Plant tRNA nucleotidyltransferase : II. Some properties of the purified enzyme from Lupinus luteus seeds

Planta
H CudnyJ Kaczkowski

Abstract

Purified lupine tRNA nucleotidyltransferase catalyzed only the incorporation of AMP and CMP into 3'-terminal-C-C-A sequences of tRNA as determined by terminal analysis of the reaction product. The incorporation of AMP and CMP was inhibited by their respective triphosphates to different degrees; UTP also showed an inhibitory effect. The pH optimum of the purified enzyme was found to be 9.5 in glycine buffer. The enzyme required magnesium or manganese ions for its activity.-SH reagents reversibly inhibited the action of the enzyme. Kinetic data, the different effects of ionic strength on the incorporation of AMP and CMP, and different rates of thermal inactivation for AMP and CMP incorporation in connection with chromatographic properties of the enzyme suggest the existence of only one form of tRNA nucleotidyltransferase with different catalytic sites for ATP and CTP.

References

Feb 5, 1977·Journal of Molecular Biology·M P Deutscher, J A Evans
Jan 1, 1973·Progress in Nucleic Acid Research and Molecular Biology·M P Deutscher
Aug 29, 1974·Biochimica Et Biophysica Acta·D S CarreF Chapeville
Nov 1, 1970·European Journal of Biochemistry·H J GrossW C Fiers
Sep 24, 1971·European Journal of Biochemistry·H SternbachF Cramer
Dec 14, 1970·Biochimica Et Biophysica Acta·D S CarreF Chapeville

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