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Literature summary for 1.15.1.1 extracted from

  • Li, H.; Feng, Z.; Sun, Y.; Ning, S.; Zhou, W.; Liu, A.; Pan, F.; Zhao, X.; Zhu, H.; Lu, J.
    Engineering a thermostable iron superoxide dismutase based on manganese superoxide dismutase from Thermus thermophilus (2016), Process Biochem., 51, 39-47 .
No PubMed abstract available
Search for more literature for 1.15.1.1

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
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
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
H84A site-directed mutagenesis, the mutant exhibits a specific activity comparable to that of the wild-type enzyme Thermus thermophilus
additional information structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ recombinant mutant H29A and H171A specificity Thermus thermophilus
Mn2+ a Mn-SOD, wild-type specificity, and mutant H84A Thermus thermophilus
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 superoxide + 2 H+ Thermus thermophilus
-
 O2 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus P61502
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 superoxide + 2 H+
-
 Thermus thermophilus O2 + H2O2
-
 ?

Subunits

Subunits Comment Organism
? x * 26000, recombinant enzyme mutants H29A and H171A, SDS-PAGE Thermus thermophilus
More structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview Thermus thermophilus

Synonyms

Synonyms Comment Organism
manganese superoxide dismutase
-
 Thermus thermophilus
Mn-SOD
-
 Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 50 purified enzyme mutants H29A and H171A, 30 min, stable Thermus thermophilus
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
80
-
 mutant H171A retains 20% activity after 1 h Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
 assay at Thermus thermophilus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 10 purified enzyme mutants H29A and H171A, 4°C, 30 min, both retain over 80% activity Thermus thermophilus
11
-
 purified enzyme mutants H29A and H171A, 4°C, 30 min, both retain over 60% activity Thermus thermophilus

pI Value

Organism Comment pI Value Maximum pI Value
Thermus thermophilus enzyme mutants H29A and H171A
-
 8

General Information

General Information Comment Organism
additional information structure models of three mutants His29Ala, His84Ala, and His171Ala, overview Thermus thermophilus