[Thymidine and thymidylate kinases from the scallop Mizuhopecten yessoensis gonads].
Thymidine and thymidylate kinases were isolated from the gonads of scallop Mizuhopecten yessoensis. The enzymes were purified 537- and 100-fold, respectively, and were free of phosphatase and ATPase impurities. Ions of bivalent metals and ATP were necessary for both the nucleoside and nucleotide kinase activities; the pH optimum fall into the range of 7.5-8.5. KCl and NaCl at a concentration of up to 100 mM had no inhibiting effect on the activities of these scallop enzymes. Thymidine kinase catalyzed thymidine, and, at a lower rate, deoxycytidine phosphorylations did not utilize ribo- and deoxyribonucleosides, as well as pyrimidine ribonucleosides, as a phosphate acceptor. Thymidylate kinase phosphorylated TMP and dCMP with an efficiency of about 30%. In addition to ATP, these enzymes can also utilize with different efficiencies dATP, dGTP, GTP, UTP, and CTP as a donor of phosphate groups. Thymidine kinase activity was inhibited by TMP, TTP, and dCTP.
Terent'ev
L L
LL
Terent'eva
N A
NA
Rasskazov
V A
VA
D000818:Animals; D006066:Gonads / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D009711:Nucleotides / Q000737:chemistry; D049897:Pectinidae / Q000201:enzymology*; D013379:Substrate Specificity; D013936:Thymidine / Q000737:chemistry*; D013937:Thymidine Kinase / Q000737:chemistry* / Q000302:isolation & purification*
D009711:Nucleotides; D013937:Thymidine Kinase; D013936:Thymidine