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. 1963 Sep 27;141(3587):1278-9.
doi: 10.1126/science.141.3587.1278.

FEEDBACK CONTROL OF PURIFIED DEOXYCYTIDYLATE DEAMINASE

G F MALEY, F MALEY

FEEDBACK CONTROL OF PURIFIED DEOXYCYTIDYLATE DEAMINASE

G F MALEY et al. Science. .

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 degrees 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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