Cloned (Comment) | Organism |
---|---|
gene sod, DNA and amino acid sequence determination and analysis | Bombyx mori |
gene sod, DNA and amino acid sequence determination and analysis, functional overexpression of the soluble enzyme in Escherichia coli | Hyphantria cunea |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | a Cu,Zn-SOD | Bombyx mori | |
Cu2+ | a Cu,Zn-SOD | Hyphantria cunea | |
additional information | the enzyme contains 6 metal binding sites | Hyphantria cunea | |
additional information | the enzyme contains 7 metal binding sites | Bombyx mori | |
Zn2+ | a Cu,Zn-SOD | Bombyx mori | |
Zn2+ | a Cu,Zn-SOD | Hyphantria cunea |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
15832 | - |
x * 15832, sequence calculation | Hyphantria cunea |
15841 | - |
x * 15841, sequence calculation | Bombyx mori |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
O2.- + H+ | Bombyx mori | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | O2 + H2O2 | - |
? | |
O2.- + H+ | Hyphantria cunea | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | O2 + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bombyx mori | - |
silkworm | - |
Hyphantria cunea | A7BI63 | fall webworm, gene sod | - |
Purification (Comment) | Organism |
---|---|
soluble recombinant enzyme from Escherichia coli by ammonium sulfate fractionation and anion exchange chromatography to homogeneity | Hyphantria cunea |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fat body | larval tissue | Hyphantria cunea | - |
hemocyte | larval tissue | Hyphantria cunea | - |
larva | fourth-instar larva | Hyphantria cunea | - |
midgut | larval tissue | Hyphantria cunea | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
5780 | - |
purified recombinant enzyme | Hyphantria cunea |
7980 | - |
purified recombinant enzyme | Bombyx mori |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
? | |
O2.- + H+ | - |
Bombyx mori | O2 + H2O2 | - |
? | |
O2.- + H+ | - |
Hyphantria cunea | O2 + H2O2 | - |
? | |
O2.- + H+ | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | Bombyx mori | O2 + H2O2 | - |
? | |
O2.- + H+ | SOD is a regulatory enzyme involved in the degradation of superoxide anions in living organisms | Hyphantria cunea | O2 + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 15832, sequence calculation | Hyphantria cunea |
? | x * 15841, sequence calculation | Bombyx mori |
Synonyms | Comment | Organism |
---|---|---|
Cu,Zn-SOD | - |
Bombyx mori |
Cu,Zn-SOD | - |
Hyphantria cunea |
SOD | - |
Bombyx mori |
SOD | - |
Hyphantria cunea |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
and below, 30 min, purified recombinant enzyme, completely stable | Hyphantria cunea |
40 | - |
and below, completely stable | Bombyx mori |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5 | 11 | stable | Bombyx mori |
5 | 11 | purified recombinant enzyme, stable | Hyphantria cunea |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Hyphantria cunea | sequence calculation | - |
5.65 |
Bombyx mori | sequence calculation | - |
5.78 |