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Literature summary for 7.1.1.9 extracted from

  • Tsukita, S.; Koyanagi, S.; Nagata, K.; Koizuka, H.; Akashi, H.; Shimoyama, T.; Tamura, T.; Sone, N.
    Characterization of a cb-type cytochrome c oxidase from Helicobacter pylori (1999), J. Biochem., 125, 194-201.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CN-
-
Helicobacter pylori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00004
-
O2
-
Helicobacter pylori
0.0009
-
ferrocytochrome c553
-
Helicobacter pylori

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Helicobacter pylori 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE Helicobacter pylori
58000
-
1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE Helicobacter pylori
200000
-
gel filtration Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Triton X-100, Q-Sepharose, chelating Sepharose, gel filtration Helicobacter pylori

Storage Stability

Storage Stability Organism
-80°C, no severe loss of activity Helicobacter pylori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 Saccharomyces cerevisiae cytochrome c Helicobacter pylori ferricytochrome c + H2O
-
?
ferrocytochrome c + O2 horse ferrocytochrome c Helicobacter pylori ferricytochrome c + H2O
-
?
ferrocytochrome c + O2 artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine Helicobacter pylori ferricytochrome c + H2O
-
?
ferrocytochrome c553 + O2 + H+
-
Helicobacter pylori ferricytochrome c553 + H2O
-
r

Subunits

Subunits Comment Organism
dimer 1 * 58000 + 1 * 26000, 58000 Da band may be composed of 2 subunits of the cb-type oxidase, the 26000 Da subunit may be a heme c bearing diheme or mono-heme of the enzyme, SDS-PAGE Helicobacter pylori

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
252
-
ferrocytochrome c553
-
Helicobacter pylori

Cofactor

Cofactor Comment Organism Structure
heme c enzyme contains 3 heme c Helicobacter pylori
protoheme
-
Helicobacter pylori

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0026
-
CN-
-
Helicobacter pylori