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Literature summary for 1.15.1.1 extracted from

  • Wu, J.R.; Lin, Y.; Zheng, Z.Y.; Lin, C.C.; Zhan, X.B.; Shen, Y.Q.
    Improvement of the CuZn-superoxide dismutase enzyme activity and stability as a therapeutic agent by modification with polysialic acids (2010), Biotechnol. Lett., 32, 1939-1945.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information polysialylation of SOD, method development and optimization, overview. Optimal conditions for the cross-linking reaction are the ratio of polysialic acid and SOD of 40:1 with a reaction time of 24 h. Under this condition, the average cross-linking ratio is 3.9 and average molecular weight was 95 kDa derived from the molecular weight of polysialic acid with 16.2 kDa and CuZn-SOD with 32 kDa. The molecular size of the polysialylated enzyme was about 90-100 kDa, enhancement of hydratability of SOD through polysialylation, analysis by atomic force microscopy, overview Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
additional information the native enzyme is degraded by pepsin and trypsin, while the polysialylated SOD is resistant to pepsin and trypsin Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a CuZn-superoxide dismutase Sus scrofa
Zn2+ a CuZn-superoxide dismutase Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, native enzyme, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SOD enzyme activity measurement is based on the inhibition of nitroblue tetrazolium reduction by superoxide radical generated by xanthine/xanthine oxidase Sus scrofa ?
-
?

Subunits

Subunits Comment Organism
? x * 32000, native enzyme, SDS-PAGE Sus scrofa

Synonyms

Synonyms Comment Organism
CuZn-superoxide dismutase
-
Sus scrofa
SOD
-
Sus scrofa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 80 the initial activities of the polysialyated enzyme show 35-55% higher than those of the native enzyme after incubation at 70°C, and 31-45% at 80°C, the native enzyme is almost inactivated after incubation for 3 h, while the polysialylated SOD still has 49-61% residual activities Sus scrofa

pH Stability

pH Stability pH Stability Maximum Comment Organism
2 9 the pH stability of the enzyme is enhanced by the polysialylation, after 1 h at pH 2-3, the residual enzyme activity of polysialylated SOD is 64-74%, while the native SOD shows quickly decreased activity to 20-38% Sus scrofa