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Literature summary for 1.11.1.6 extracted from

  • Yamaguchi, H.; Sugiyama, K.; Hosoya, M.; Takahashi, S.; Nakayama, T.
    Gene cloning and biochemical characterization of a catalase from Gluconobacter oxydans (2011), J. Biosci. Bioeng., 111, 522-527.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
61
-
H2O2 pH and temperature not specified in the publication Gluconobacter oxydans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
4 * 80000, SDS-PAGE Gluconobacter oxydans
320000
-
-
Gluconobacter oxydans

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Gluconobacter oxydans O2 + H2O
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 80000, SDS-PAGE Gluconobacter oxydans

Synonyms

Synonyms Comment Organism
CAT
-
Gluconobacter oxydans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
the enzyme retains full activity after incubation for 30 min at 70°C Gluconobacter oxydans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
62800
-
H2O2 pH and temperature not specified in the publication Gluconobacter oxydans

pH Range

pH Minimum pH Maximum Comment Organism
4 9
-
Gluconobacter oxydans

pH Stability

pH Stability pH Stability Maximum Comment Organism
3
-
more than 60% of the original activity is retained after treatment at pH 3.0 and 40°C for 1 h Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
heme Cat is a heme b-containing protein Gluconobacter oxydans