Literature summary for 1.15.1.1 extracted from
Li, M.; Guo, S.; Li, X.; Wang, Q.; Zhu, L.; Yin, C.; Wang, W.
Engineering a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation (2017), Biotechnol. Bioprocess Eng., 22, 725-733 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
recombinant expression of His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp in Escherichia coli strain BL21(DE3) |
Aeropyrum pernix |
Protein Variants
Protein Variants |
Comment |
Organism |
additional information |
generation of a highly thermostable and stress tolerant superoxide dismutase by N-terminal modification and metal incorporation engineering. Recombinant wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp are incorporated with metal cofactors by two ways: the Fe2+- and Mn2+-contained SODs are obtained by in vivo modification (Mn-med SODAp and ntdSODAp) and in vitro reconstitution (Mn-rec SODAp and ntdSODAp), respectively |
Aeropyrum pernix |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
2-mercaptoethanol |
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, no inhibition at 1 mM |
Aeropyrum pernix |
|
EDTA |
60% inhibition of Mn-reconstituted wild-type enzyme at 10 mM, 20% at 1 mM |
Aeropyrum pernix |
|
guanidinium hydrochloride |
25% inhibition of Mn-reconstituted wild-type enzyme at 10 mM |
Aeropyrum pernix |
|
SDS |
60% inhibition of Mn-reconstituted wild-type enzyme at 1%, and 40% inhibition of the Mn-reconstituted N-terminal domain |
Aeropyrum pernix |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Fe2+ |
a Fe/MnSOD |
Aeropyrum pernix |
|
Mn2+ |
a Fe/MnSOD |
Aeropyrum pernix |
|
additional information |
the native forms of SODAp and NTD-fused N-terminal domain ntdSODAp prefer binding Fe2+ over Mn2+ (about 10fold) but contain low ion amounts in each monomer, respectively |
Aeropyrum pernix |
|
Natural Substrates/ Products (Substrates)
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
2 superoxide + 2 H+ |
Aeropyrum pernix |
- |
O2 + H2O2 |
- |
? |
|
Organic Solvent Stability
Organic Solvent |
Comment |
Organism |
additional information |
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits higher tolerance for denaturants and organic media than recombinant wild-type Mn-rec SODAp |
Aeropyrum pernix |
Organism
Organism |
UniProt |
Comment |
Textmining |
Aeropyrum pernix |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
recombinant His-tagged wild-type enzyme SODAp and NTD-fused N-terminal domain ntdSODAp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography |
Aeropyrum pernix |
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
2.585 |
- |
purified recombinant Mn-reconstituted wild-type SOD, pH 7.8, 25°C |
Aeropyrum pernix |
4.155 |
- |
purified recombinant Mn-reconstituted N-terminal domain mutant SOD, pH 7.8, 25°C |
Aeropyrum pernix |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
2 superoxide + 2 H+ |
- |
Aeropyrum pernix |
O2 + H2O2 |
- |
? |
|
additional information |
SOD enzyme activity is determined by measuring enzyme ability to inhibit the photochemical reduction of nitrobluetetrazolium |
Aeropyrum pernix |
? |
- |
? |
|
Synonyms
Synonyms |
Comment |
Organism |
SOD |
- |
Aeropyrum pernix |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
50 |
- |
wild-type enzyme SODAp |
Aeropyrum pernix |
70 |
- |
recombinant fusion enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C |
Aeropyrum pernix |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
70 |
110 |
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10 |
Aeropyrum pernix |
100 |
- |
recombinant wild-type enzyme SODAp retains 44&% of maximal activity, while recombinant Mn-rec ntdSODAp N-termina domain retains 58% activity |
Aeropyrum pernix |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
7.8 |
- |
assay at |
Aeropyrum pernix |
pH Stability
pH Stability |
pH Stability Maximum |
Comment |
Organism |
4 |
10 |
recombinant N-terminal domain of the enzyme SOD obtained by in vitro reconstitution (Mn-rec ntdSODAp) exhibits improved optimum temperature at 70°C and dramatically enhanced thermostability especially at 110°C with enhanced pH stability from pH 4 to pH 10 |
Aeropyrum pernix |
General Information
General Information |
Comment |
Organism |
physiological function |
superoxide dismutases protect against oxidative stress by disproportionation of the superoxide anion radical to hydrogen peroxide and dioxygen through a redox cycle of metal ions |
Aeropyrum pernix |