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Avian liver mevalonate 5-diphosphate decarboxylase: substrate and inhibitor activities of the phosphorothioate analogues of adenosine triphosphate.

The diastereoisomers of ATP alpha S and of ATP beta S have been used as substrate analogues for avian liver mevalonate 5-diphosphate decarboxylase. When the diastereoisomers of ATP alpha S were used, no reversal of the stereospecificity was seen upon changing Mg2+ for Cd2+, thus suggesting that the metal ion does not coordinate through the alpha-phosphoryl group of the nucleotide. Reversal of the stereospecificity, however, was observed when using the diastereoisomers of ATP beta S and upon changing Mg2+ by Zn2+ as the activating metal ion. Similar competitive inhibition constants for the diastereoisomers of MgATP beta S against MgATP were found. It is proposed that the active metal-nucleotide complex in catalysis is the lambda, beta-gamma MgATP complex.