Any feedback?
Literature summary extracted from
- Engineering a thermostable iron superoxide dismutase based on manganese superoxide dismutase from Thermus thermophilus (2016), Process Biochem., 51, 39-47 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3) | Thermus thermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | H171A | site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His171Ala is 59% suggesting that the mutant folds with a reasonable secondary structure. Mutant His171Ala exhibits a 39.6% higher activity than the wild-type. Mutant His171Ala is a Fe-SOD with Zn, Ni,and Fe contents of 180, 77, and 530 ng/mg, respectively. Mutant His171Ala exhibits a specific activity 39.6% higher than that of the wild type enzyme | Thermus thermophilus |
| 1.15.1.1 | H29A | site-directed mutagenesis, the mutation changes the metal-binding specificity of the mutant enzyme from Mn to Fe. The alpha-helix content of mutant His29Ala is 66% , suggesting that the mutant folds with a reasonable secondary structure. Mutant His29Ala shows an activity comparable to that of the wild-type. Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. The mutant exhibits a specific activity comparable to that of the wild-type enzyme | Thermus thermophilus |
| 1.15.1.1 | H84A | site-directed mutagenesis, the mutant exhibits a specific activity comparable to that of the wild-type enzyme | Thermus thermophilus |
| 1.15.1.1 | additional information | structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview | Thermus thermophilus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.15.1.1 | Fe2+ | recombinant mutant H29A and H171A specificity | Thermus thermophilus |  |
| 1.15.1.1 | Mn2+ | a Mn-SOD, wild-type specificity, and mutant H84A | Thermus thermophilus | |
| 1.15.1.1 | additional information | Zn, Ni, and Fe contents of the His29Ala enzyme mutant are 180, 76, and 300 ng/mg, respectively, and the amount of Fe is almost twice that of Zn and fourtimes that of Ni, suggesting that His29Ala mainly is a Fe-SOD. Metal binding trutcure involving residues His29 and His171, overview | Thermus thermophilus |
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+ | Thermus thermophilus | - |
O2 + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.15.1.1 | Thermus thermophilus | P61502 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.15.1.1 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography | Thermus thermophilus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.15.1.1 | 2 superoxide + 2 H+ | - |
Thermus thermophilus | O2 + H2O2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | ? | x * 26000, recombinant enzyme mutants H29A and H171A, SDS-PAGE | Thermus thermophilus |
| 1.15.1.1 | More | structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | manganese superoxide dismutase | - |
Thermus thermophilus |
| 1.15.1.1 | Mn-SOD | - |
Thermus thermophilus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 25 | - |
assay at | Thermus thermophilus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 30 | 50 | purified enzyme mutants H29A and H171A, 30 min, stable | Thermus thermophilus |
| 1.15.1.1 | 70 | - |
purified enzyme mutants H29A and H171A, 30 min, retain 51% and 36.7% activity, respectively, mutant H29A retains 20% activity after 1 h, half-lives of SOD activity for His171Ala and His29Ala mutants are 33 and 15 min | Thermus thermophilus |
| 1.15.1.1 | 80 | - |
mutant H171A retains 20% activity after 1 h | Thermus thermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 8.2 | - |
assay at | Thermus thermophilus |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.15.1.1 | 5 | 10 | purified enzyme mutants H29A and H171A, 4°C, 30 min, both retain over 80% activity | Thermus thermophilus |
| 1.15.1.1 | 11 | - |
purified enzyme mutants H29A and H171A, 4°C, 30 min, both retain over 60% activity | Thermus thermophilus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.15.1.1 | Thermus thermophilus | enzyme mutants H29A and H171A | - |
8 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.15.1.1 | additional information | structure models of three mutants His29Ala, His84Ala, and His171Ala, overview | Thermus thermophilus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
