Deoxycytidine monophosphate deaminase

Gelbard, A. S., Kim, J. H., and Perez, A. G., 1969, Fluctuations in deoxycytidine monophosphate deaminase activity during the cell cycle in synchronous populations of HeLa cells, Biochim. Biophys. Acta 182 564. 

Deoxycytidylate deaminase was first isolated from sea urchin e s by Scarano and has since been demonstrated in many animal tissues the deaminases from spleen and chick embryo have been partly purified (23, 24). The enzyme requires that the substrate must be a 4-aminopyrimidine deoxyribonucleoside 5 -monophosphate, and will accept the following substituents at the pyrimidine 5-position methyl, hydroxymethyl, fluoro, iodo, and bromo. Notably, the following are not deaminated cytidine, deoxycytidine, eytidylate, dCDP, and dCTP. The concentration of this enzyme in cells appears to be related to their proliferative state in that the enzyme is found in growing tissues, but activities are low in adult tissues such as liver. 

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