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Literature summary extracted from

  • Maeda-Yorita, K.; Aki, K.; Sagai, H.; Misaki, H.; Massey, V.
    L-lactate oxidase and L-lactate monooxygenase mechanistic variations on a common structural theme (1995), Biochimie, 77, 631-642 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.2 expression in Escherichia coli Aerococcus viridans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.2 0.00034
-
 (S)-lactate pH 7.0, 4°C Aerococcus viridans
1.1.3.2 0.00094
-
 (S)-lactate pH 7.0, 25°C Aerococcus viridans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.2 80000
-
 gel filtration Aerococcus viridans

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.2 Aerococcus viridans Q44467
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.2 210
-
 pH 7.0, 37°C Aerococcus viridans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.2 (S)-lactate + O2
-
 Aerococcus viridans pyruvate + H2O2
-
 ?
1.1.3.2 additional information contrary to lactate monooxygenase, with lactate oxidase the complex of reduced flavin enzyme and pyruvate dissociates rapidly, with the result that it is the free reduced flavin form of the enzyme that reacts with O2, to give the observed products, pyruvate and H2O2 Aerococcus viridans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.2 dimer 2 * 40000, SDS-PAGE and calculated Aerococcus viridans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.2 31
-
 (S)-lactate pH 7.0, 4°C Aerococcus viridans
1.1.3.2 280
-
 (S)-lactate pH 7.0, 25°C Aerococcus viridans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.2 FMN
-
 Aerococcus viridans