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Literature summary extracted from

  • Fernandes, A.T.; Damas, J.M.; Todorovic, S.; Huber, R.; Baratto, M.C.; Pogni, R.; Soares, C.M.; Martins, L.O.
    The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity (2010), FEBS J., 277, 3176-3189.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.4 expression in Escherichia coli Pyrobaculum aerophilum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.4 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

EC Number Protein Variants Comment Organism
1.7.2.4 E296Q mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type Pyrobaculum aerophilum
1.7.2.4 M297A mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type Pyrobaculum aerophilum
1.7.2.4 M389A mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type Pyrobaculum aerophilum
1.7.2.4 W355A mutation near T1 copper site, similar biochemical and spectroscopic properties to those of the wild type Pyrobaculum aerophilum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.4 0.032
-
 N2O pH 7.6, 25°C Pyrobaculum aerophilum
1.7.2.4 0.033
-
 Fe2+ pH 7.6, 25°C Pyrobaculum aerophilum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.4 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.4 49600
-
 gel fitlration Pyrobaculum aerophilum
1.7.2.4 52000
-
 1 * 52900, calculated, 1 * 52000, SDS-PAGE Pyrobaculum aerophilum
1.7.2.4 52900
-
 1 * 52900, calculated, 1 * 52000, SDS-PAGE Pyrobaculum aerophilum

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.4 Pyrobaculum aerophilum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.4 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 ?
-
 ?
1.7.2.4 N2O + 2 Fe2+ + 2 H+
-
 Pyrobaculum aerophilum N2 + H2O + 2 Fe3+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.4 monomer 1 * 52900, calculated, 1 * 52000, SDS-PAGE Pyrobaculum aerophilum

Synonyms

EC Number Synonyms Comment Organism
1.7.2.4 McoP
-
 Pyrobaculum aerophilum
1.7.2.4 multicopper oxidase
-
 Pyrobaculum aerophilum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.4 85
-
-
 Pyrobaculum aerophilum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.7.2.4 85
-
 half-life 5.5 h Pyrobaculum aerophilum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.4 8
-
 N2O pH 7.6, 25°C Pyrobaculum aerophilum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.7.2.4 242
-
 Fe2+ pH 7.6, 25°C Pyrobaculum aerophilum
1.7.2.4 250
-
 N2O pH 7.6, 25°C Pyrobaculum aerophilum