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Literature summary for 1.15.1.1 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

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
additional information quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview Bos taurus
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus SOD inhibits the autoxidation of pyrogallol ?
-
?
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-
additional information quantitative determination of an isotopically enriched metalloenzyme containing two different metal isotopes, method development, overview Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SOD inhibits the autoxidation of pyrogallol Bos taurus ?
-
?
O2.- + H+
-
Bos taurus O2 + H2O2
-
?
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

Subunits Comment Organism
homodimer
-
Bos taurus

Synonyms

Synonyms Comment Organism
Cu/Zn-SOD
-
Bos taurus
SOD
-
Bos taurus

Temperature Stability [°C]

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

pH Optimum

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