The structure of L-lactate oxidase from Mycobacterium smegmatis

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Abstract
An improved purification was developed for L-lactate oxidase from M. smegmatis. The MW 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. An amino acid analysis, determinations of protein and flavin, a sedimentation-velocity analysis and an approach to equilibrium analysis gave values for the subunit MW in the range of 43,500-47,000. L-Lactate oxidase apparently contains 8 subunits of MW 43,500. Cross-linking of the subunits with dimethyl suberimidate and EM studies were consistent with an octameric structure.