Isolation and properties of tRNA nucleotidyltransferase from wheat embryos.
From wheat embryos, tRNA nucleotidyltransferase (EC 2.7.7.25) was isolated. By chromatography on Sepharose 6B, DEAE-cellulose and affinity chromatography on tRNA-hydrazyl-Sepharose 4B, 7000-fold purification of the enzyme was achieved. The enzyme required for its activity Mg2+ or Mn2+ ion. ATP inhibited incorporation of CMP from CTP into lupin tRNA, and CTP acted as a competitive inhibitor of AMP incorporation from ATP. The regulatory role of ATP in incorporation of terminal CMP into tRNA is discussed. The incorporation of terminal CMP into tRNA deprived of terminal CCA or CA, was also studied.
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D010944:Plants / Q000201:enzymology*; D012316:RNA Nucleotidyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D014908:Triticum / Q000201:enzymology
D000249:Adenosine Monophosphate; D008345:Manganese; D000255:Adenosine Triphosphate; D012316:RNA Nucleotidyltransferases; D008274:Magnesium