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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