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Literature summary for 1.15.1.1 extracted from

  • Borders, C.L., Jr.; Bjerrum, M.J.; Schirmer, M.A.; Oliver, S.G.
    Characterization of recombinant Saccharomyces cerevisiae manganese-containing superoxide dismutase and its H30A and K170R mutants expressed in Escherichia coli (1998), Biochemistry, 37, 11323-11331.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Mn-SOD, expression of wild-type and mutants in Escherichia coli Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
H30A active site mutant, site-directed mutagenesis, activity, sensitivity to heat and inhibitors unchanged compared to wild-type Saccharomyces cerevisiae
K170R active site mutant, site-directed mutagenesis, unchanged activity, decreased thermal stability, more stable to 2,4,6-trinotrobenzenesulfonate than the wild-type, completely inactivated by phenylglyoxal Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
2,4,6-Trinitrobenzenesulfonate 0.5 M, pH 9.0, 25°C, native wild-type enzyme: half-life 3.5 min, recombinant wild-type enzyme: half-life: 5.1 min, recombinant mutant H30A: half-life 5.5 min, recombinant mutant K170R half-life 101 min Saccharomyces cerevisiae
Phenylglyoxal 25% activity remaining after 3 h for native and recombinant wild-type and recombinant mutant H30A, complete inactivation of recombinant mutant K179R after 7 min Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
Mn-SOD
-
Saccharomyces cerevisiae Mn-SOD
-
Mn-SOD
-

Reaction

Reaction Comment Organism Reaction ID
2 superoxide + 2 H+ = O2 + H2O2 amino acid sequence alignment and comparison Saccharomyces cerevisiae
2 superoxide + 2 H+ = O2 + H2O2 A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
Mn-SOD, native and recombinant wild-type and mutants Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O2- + H+
-
Saccharomyces cerevisiae O2 + H2O2
-
?
O2- + H+
-
Saccharomyces cerevisiae Mn-SOD O2 + H2O2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
native wild-type enzyme: half-life 4.7 h, recombinant wild-type enzyme: half-life: 2.8 h, recombinant mutant H30A: half-life 2.7 h, recombinant mutant K170R half-life 0.36 h Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Saccharomyces cerevisiae