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.
D000079:Acetaldehyde / Q000031:analogs & derivatives / Q000378:metabolism; D000085:Acetates / Q000032:analysis; D000476:Alkanesulfonates / Q000378:metabolism; D004790:Enzyme Induction; D008190:Lyases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013447:Sulfites / Q000032:analysis; D013654:Taurine / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000378:metabolism; D000637:Transaminases / Q000378:metabolism
D000085:Acetates; D000476:Alkanesulfonates; D013447:Sulfites; D013654:Taurine; C015517:sulfoacetaldehyde; C022707:sulphoacetaldehyde lyase; D000637:Transaminases; C022715:taurine pyruvate aminotransferase; D008190:Lyases; D000079:Acetaldehyde; D013835:Thiamine Pyrophosphate