Purification and properties of Aerococcus viridans lactate oxidase

Biochem Biophys Res Commun. 1989 Oct 31;164(2):919-26. doi: 10.1016/0006-291x(89)91546-5.


Lactate oxidase was purified from cells of Aerococcus viridans by a procedure which utilized ammonium sulfate fractionation, DEAE Sepharose CL-6B chromatography, and Sephadex G-100 chromatography. The final preparation was homogeneous by SDS-polyacrylamide gel electrophoresis. The enzyme appears to be a tetramer with a subunit molecular weight of 44,000 and utilizes FMN as a cofactor. The enzyme was highly specific for L-lactate. D-lactate, glycolate, and D,L-2-hydroxybutyrate were not oxidized by the enzyme but were competitive inhibitors. The enzyme could be irreversibly inactivated by incubation with bromopyruvate. This inactivation appears to involve a covalent modification near the active site of the enzyme; however, the flavin cofactor is not the site of this modification.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Kinetics
  • Mixed Function Oxygenases / metabolism
  • Molecular Weight
  • Streptococcaceae / enzymology*
  • Streptococcaceae / growth & development


  • Mixed Function Oxygenases
  • lactate 2-monooxygenase