Abstract
Abstract Upon deamination of chirally labeled [2-2H, 3H]ethanolamine by the adenosylcobalamin-dependent ethanolamine ammonia-lyase (EC 4.3.1.7) from Clostridium sp., chirality of the labeled carbon atom is lost. This result is consistent with a mechanism involving the 1-amino-1-hydroxyethane2-yl radical as a catalytic intermediate.
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