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Literature summary extracted from
- Characterization of superoxide dismutase from the fall webworm, Hyphantria cunea: comparison of its properties to superoxide dismutase from the silkworm Bombyx mori (2007), Appl. Entomol. Zool., 42, 465-472.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | gene sod, DNA and amino acid sequence determination and analysis | Bombyx mori |
| 1.15.1.1 | gene sod, DNA and amino acid sequence determination and analysis, functional overexpression of the soluble enzyme in Escherichia coli | Hyphantria cunea |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.15.1.1 | Cu2+ | a Cu,Zn-SOD | Bombyx mori |  |
| 1.15.1.1 | Cu2+ | a Cu,Zn-SOD | Hyphantria cunea | |
| 1.15.1.1 | additional information | the enzyme contains 6 metal binding sites | Hyphantria cunea | |
| 1.15.1.1 | additional information | the enzyme contains 7 metal binding sites | Bombyx mori | |
| 1.15.1.1 | Zn2+ | a Cu,Zn-SOD | Bombyx mori | |
| 1.15.1.1 | Zn2+ | a Cu,Zn-SOD | Hyphantria cunea | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 15832 | - |
x * 15832, sequence calculation | Hyphantria cunea |
| 1.15.1.1 | 15841 | - |
x * 15841, sequence calculation | Bombyx mori |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.15.1.1 | O2.- + H+ | Bombyx mori | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | O2 + H2O2 | - |
? | |
| 1.15.1.1 | O2.- + H+ | Hyphantria cunea | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | O2 + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.15.1.1 | Bombyx mori | - |
silkworm | - |
| 1.15.1.1 | Hyphantria cunea | A7BI63 | fall webworm, gene sod | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | soluble recombinant enzyme from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography to homogeneity | Hyphantria cunea |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.15.1.1 | fat body | larval tissue | Hyphantria cunea | - |
| 1.15.1.1 | hemocyte | larval tissue | Hyphantria cunea | - |
| 1.15.1.1 | larva | fourth-instar larva | Hyphantria cunea | - |
| 1.15.1.1 | midgut | larval tissue | Hyphantria cunea | - |
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 | 5780 | - |
purified recombinant enzyme | Hyphantria cunea |
| 1.15.1.1 | 7980 | - |
purified recombinant enzyme | Bombyx mori |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.15.1.1 | O2.- + 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate | i.e. WST-1, activity assay detection method | Hyphantria cunea | ? | - |
? | |
| 1.15.1.1 | O2.- + H+ | - |
Bombyx mori | O2 + H2O2 | - |
? | |
| 1.15.1.1 | O2.- + H+ | - |
Hyphantria cunea | O2 + H2O2 | - |
? | |
| 1.15.1.1 | O2.- + H+ | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | Bombyx mori | O2 + H2O2 | - |
? | |
| 1.15.1.1 | O2.- + H+ | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | Hyphantria cunea | O2 + H2O2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | ? | x * 15832, sequence calculation | Hyphantria cunea |
| 1.15.1.1 | ? | x * 15841, sequence calculation | Bombyx mori |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | Cu,Zn-SOD | - |
Bombyx mori |
| 1.15.1.1 | Cu,Zn-SOD | - |
Hyphantria cunea |
| 1.15.1.1 | SOD | - |
Bombyx mori |
| 1.15.1.1 | SOD | - |
Hyphantria cunea |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 40 | - |
and below, 30 min, purified recombinant enzyme, completely stable | Hyphantria cunea |
| 1.15.1.1 | 40 | - |
and below, completely stable | Bombyx mori |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 5 | 11 | stable | Bombyx mori |
| 1.15.1.1 | 5 | 11 | purified recombinant enzyme, stable | Hyphantria cunea |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.15.1.1 | Hyphantria cunea | sequence calculation | - |
5.65 |
| 1.15.1.1 | Bombyx mori | sequence calculation | - |
5.78 |
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