
Streptococcal pyruvate oxidase (SpxB) is a hydrogen peroxide‐generating enzyme and plays a critical role in Streptococcus sanguinis interspecies interactions, but less is known about its biochemistry. We examined SpxB subcellular localization using protein fractionation and microscopy and found SpxB to be primarily cytoplasmic, but a small portion is also membrane associated. Potential post translational modifications of SpxB were determined using coimmunoprecipitation and mass spectrometry. Overall, our data suggest that SpxB post translational modifications likely play a major role to regulate SpxB function in S.sanguinis.
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