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Literature summary for 1.11.1.6 extracted from

  • Hilbers, F.; von der Hocht, I.; Ludwig, B.; Michel, H.
    True wild type and recombinant wild type cytochrome c oxidase from Paracoccus denitrificans show a 20-fold difference in their catalase activity (2013), Biochim. Biophys. Acta, 1827, 319-327.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylcholine
-
Paracoccus denitrificans

Cloned(Commentary)

Cloned (Comment) Organism
gene ctaDII, which codes for subunit I of CcO, expression in Escherichia coli strain DH5alpha, the recombinant enzyme shows reduced catalase activity and thermal stability, overview. Expression of subunit I in the wild-type strain increases the catalase activity by 20fold. Overproduction of SU I might impair the correct insertion of heme a3 and CuB because of a deficiency in metal inserting chaperones. An altered distance between heme a3 and CuB and variations in protein structure are possible reasons for the observed increased catalase activity. Co-expression of chaperone-encoding genes genes ctaG and surf1c reduces the catalase activity of the organism, thermal stability is altered about aging, overview Paracoccus denitrificans

Protein Variants

Protein Variants Comment Organism
additional information deletion of the chromosomally encoded gene ctaDII (coding for subunit I present in aa3 CcO), is complemented on a low copy number plasmid controlled by the promoter of the cta operon Paracoccus denitrificans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, overview Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2O2 Paracoccus denitrificans
-
O2 + 2 H2O
-
?
2 H2O2 Paracoccus denitrificans AO1
-
O2 + 2 H2O
-
?
additional information Paracoccus denitrificans bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity ?
-
?
additional information Paracoccus denitrificans AO1 bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans P08303 cytochrome c oxidase with catalase activity; gene ctaG
-
Paracoccus denitrificans AO1 P08303 cytochrome c oxidase with catalase activity; gene ctaG
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from membranes by solubilization with beta--dodecylmaltoside, immuno-affinity chromatography using a Strep-tagged antibody, and ultrafiltration. X-ray crystallography as well as mass spectrometry analysis reveal no signs for any covalent modification of subunit I besides the crosslink between H276 and Y280 Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
Paracoccus denitrificans O2 + 2 H2O
-
?
2 H2O2
-
Paracoccus denitrificans AO1 O2 + 2 H2O
-
?
additional information bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity Paracoccus denitrificans ?
-
?
additional information bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity Paracoccus denitrificans AO1 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Paracoccus denitrificans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Paracoccus denitrificans

pH Range

pH Minimum pH Maximum Comment Organism
5 10 activit range Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
heme
-
Paracoccus denitrificans

General Information

General Information Comment Organism
malfunction the recombinant enzyme shows reduced catalase activity and thermal stability, overview Paracoccus denitrificans
additional information the enzyme's binuclear active center, residing in subunit I, contains heme a3 and CuB. Apart from its oxygen reductase activity, the protein possesses a peroxidase and a catalase activity Paracoccus denitrificans
physiological function the catalase activity of CcO is clearly a side reaction Paracoccus denitrificans