Reports

Feedback Control of Purified Deoxycytidylate Deaminase

Science  27 Sep 1963:
Vol. 141, Issue 3587, pp. 1278-1279
DOI: 10.1126/science.141.3587.1278

Abstract

The activity of purified deoxycytidylate deaminase obtained from chick-embryo extracts is dependent upon the presence of deoxycytidine triphosphate and magnesium ions. The stability of the enzyme at 37 °C is markedly enhanced by deoxycytidine triphosphate, and less so by the other deoxyribonucleotides. The inhibition by p-chloromercuribenzoate, urea, and deoxythymidine triphosphate, is reversed by deoxycytidine triphosphate. This reversal suggests that the regulation of enzyme activity is effected through configurational changes in the enzyme structure.

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