Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.15.1.1	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

EC Number	Inhibitors	Comment	Organism	Structure
1.15.1.1	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

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

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.15.1.1	32000	-	x * 32000, native enzyme, SDS-PAGE	Sus scrofa

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.15.1.1	Sus scrofa	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.15.1.1	blood	-	Sus scrofa	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.15.1.1	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

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.15.1.1	CuZn-superoxide dismutase	-	Sus scrofa
1.15.1.1	SOD	-	Sus scrofa

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.15.1.1	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

EC Number	pH Stability	pH Stability Maximum	Comment	Organism
1.15.1.1	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

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Release 2023.1 (January 2023)