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Literature summary for 1.1.3.2 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
Search for more literature for 1.1.3.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aerococcus viridans

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + O2
-
 Aerococcus viridans pyruvate + H2O2
-
 ?
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

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Aerococcus viridans