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Literature summary for 1.11.1.6 extracted from

  • Meir, E.; Yagil, E.
    Further characterization of the two catalses Escherichia coli (1985), Curr. Microbiol., 12, 315-320.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
3-amino-1H-1,2,4-triazole isoenzyme HPI: 25% inhibition at 10 mM, isoenzyme HPII: 70-80% inhibition at 10 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7
-
H2O2 isoenzyme HPI Escherichia coli
10
-
H2O2 isoenzyme HPII, pH 10.5 Escherichia coli
18.2
-
H2O2 isoenzyme HPII, pH 6.8 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2O2 Escherichia coli one monofunctional, two bifunctional catalases O2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Escherichia coli
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 one monofunctional, two bifunctional catalases Escherichia coli O2 + H2O
-
?

Synonyms

Synonyms Comment Organism
HPI-A catalase-peroxidase isoenzyme Escherichia coli
HPI-B catalase-peroxidase isoenzyme Escherichia coli
HPII monofunctional catalase Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
1.5fold activation for isoenzyme HPII, inactivation for isoenzymes HPI-A, HPI-B Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
isoenzyme HPII, first pH-optimum Escherichia coli
10.5
-
isoenzyme HPII, second pH-optimum Escherichia coli