Taurine catabolism. II. biochemical and genetic evidence for sulfoacetaldehyde sulfo-lyase involvement.

Cell-free extracts of Pseudomonas aeruginosa. TAU-5 catalyze the cleavage of chemically or enzymatically synthesized sulfoacetaldehyde to form acetate and sulfite. The activity is enhanced by the presence of thiamine pyrophosphate. The sulfo-lyase responsible for this reaction has been partially purified 9-fold in order to separate it from taurine: pyruvate aminotransferase and to demonstrate its role in taurine catabolism. The sulfo-lyase is induced in organisms grown on taurine but not on other compounds tested. The induction occurs co-ordinately with the induction of the aminotransferase. Mutagenesis of the organism yielded a strain which lacks the sulfo-lyase and in incapable of growing on taurine. A revertant of this strain regained all the prototrophic characterics.