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Literature summary extracted from

  • Zhan, Z.J.; Zhou, Z.G.; Shan, W.G.
    Preparation and characterization of Cu,Zn-superoxide dismutase covalently modified by polyunsaturated fatty acids (2009), Biochemistry (Moscow), 74, 1266-1269.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.1 additional information chemical modification of the enzyme with linoleic and alpha-linolenic acids using two different methods leads to higher retained enzymatic activity compared with SOD modified by macromolecular substances. Enhanced heat stability, acid and alkali resistance, and anti-pepsin/trypsin ability of the modified SOD are observed and compared to those of the natural enzyme, the apparent oil-water partition coefficient of the modified enzyme is especially increased, overview Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Bos taurus
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-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.15.1.1 erythrocyte
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.15.1.1 additional information
-
 activity of native enzyme and modified, fatty acid-conjugated enzyme, overview, coupled assay method using inhibition of the autooxidation of pyrogallol Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 additional information coupled assay method using inhibition of the autooxidation of pyrogallol Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 Cu,Zn-SOD
-
 Bos taurus
1.15.1.1 Cu,Zn-superoxide dismutase
-
 Bos taurus
1.15.1.1 SOD
-
 Bos taurus