Structural study of selenocysteine lyase

establish structure-function relationships for the enolase reaction.The crystal structures of the activated enolase (carboxylated on Lys 173) and enolase liganded with Mg and 2,3-diketohexane, a stable alternate substrate, were determined.The stereochemical course of the reaction catalyzed by the enolase was determined using stereospecifically deuterated samples of an alternate substrate.On the basis of these experiments we conclude that the enolase, the functionally divergent member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate , but the proton abstraction is catalyzed by a different general base.

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