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Literature summary for 1.15.1.1 extracted from

  • Pedersen, H.L.; Willassen, N.P.; Leiros, I.
    The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicida (2009), Acta Crystallogr. Sect. F, 65, 84-92.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene sodB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) Aliivibrio salmonicida

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme by hanging drop vapour diffusion method, 6.5 mg/ml protein in a solution containing 0.1 M Tris-HCl, 1.4 M sodium citrate pH 8.5, 18°C, few days, X-ray diffraction structure determination and analysis at 1.7 A resolution Aliivibrio salmonicida

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aliivibrio salmonicida B6ENP9 gene sodB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) Aliivibrio salmonicida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 O2.- + 2 H+
-
Aliivibrio salmonicida O2 + H2O2
-
?

Synonyms

Synonyms Comment Organism
FeSOD
-
Aliivibrio salmonicida
iron superoxide dismutase
-
Aliivibrio salmonicida

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared to the enzyme from Escherichia coli, structure-thermostability relationship, overview Aliivibrio salmonicida
57
-
purified recombinant enzyme, loss of over 50% activity Aliivibrio salmonicida