Abstract
Recently, it has been shown that Se-(2-aminoethyl)selenosulfuric acid (H2NCH2CH2—SeSO3H) or Se-sulfoselenocysteamine (SeSC) may undergo transamination with α-ketoglutaric acid in the presence of sonicated rat liver mitochondria giving acetaldehyde and selenosulfate as final products, in addition to glutamate.1 In the same conditions selenohypotaurine may also transaminate2 whereas other analogues, e.g. hypotaurine, taurine, selenotaurine and S-sulfocysteamine do not react. This is a very interesting example of an enzymic reaction in which the substitution of a selenium atom by a sulfur atom in the substrate molecule significantly affects the substrate specificity of the enzyme.