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Literature summary for 1.15.1.1 extracted from

  • Xu, H.H.; Ma, H.; Hu, B.Q.; Lowrie, D.B.; Fan, X.Y.; Wen, C.G.
    Molecular cloning, identification and functional characterization of a novel intracellular Cu-Zn superoxide dismutase from the freshwater mussel Cristaria plicata (2010), Fish Shellfish Immunol., 29, 615-622.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene CuZnSOD, DNA and amino acid sequence determination and analysis, recombinant His6-tagged Cp-icCuZnSOD with high enzyme activity is induced to be expressed in Escherichia coli strain BL21(DE3) as a soluble form by IPTG supplemented with Cu/Zn ions at 20°C for 8 h Cristaria plicata

Inhibitors

Inhibitors Comment Organism Structure
SDS recombinant Cp-icCuZnSOD is active and retains more than 80% activity under treatment with 1-6% SDS. It retains 70% activity after treatment with 8% SDS but activity is rapidly lowered to 52% after treatment with 10% SDS Cristaria plicata

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm Cp-icCuZnSOD contains no signal peptide Cristaria plicata 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His46, His48, His63, and His120 for Cu2+ binding Cristaria plicata
Zn2+ an intracellular Cu-Zn superoxide dismutase. The enzyme amino acid sequence contains several highly conserved motifs including Cu/Zn ions binding sites, i.e. His63, His71, His80, and Asp83 for Zn2+ binding Cristaria plicata

Organism

Organism UniProt Comment Textmining
Cristaria plicata
-
gene CuZnSOD
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble Cp-icCuZnSOD by nickel affinity chromatography Cristaria plicata

Synonyms

Synonyms Comment Organism
CpSOD
-
Cristaria plicata
CuZnSOD
-
Cristaria plicata
intracellular Cu-Zn superoxide dismutase
-
Cristaria plicata
More the enzyme belongs to the superoxide dismutase family of important antioxidant metalloenzymes that catalyze superoxide radicals from cellular oxidative metabolism into hydrogen peroxideand molecular oxygen Cristaria plicata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 90 the recombinant enzyme retains more than 80% activity between 10°C and 60°C, but loses activity rapidly, which is reduced to 54% and 40% at 70°C and 80°C, respectively, and it is almost inactive at 90°C Cristaria plicata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
Cristaria plicata

pH Range

pH Minimum pH Maximum Comment Organism
2 9 activity range, the enzyme shows 30% of maximal activity at pH 10.0 and is inactive at pH 11.0 Cristaria plicata

General Information

General Information Comment Organism
additional information CpSOD contains an intracellular disulfide bond and two CuZnSOD family signatures Cristaria plicata
physiological function protection by recombinant Cp-icCuZnSOD against alcohol-injury in human hepatocyte L02 cell line Cristaria plicata