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Literature summary for 1.15.1.1 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

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Streptococcus mutans

Substrates and Products (Substrate)

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

Subunits

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