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Literature summary extracted from

  • Deitrich, C.L.; Raab, A.; Pioselli, B.; Thomas-Oates, J.E.; Feldmann, J.
    Chemical preparation of an isotopically enriched superoxide dismutase and its characterization as a standard for species-specific isotope dilution analysis (2007), Anal. Chem., 79, 8381-8390.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.15.1.1 the enzyme is remarkably stable at high temperatures and even under denaturing conditions Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Cu2+ the concentration of enzyme bound Cu2+ is 1.63 mg/l, the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], replacement of natural cofactor Cu2+ by isotopically enriched 65Cu, method, overview Bos taurus
1.15.1.1 additional information quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview Bos taurus
1.15.1.1 Zn2+ the concentration of enzyme bound Zn2+ is 1.68 mg/l, the Zn ion plays a structural role, replacement of natural cofactor Zn2+ by isotopically enriched 68Zn, method, overview Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.1 additional information Bos taurus SOD inhibits the autoxidation of pyrogallol ?
-
?
1.15.1.1 O2.- + H+ Bos taurus the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role O2 + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.15.1.1 liver
-
Bos taurus
-
1.15.1.1 additional information quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview 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
-
activities of the native metalloenzyme and isotopically enriched metalloenzyme containing two different metal isotopes, measurement of SOD inhibition of the autoxidation of pyrogallol, method development, overview Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 additional information SOD inhibits the autoxidation of pyrogallol Bos taurus ?
-
?
1.15.1.1 O2.- + H+
-
Bos taurus O2 + H2O2
-
?
1.15.1.1 O2.- + H+ the enzyme catalyzes the disproportionation of superoxide via its Cu ion redox cycle [Cu-(II)/Cu(I)], protecting the organism from oxidative stress, while the neighboring Zn ion plays a structural role Bos taurus O2 + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 homodimer
-
Bos taurus

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 Cu/Zn-SOD
-
Bos taurus
1.15.1.1 SOD
-
Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.15.1.1 additional information
-
the enzyme is remarkably stable at high temperatures Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.15.1.1 8.2
-
assay at Bos taurus