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Literature summary for 1.7.2.4 extracted from
- The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity (2010), FEBS J., 277, 3176-3189.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pyrobaculum aerophilum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| modeling of structure. The residues contributing to the semiocclusion of the T1 copper site are Trp355, Met389, and Met297. There is a negatively charged residue in the neighborhood of the T1 site, Glu296 | Pyrobaculum aerophilum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E296Q | mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type | Pyrobaculum aerophilum |
| M297A | mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type | Pyrobaculum aerophilum |
| M389A | mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type | Pyrobaculum aerophilum |
| W355A | mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type | Pyrobaculum aerophilum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.032 | - |
N2O | pH 7.6, 25°C | Pyrobaculum aerophilum |  |
| 0.033 | - |
Fe2+ | pH 7.6, 25°C | Pyrobaculum aerophilum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| copper | 3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold | Pyrobaculum aerophilum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 49600 | - |
gel fitlration | Pyrobaculum aerophilum |
| 52000 | - |
1 * 52900, calculated, 1 * 52000, SDS-PAGE | Pyrobaculum aerophilum |
| 52900 | - |
1 * 52900, calculated, 1 * 52000, SDS-PAGE | Pyrobaculum aerophilum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrobaculum aerophilum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme shows Cu+/Fe2+ oxidation kinetics that follow the Michaelis-Menten model, with 2fold to 10fold higher efficiencies for Cu+ and Fe2+ as compared with the tested aromatic compounds | Pyrobaculum aerophilum | ? | - |
? | |
| N2O + 2 Fe2+ + 2 H+ | - |
Pyrobaculum aerophilum | N2 + H2O + 2 Fe3+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 52900, calculated, 1 * 52000, SDS-PAGE | Pyrobaculum aerophilum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| McoP | - |
Pyrobaculum aerophilum |
| multicopper oxidase | - |
Pyrobaculum aerophilum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
- |
Pyrobaculum aerophilum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
half-life 5.5 h | Pyrobaculum aerophilum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 8 | - |
N2O | pH 7.6, 25°C | Pyrobaculum aerophilum | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 242 | - |
Fe2+ | pH 7.6, 25°C | Pyrobaculum aerophilum | |
| 250 | - |
N2O | pH 7.6, 25°C | Pyrobaculum aerophilum | |
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Release 2023.1 (January 2023)
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