Enzymatic oxidation of isethionate to sulfoacetaldehyde in bacterial extract.
Isethionate degradation in a bacterial extract was shown by the isolation of enzymes and by identification of an intermediate to take place in two steps; dehydrogenation to sulfoacetaldehyde and desulfonation leading to the formation of sulfite and acetate. The enzyme responsible for isethionate oxidation in the presence of FAD was particulate in nature and a solubilized preparation obtained by extraction with buffer of low ionic strength had oxidizing activities against only isethionate and n-butanol among compounds tested. The enzyme was inhibited by thiol and carbonyl reagents.
D000079:Acetaldehyde / Q000031:analogs & derivatives* / Q000378:metabolism; D000476:Alkanesulfonates / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide; D007513:Isethionic Acid / Q000378:metabolism*; D007700:Kinetics; D010088:Oxidoreductases / Q000378:metabolism; D013447:Sulfites / Q000378:metabolism
D000476:Alkanesulfonates; D013447:Sulfites; D005182:Flavin-Adenine Dinucleotide; D007513:Isethionic Acid; D010088:Oxidoreductases; D000079:Acetaldehyde