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Literature summary extracted from

  • Vance, P.G.; Keele, B.B.; Rajagopalan, K.V.
    Superoxide dismutase from Streptococcus mutans. Isolation and characterization of two forms of the enzyme (1972), J. Biol. Chem., 247, 4782-4786.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Cu2+ no copper Streptococcus mutans
1.15.1.1 Mn2+ isoform I, 1.85 atoms manganese per mol of enzyme Streptococcus mutans
1.15.1.1 Zn2+ no zinc Streptococcus mutans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.1 18500
-
2 * 18500, isozyme I, SDS-PAGE Streptococcus mutans
1.15.1.1 19500
-
2 * 19500, isozyme II, SDS-PAGE Streptococcus mutans
1.15.1.1 31200
-
-
Streptococcus mutans
1.15.1.1 40250
-
superoxide dismutase I, sedimentation equilibrium analysis Streptococcus mutans

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Streptococcus mutans
-
2 isoenzymes I and II
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.1 2 isoenzymes: superoxide dismutase I and II Streptococcus mutans

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
-
-
Streptococcus mutans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 O2- + H+
-
Streptococcus mutans O2 + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 dimer 2 * 19500, isozyme II, SDS-PAGE Streptococcus mutans
1.15.1.1 dimer 2 * 18500, isozyme I, SDS-PAGE Streptococcus mutans