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Literature summary extracted from
- 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.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.6 | phosphatidylcholine | - |
Paracoccus denitrificans |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.11.1.6 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.11.1.6 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.11.1.6 | additional information | - |
additional information | Michaelis-Menten kinetics, overview | Paracoccus denitrificans |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.6 | 2 H2O2 | Paracoccus denitrificans | - |
O2 + 2 H2O | - |
? | |
| 1.11.1.6 | 2 H2O2 | Paracoccus denitrificans AO1 | - |
O2 + 2 H2O | - |
? | |
| 1.11.1.6 | additional information | Paracoccus denitrificans | bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity | ? | - |
? | |
| 1.11.1.6 | additional information | Paracoccus denitrificans AO1 | bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.6 | Paracoccus denitrificans | P08303 | cytochrome c oxidase with catalase activity; gene ctaG | - |
| 1.11.1.6 | Paracoccus denitrificans AO1 | P08303 | cytochrome c oxidase with catalase activity; gene ctaG | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.11.1.6 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.6 | 2 H2O2 | - |
Paracoccus denitrificans | O2 + 2 H2O | - |
? | |
| 1.11.1.6 | 2 H2O2 | - |
Paracoccus denitrificans AO1 | O2 + 2 H2O | - |
? | |
| 1.11.1.6 | additional information | bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity | Paracoccus denitrificans | ? | - |
? | |
| 1.11.1.6 | additional information | bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity | Paracoccus denitrificans AO1 | ? | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.6 | 40 | - |
assay at | Paracoccus denitrificans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.6 | 7.5 | - |
- |
Paracoccus denitrificans |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.6 | 5 | 10 | activit range | Paracoccus denitrificans |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.6 | heme | - |
Paracoccus denitrificans | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.11.1.6 | malfunction | the recombinant enzyme shows reduced catalase activity and thermal stability, overview | Paracoccus denitrificans |
| 1.11.1.6 | 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 |
| 1.11.1.6 | physiological function | the catalase activity of CcO is clearly a side reaction | Paracoccus denitrificans |
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