Journal of Biological Chemistry
Volume 274, Issue 34, 20 August 1999, Pages 23841-23843
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ENZYMOLOGY
Activity of Yeast Orotidine-5′-phosphate Decarboxylase in the Absence of Metals*

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Yeast orotidine-5′-phosphate decarboxylase was recently shown to contain zinc and to be inhibited by zinc-complexing agents. When the gene for the yeast enzyme was expressed in Escherichia coli, the gene product was devoid of metal atoms but exhibited a specific activity and molecular mass similar to those of the enzyme obtained directly from yeast. This invalidates the hypothesis that zinc is involved in substrate decarboxylation. The zinc-free enzyme undergoes thermal inactivation at a somewhat lower temperature than does the zinc-containing enzyme isolated from yeast.

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*

This work was supported in part by National Institutes of Health Grant GM-18324 and National Institutes of Health Training Grant GM-08570.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a grant from the Research Corporation.