiera gymnorhiza | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Apostichopus japonicus | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Pinctada fucata | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Sonneratia alba | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Tetraselmis gracilis | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Alvinella pompejana | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Haliotis discus discus | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Geobacillus sp. EPT3 | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Sparus aurata | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Photobacterium sepia | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Nodularia sp. (in: Bacteria) | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Minutocellus polymorphus | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Cylindrotheca closterium | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Ulva linza | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Schwanniomyces vanrijiae var. vanrijiae | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Lampanyctus crocodilus | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Xiphias gladius | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Prionace glauca | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Cliona celata | - |
O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | Schwanniomyces vanrijiae var. vanrijiae 020 | - |
O2 + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.15.1.1 | Alvinella pompejana | - |
from chimney walls of deep sea hydrothermal vents along the East Pacific Rise | - |
| 1.15.1.1 | Apostichopus japonicus | - |
- |
- |
| 1.15.1.1 | Avicennia marina | - |
- |
- |
| 1.15.1.1 | Bruguiera gymnorhiza | - |
- |
- |
| 1.15.1.1 | Cliona celata | - |
- |
- |
| 1.15.1.1 | Conticribra weissflogii | - |
- |
- |
| 1.15.1.1 | Crassostrea gigas | - |
- |
- |
| 1.15.1.1 | Cylindrotheca closterium | - |
- |
- |
| 1.15.1.1 | Debaryomyces hansenii | - |
- |
- |
| 1.15.1.1 | Gadus morhua | - |
- |
- |
| 1.15.1.1 | Geobacillus sp. EPT3 | T1T1K2 | - |
- |
| 1.15.1.1 | Haliotis discus discus | - |
- |
- |
| 1.15.1.1 | Lampanyctus crocodilus | - |
- |
- |
| 1.15.1.1 | Lingulodinium polyedra | - |
formerly Gonyaulax polyedra | - |
| 1.15.1.1 | Minutocellus polymorphus | - |
- |
- |
| 1.15.1.1 | Mytilus edulis | - |
three isoforms of Cu/Zn-SOD | - |
| 1.15.1.1 | Nodularia sp. (in: Bacteria) | - |
- |
- |
| 1.15.1.1 | Penaeus vannamei | - |
- |
- |
| 1.15.1.1 | Photobacterium leiognathi | - |
- |
- |
| 1.15.1.1 | Photobacterium sepia | - |
- |
- |
| 1.15.1.1 | Pinctada fucata | - |
- |
- |
| 1.15.1.1 | Porphyridium purpureum | - |
- |
- |
| 1.15.1.1 | Prionace glauca | - |
- |
- |
| 1.15.1.1 | Schwanniomyces vanrijiae var. vanrijiae | - |
- |
- |
| 1.15.1.1 | Schwanniomyces vanrijiae var. vanrijiae 020 | - |
- |
- |
| 1.15.1.1 | Sonneratia alba | - |
- |
- |
| 1.15.1.1 | Sparus aurata | M9NZV8 | - |
- |
| 1.15.1.1 | Sparus aurata | M9P0B0 | - |
- |
| 1.15.1.1 | Tetraselmis gracilis | - |
- |
- |
| 1.15.1.1 | Tetraselmis subcordiformis | - |
- |
- |
| 1.15.1.1 | Ulva linza | - |
- |
- |
| 1.15.1.1 | Xiphias gladius | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | Cu/Zn-SOD from digestive gland and gills | Mytilus edulis |
| 1.15.1.1 | Cu/Zn-SOD isozyme | Sparus aurata |
| 1.15.1.1 | from liver | Xiphias gladius |
| 1.15.1.1 | Mn-SOD isozyme | Sparus aurata |
| 1.15.1.1 | native enzyme by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration | Ulva linza |
| 1.15.1.1 | native enzyme to homogeneity | Porphyridium purpureum |
| 1.15.1.1 | recombinant His-tagged enzyme from Escherichia coli strain Rosetta-gami by nickel affinity chromatgraphy | Sonneratia alba |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.15.1.1 | digestive gland | - |
Mytilus edulis | - |
| 1.15.1.1 | flower | - |
Sonneratia alba | - |
| 1.15.1.1 | fruit | - |
Sonneratia alba | - |
| 1.15.1.1 | gill | - |
Mytilus edulis | - |
| 1.15.1.1 | gill | - |
Pinctada fucata | - |
| 1.15.1.1 | gill | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | heart | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | hemocyte | - |
Pinctada fucata | - |
| 1.15.1.1 | hemocyte | Cg-EcSOD-expressing hemocytes were seen in blood circulation, in connective tissues, and closely associated to endothelium blood vessels. Cg-EcSOD presents in its amino acid sequence a LPS-binding motif found in the endotoxin receptor CD14, the protein displays an affinity to Escherichia coli bacteria and to LPS and lipid A | Crassostrea gigas | - |
| 1.15.1.1 | hemocyte | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | hepatopancreas | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | intestine | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | leaf | - |
Bruguiera gymnorhiza | - |
| 1.15.1.1 | leaf | highest expression in leaf tissues | Sonneratia alba | - |
| 1.15.1.1 | liver | - |
Xiphias gladius | - |
| 1.15.1.1 | additional information | quantitative real-time PCR enzyme tissue expression analysis | Sonneratia alba | - |
| 1.15.1.1 | additional information | semi-quantitative enzyme expression analysis in adult tissues shows that the pfSOD mRNA is abundantly expressed in hemocytes and gill and scarcely expressed in other tissues tested | Pinctada fucata | - |
| 1.15.1.1 | muscle | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | nervous system | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | plasma | - |
Crassostrea gigas | - |
| 1.15.1.1 | pleopod | cytoplasmic manganese SOD | Penaeus vannamei | - |
| 1.15.1.1 | root | - |
Sonneratia alba | - |
| 1.15.1.1 | stem | - |
Sonneratia alba | - |
| 1.15.1.1 | trichome | - |
Nodularia sp. (in: Bacteria) | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | additional information | - |
value of SOD activity is 163.4 U/g total protein in wet tissues | Cliona celata |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Photobacterium leiognathi | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Porphyridium purpureum | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Mytilus edulis | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Crassostrea gigas | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Gadus morhua | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Penaeus vannamei | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Debaryomyces hansenii | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Lingulodinium polyedra | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Tetraselmis subcordiformis | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Conticribra weissflogii | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Avicennia marina | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Bruguiera gymnorhiza | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Apostichopus japonicus | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Pinctada fucata | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Sonneratia alba | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Tetraselmis gracilis | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Alvinella pompejana | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Haliotis discus discus | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Geobacillus sp. EPT3 | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Sparus aurata | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Photobacterium sepia | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Nodularia sp. (in: Bacteria) | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Minutocellus polymorphus | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Cylindrotheca closterium | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Ulva linza | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Schwanniomyces vanrijiae var. vanrijiae | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Lampanyctus crocodilus | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Xiphias gladius | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Prionace glauca | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Cliona celata | O2 + H2O2 | - |
? | |
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Schwanniomyces vanrijiae var. vanrijiae 020 | O2 + H2O2 | - |
? | |
| 1.15.1.1 | additional information | the extracellular enzyme appears to bind lipopolysaccharides, recognition mechanisms can be provided by several actors which can interplay such as plasma LBP-binding protein (LBP), membrane bound or soluble forms of CD14 and integrins | Crassostrea gigas | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | ? | x * 37600 | Lampanyctus crocodilus |
| 1.15.1.1 | ? | x * 15800-16600 , two isozymes, sequence calculation, x * 18000, SDS-PAGE | Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | ? | x * 15920, sequence calculation, x * 18000, SDS-PAGE | Debaryomyces hansenii |
| 1.15.1.1 | ? | x * 30000, about, sequence calculation, x * 25000, recombinant enzyme, SDS-PAGE | Sonneratia alba |
| 1.15.1.1 | homodimer | 2 * 23000, SDS-PAGE | Ulva linza |
| 1.15.1.1 | homodimer | 2 * 40000 | Porphyridium purpureum |
| 1.15.1.1 | monomer | 1 * 50230, sequence calculation, 1 * 59000, SDS-PAGE | Geobacillus sp. EPT3 |
| 1.15.1.1 | More | amino acid sequence comparisons, the swortfish SOD has a higher content of arginine and tyrosine than the corresponding bovine enzyme and appears to dissociate more readily into subunits. The swortfish enzyme has a higher content of arginine and tyrosine, high homology with the other eukaryotic enzymes,and low homology with the Photobacterium leiognuthi enzyme | Xiphias gladius |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | ApMn-SOD1 | - |
Alvinella pompejana |
| 1.15.1.1 | ApMn-SOD2 | - |
Alvinella pompejana |
| 1.15.1.1 | Cg-EcSOD | - |
Crassostrea gigas |
| 1.15.1.1 | chloroplastic Fe-SOD | - |
Ulva linza |
| 1.15.1.1 | cMn-SOD | - |
Penaeus vannamei |
| 1.15.1.1 | Cu-Zn-SOD | - |
Debaryomyces hansenii |
| 1.15.1.1 | Cu/Zn-SOD | - |
Mytilus edulis |
| 1.15.1.1 | Cu/Zn-SOD | - |
Crassostrea gigas |
| 1.15.1.1 | Cu/Zn-SOD | - |
Pinctada fucata |
| 1.15.1.1 | Cu/Zn-SOD | - |
Haliotis discus discus |
| 1.15.1.1 | Cu/Zn-SOD | - |
Sparus aurata |
| 1.15.1.1 | Cu/Zn-SOD | - |
Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | Cu/Zn-SOD | - |
Lampanyctus crocodilus |
| 1.15.1.1 | Cu/Zn-SOD | - |
Xiphias gladius |
| 1.15.1.1 | cytoplasmic manganese SOD | - |
Penaeus vannamei |
| 1.15.1.1 | cytosolic Cu/Zn-SOD | - |
Bruguiera gymnorhiza |
| 1.15.1.1 | dhsod-1 | - |
Debaryomyces hansenii |
| 1.15.1.1 | ElFe-SOD | - |
Ulva linza |
| 1.15.1.1 | ElSOD | - |
Ulva linza |
| 1.15.1.1 | extracellular SOD | - |
Crassostrea gigas |
| 1.15.1.1 | Fe-SOD | - |
Photobacterium leiognathi |
| 1.15.1.1 | Fe-SOD | - |
Lingulodinium polyedra |
| 1.15.1.1 | Fe-SOD | - |
Sonneratia alba |
| 1.15.1.1 | Fe-SOD | - |
Nodularia sp. (in: Bacteria) |
| 1.15.1.1 | Fe-SOD | - |
Ulva linza |
| 1.15.1.1 | LSOD | - |
Lampanyctus crocodilus |
| 1.15.1.1 | Mn-SOD | - |
Haliotis discus discus |
| 1.15.1.1 | Mn-SOD | - |
Geobacillus sp. EPT3 |
| 1.15.1.1 | Mn-SOD | - |
Sparus aurata |
| 1.15.1.1 | pfSOD | - |
Pinctada fucata |
| 1.15.1.1 | SaFe-SOD | - |
Sonneratia alba |
| 1.15.1.1 | SOD | - |
Photobacterium leiognathi |
| 1.15.1.1 | SOD | - |
Porphyridium purpureum |
| 1.15.1.1 | SOD | - |
Mytilus edulis |
| 1.15.1.1 | SOD | - |
Crassostrea gigas |
| 1.15.1.1 | SOD | - |
Gadus morhua |
| 1.15.1.1 | SOD | - |
Penaeus vannamei |
| 1.15.1.1 | SOD | - |
Debaryomyces hansenii |
| 1.15.1.1 | SOD | - |
Lingulodinium polyedra |
| 1.15.1.1 | SOD | - |
Tetraselmis subcordiformis |
| 1.15.1.1 | SOD | - |
Conticribra weissflogii |
| 1.15.1.1 | SOD | - |
Avicennia marina |
| 1.15.1.1 | SOD | - |
Apostichopus japonicus |
| 1.15.1.1 | SOD | - |
Pinctada fucata |
| 1.15.1.1 | SOD | - |
Sonneratia alba |
| 1.15.1.1 | SOD | - |
Tetraselmis gracilis |
| 1.15.1.1 | SOD | - |
Alvinella pompejana |
| 1.15.1.1 | SOD | - |
Haliotis discus discus |
| 1.15.1.1 | SOD | - |
Geobacillus sp. EPT3 |
| 1.15.1.1 | SOD | - |
Sparus aurata |
| 1.15.1.1 | SOD | - |
Nodularia sp. (in: Bacteria) |
| 1.15.1.1 | SOD | - |
Minutocellus polymorphus |
| 1.15.1.1 | SOD | - |
Cylindrotheca closterium |
| 1.15.1.1 | SOD | - |
Ulva linza |
| 1.15.1.1 | SOD | - |
Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | SOD | - |
Lampanyctus crocodilus |
| 1.15.1.1 | SOD | - |
Xiphias gladius |
| 1.15.1.1 | SOD | - |
Prionace glauca |
| 1.15.1.1 | SOD | - |
Cliona celata |
| 1.15.1.1 | SOD1 | - |
Avicennia marina |
| 1.15.1.1 | SOD1 | - |
Haliotis discus discus |
| 1.15.1.1 | SOD2 | - |
Haliotis discus discus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 25 | - |
assay at | Sonneratia alba |
| 1.15.1.1 | 35 | - |
- |
Ulva linza |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | - |
35 | maximal enzyme activity at 35°C, and 29.8% relative activity at 0°C | Ulva linza |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | additional information | - |
a higher thermostable enzyme | Lampanyctus crocodilus |
| 1.15.1.1 | additional information | - |
a highly thermostable enzyme | Photobacterium leiognathi |
| 1.15.1.1 | additional information | - |
a highly thermostable enzyme | Photobacterium sepia |
| 1.15.1.1 | additional information | - |
a highly thermostable enzyme, occurrence of an additional sulfur-containing hydrogen bond involving the M110 residue and the effect of the A138 residue on the backbone entropy | Alvinella pompejana |
| 1.15.1.1 | additional information | - |
a thermostable enzyme | Sonneratia alba |
| 1.15.1.1 | additional information | - |
high thermostability | Gadus morhua |
| 1.15.1.1 | 40 | - |
stable below | Ulva linza |
| 1.15.1.1 | 50 | - |
highly thermostable at | Geobacillus sp. EPT3 |
| 1.15.1.1 | 65 | - |
purified enzyme, half-life is 110 min | Alvinella pompejana |
| 1.15.1.1 | 80 | - |
purified enzyme, half-life is 9.8-20.8 min | Alvinella pompejana |
| 1.15.1.1 | 100 | - |
purified enzyme, strong stability at pH 6.0-7.0, the enzyme survives boiling for 10 min without losing more than 60% of activity | Debaryomyces hansenii |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 3.5 | 9.5 | stable at, 25°C | Sonneratia alba |
| 1.15.1.1 | 4 | 12 | stable at | Conticribra weissflogii |
| 1.15.1.1 | 5 | 11 | quite stable at | Geobacillus sp. EPT3 |
| 1.15.1.1 | 5 | 10 | stable at | Ulva linza |
| 1.15.1.1 | 6 | 7 | purified enzyme, strong stability at pH 6.0-7.0, the enzyme survives boiling for 10 min without losing more than 60% of activity | Debaryomyces hansenii |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.15.1.1 | Prionace glauca | the enzyme has a low isoelectric point | - |
additional information |
| 1.15.1.1 | Debaryomyces hansenii | two pI ranges: 5.14-4.0 and 1.6-1.8, isoelectric focusing | 1.8 | 1.6 |
| 1.15.1.1 | Debaryomyces hansenii | two pI ranges: 5.14-4.0 and 1.6-1.8, isoelectric focusing | 5.14 | 4 |
| 1.15.1.1 | Photobacterium sepia | - |
- |
4.1 |
| 1.15.1.1 | Porphyridium purpureum | isoelectric focusing | - |
4.2 |
| 1.15.1.1 | Photobacterium leiognathi | - |
- |
4.4 |
| 1.15.1.1 | Mytilus edulis | isozyme 3, isoelectric focusing | - |
4.55 |
| 1.15.1.1 | Mytilus edulis | isozyme 1, isoelectric focusing | - |
4.6 |
| 1.15.1.1 | Geobacillus sp. EPT3 | - |
- |
4.65 |
| 1.15.1.1 | Mytilus edulis | isozyme 2, isoelectric focusing | - |
4.7 |
| 1.15.1.1 | Lampanyctus crocodilus | - |
- |
6.35 |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.15.1.1 | Avicennia marina | a decrease in mRNA levels is observed for Sod1 with osmotic stress treatment | down |
| 1.15.1.1 | Tetraselmis subcordiformis | the enzyme is downregulated by UV-B radiation | down |
| 1.15.1.1 | Schwanniomyces vanrijiae var. vanrijiae | treatment with CuSO4 inhibits expression of SOD protein, addition of Mn2+ to the medium reduces the enzyme expressions | down |
| 1.15.1.1 | Pinctada fucata | after challenge with lipopolysaccharide (LPS), expression of pfSOD mRNA in hemocytes is increased, reaching the highest level at 8 h, then dropping to basal levels at 36 h | up |
| 1.15.1.1 | Schwanniomyces vanrijiae var. vanrijiae | enzyme expression is increased when cells are cultured with Cu2+, Cr2+, Fe3+ and Ni2+ | up |
| 1.15.1.1 | Penaeus vannamei | infection of the organism by white spot syndrome virus increases the expression of cMn-SOD. Transcript levels increase transiently 1 h post-infection and then decrease as the viral infection progresses to levels significantly lower than uninfected controls by 12 h post-infection | up |
| 1.15.1.1 | Bruguiera gymnorhiza | NaCl treatment increases the transcript level of cytosolic Cu/Zn-SOD in young and mature leaves rather than in old leaves. Expression of the cytosolic Cu/Zn-SOD gene is induced by exogenous abscisic acid | up |
| 1.15.1.1 | Avicennia marina | Sod1 mRNA levels are induced by iron, light stress and by direct H2O2stress treatment, thus confirming their role in oxidative stress response | up |
| 1.15.1.1 | Lingulodinium polyedra | the enzyme Fe-SOD is induced after exposure to toxic metal ions | up |
| 1.15.1.1 | Tetraselmis gracilis | the enzyme is induced by Cd2+ | up |
| 1.15.1.1 | Haliotis discus discus | the mRNA levels of Cu/Zn-SOD is increased in general during the metal (copper, zinc and cadmium) or thermal treatments | up |
| 1.15.1.1 | Haliotis discus discus | the mRNA levels of Mn-SOD is increased in general during the metal (copper, zinc and cadmium) or thermal treatments | up |
| 1.15.1.1 | Apostichopus japonicus | up-regulation of SOD mRNA with low salinity stress, increase levels of Sod mRNA by thermal and osmotic stresses | up |
| 1.15.1.1 | Nodularia sp. (in: Bacteria) | UV-irradiation induces the enzyme | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | evolution | phylogenetic analysis clusters cMn-SODs and mitochondrial Mn-SODs in two separate groups | Penaeus vannamei |
| 1.15.1.1 | evolution | the two different allelic forms of a Mn-SOD involved in ROS detoxification, ApMn-SOD1 and ApMn-SOD2, differ only by two substitutions, M110L and A138G, identified in an Alvinella pompejana cDNA library | Alvinella pompejana |
| 1.15.1.1 | evolution | the two different allelic forms of a Mn-SOD involved in ROS detoxification, ApMn-SOD1 and ApMn-SOD2, differ only by two substitutions, M110L and A138G, identified in an Alvinella pompejana cDNA library. ApMn-SOD2 is rare (2%) and only found in the heterozygous state | Alvinella pompejana |
| 1.15.1.1 | additional information | blue mussels from chemically contaminated area in Le Havre harbor exhibited a third Cu/Zn-SOD isoform characterized by a more acidic isoelectric point (pI 4.55) and a native apparent molecular mass of 130 kDa. When maintained in clean marine water, mussels from this area showed a transitory decrease in total SOD activity accompanied by the disappearance of the SOD-3 band | Mytilus edulis |
| 1.15.1.1 | additional information | ElSOD as a cold-adapted enzyme | Ulva linza |
| 1.15.1.1 | additional information | histidine and tryptophan residues are involved in the catalytic activity | Photobacterium leiognathi |
| 1.15.1.1 | additional information | histidine and tryptophan residues are involved in the catalytic activity | Geobacillus sp. EPT3 |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Photobacterium leiognathi |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Porphyridium purpureum |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Mytilus edulis |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Crassostrea gigas |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Gadus morhua |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Penaeus vannamei |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Debaryomyces hansenii |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Lingulodinium polyedra |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Tetraselmis subcordiformis |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Conticribra weissflogii |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Avicennia marina |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Bruguiera gymnorhiza |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Apostichopus japonicus |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Pinctada fucata |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Sonneratia alba |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Haliotis discus discus |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Geobacillus sp. EPT3 |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Sparus aurata |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Photobacterium sepia |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Cylindrotheca closterium |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Schwanniomyces vanrijiae var. vanrijiae |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Lampanyctus crocodilus |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Xiphias gladius |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Prionace glauca |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes | Cliona celata |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. An increase in the Fe-SOD content, particularly evident in scum samples that are continuously exposed to high irradiances, may have a role in the photo adaptation of diazotrophic cyanobacteria and help to protect them from light injury in the Baltic Sea | Nodularia sp. (in: Bacteria) |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. ElSOD is a cold-adapted SOD, which shows its potential valuein antioxidant utilization | Ulva linza |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The enzyme of Tetraselmis gracilis is important to prevent oxidative stress such as nutrient and light availability | Tetraselmis gracilis |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The enzyme plays an important role in preventing oxidative stress triggered by a number of factors that affect growth, such as nutrient and light availability | Minutocellus polymorphus |
| 1.15.1.1 | physiological function | the ability of marine organism to cope with oxidative stress is one of the main factors that influence its survival in the marine environment, when senescence conditions prevail. The antioxidative defense system includes enzymatic and non-enzymatic components. Among the enzymatic system, superoxide dismutases are the first and most important of the antioxidant metalloenzymes. The organism is exposed to various challenging conditions (e.g. high temperature, hypoxia and the presence of sulphides, heavy metals and radiations), which increase the production of dangerous reactive oxygen species (ROS). Two different allelic forms of a Mn-SOD involved in reactive oxygen species detoxification, ApMn-SOD1 and ApMn-SOD2 | Alvinella pompejana |
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