J Biochem. 1977 Jun;81(6):1911-6.

Enzymatic oxidation of isethionate to sulfoacetaldehyde in bacterial extract.

Kondo H, Niki H, Takahashi S, Ishimoto M.

Abstract

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.

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