The structure of L-lactate oxidase from Mycobacterium smegmatis.
1. An improved purification was developed for L-lactate oxidase from Mycobacterium smegmatis. 2. The mol.wt. of the native enzyme by a sedimentation-equilibrium analysis was 345 000, and other ultracentrifuge methods gave values in the range 345 000-350 000. 3. An amino acid analysis, determinations of protein and flavin, a sedimentation-velocity analysis and an approach to equilibrium analysis gave values for the subunit mol.wt. in the range 43 500-47 000. 4. It was concluded that L-lactate oxidase contains eight subunits of mol.wt. 43 500. 5. Cross-linking of the subunits with dimethyl suberimidate and electron-microscopy studies were consistent with an octameric structure.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D007773:Lactates; D008854:Microscopy, Electron; D006899:Mixed Function Oxygenases / Q000032:analysis*; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology*; D010088:Oxidoreductases / Q000032:analysis*; D013057:Spectrum Analysis
D000596:Amino Acids; D007773:Lactates; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases