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Literature summary for 1.15.1.1 extracted from
- Iron-dependent superoxide dismutase from novel thermoacidophilic crenarchaeon Acidilobus saccharovorans: from gene to active enzyme (2012), Biochemistry (Moscow), 77, 1368-1376.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Acidilobus saccharovorans |
| gene locus Asac_0498, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta-gami(DE3) | Acidilobus saccharovorans |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | a Fe-SOD, the enzyme is able to bind various bivalent metals in the active site | Acidilobus saccharovorans |  |
| Fe2+ | presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein | Acidilobus saccharovorans | |
| Mn2+ | presence of 0.25 Fe atom and 0.01 Mn atom per monomer of protein | Acidilobus saccharovorans | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 23954 | - |
4 * 23954, sequence calculation | Acidilobus saccharovorans |
| 98500 | - |
recombinant enzyme, sedimentation velocity analysis | Acidilobus saccharovorans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 O2.- + 2 H+ | Acidilobus saccharovorans | - |
O2 + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidilobus saccharovorans | D9Q0R7 | - |
- |
| Acidilobus saccharovorans | D9Q0R7 | isolated from a terrestrial acidic hot spring, Kamchatka peninsula, Russia, gene ASAC_0498 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Acidilobus saccharovorans |
| recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain Rosetta-gami(DE3) | Acidilobus saccharovorans |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | optimal conditions for growth of this organism are 82-92°C, pH 3.0-4.0 | Acidilobus saccharovorans | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1700 | - |
purified recombinant enzyme, pH 7.5, 25°C | Acidilobus saccharovorans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 O2.- + 2 H+ | - |
Acidilobus saccharovorans | O2 + H2O2 | - |
? | |
| additional information | SOD activity is determined by a modified method of inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system generating superoxide ions | Acidilobus saccharovorans | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional structure modelling, overview | Acidilobus saccharovorans |
| tetramer | 4 * 23954, sequence calculation | Acidilobus saccharovorans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ASAC_0498 | locus name | Acidilobus saccharovorans |
| Fe-SOD | - |
Acidilobus saccharovorans |
| Fe-SOD_ASAC | - |
Acidilobus saccharovorans |
| iron-dependent superoxide dismutase | - |
Acidilobus saccharovorans |
| SOD | - |
Acidilobus saccharovorans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Acidilobus saccharovorans |
| 70 | - |
- |
Acidilobus saccharovorans |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 90 | activity range, profile overview | Acidilobus saccharovorans |
| 40 | 90 | 40°C: about 50% of maximal activity, 90°C: 75% of maximal activity | Acidilobus saccharovorans |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal stability and activity of the enzyme directly depends on the nature of the reconstituted metal and the degree of saturation of binding sites | Acidilobus saccharovorans |
| 20 | 90 | secondary structure of SOD_ASAC is stable within this temperature range | Acidilobus saccharovorans |
| 40 | 90 | over 50% activity within this range, most stable at 70°C, profile overview | Acidilobus saccharovorans |
| 80 | - |
purified recombinant enzyme, 66 h, 50% activity remaining | Acidilobus saccharovorans |
| 107 | - |
the denaturation temperature of the enzyme is 107.3°C | Acidilobus saccharovorans |
| 107.3 | - |
denaturing temperature | Acidilobus saccharovorans |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Acidilobus saccharovorans |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | activity does not change in the pH-range 4-10 | Acidilobus saccharovorans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | three-dimensional structure modelling, overview. The active site is surrounded by aromatic amino acid residues Trp131, Trp84, Phe168, Tyr139, and Tyr83 and is localized near the potential contact of monomers in the dimer | Acidilobus saccharovorans |
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