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Literature summary for 1.15.1.1 extracted from
- Biochemical and molecular characterization of a novel Cu/Zn superoxide dismutase from Amaranthus hypochondriacus L. an intrinsically disordered protein (2015), Appl. Biochem. Biotechnol., 176, 2328-2345 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| AhSOD DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) | Amaranthus hypochondriacus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| H2O2 | - |
Amaranthus hypochondriacus |  |
| KCN | - |
Amaranthus hypochondriacus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding | Amaranthus hypochondriacus | |
| additional information | enzyme affinities for copper, zinc, and nickel, overview | Amaranthus hypochondriacus | |
| Zn2+ | a Cu/ZnSOD, highly conserved amino acid residues are involved in Cu/Zn binding | Amaranthus hypochondriacus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28500 | - |
recombinant His-tagged enzyme, gel filtration | Amaranthus hypochondriacus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 superoxide + 2 H+ | Amaranthus hypochondriacus | - |
O2 + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Amaranthus hypochondriacus | F6JRN6 | cv. Nutrisol | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and dialysis, anion exchange chromatography and dialysis, and ultrafiltration | Amaranthus hypochondriacus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| root | - |
Amaranthus hypochondriacus | - |
| seedling | - |
Amaranthus hypochondriacus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 superoxide + 2 H+ | - |
Amaranthus hypochondriacus | O2 + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 15600, about, sequence calculation | Amaranthus hypochondriacus |
| More | enzyme structural analysis by circular dichroism analysis, recombinnat AhSOD is an intrinsically disorder enzyme, sequence comparisons and three-dimensional model | Amaranthus hypochondriacus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AhSOD | - |
Amaranthus hypochondriacus |
| Cu/Zn superoxide dismutase | - |
Amaranthus hypochondriacus |
| Cu/ZnSOD | - |
Amaranthus hypochondriacus |
| SOD | - |
Amaranthus hypochondriacus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Amaranthus hypochondriacus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Amaranthus hypochondriacus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Amaranthus hypochondriacus | sequence calculation | - |
5.4 |
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