FEEDBACK CONTROL OF PURIFIED DEOXYCYTIDYLATE DEAMINASE.
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.
D000619:Aminohydrolases; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002642:Chick Embryo; D003597:Cytosine Nucleotides; D003844:DCMP Deaminase; D008274:Magnesium; D009711:Nucleotides; D012106:Research; D013942:Thymine Nucleotides; D014508:Urea
D003597:Cytosine Nucleotides; D009711:Nucleotides; D013942:Thymine Nucleotides; D014508:Urea; D000619:Aminohydrolases; D003844:DCMP Deaminase; D008274:Magnesium; C024157:thymidine 5'-triphosphate
AMINOHYDROLASES; CHEMISTRY; CHICK EMBRYO; EXPERIMENTAL LAB STUDY; NUCLEOTIDES; UREA