Abstract
Abstract We discovered peculiar enzymes participating in selenium amino acid metabolism: selenocysteine β-lyase occurring in mammalian tissues and bacteria, and D-selenocystine α,β-lyase occurring in Clostridium sticklandii. We here describe enzymological properties and reaction mechanisms of these enzymes. We synthesized the selenocysteine analogues of Neurospora crassa copper metallothionein as well as four diastereoisomers of glutathione. Their physicochemical properties and reactivity with peroxides are also described.
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