Biopolym. Cell. 2001; 17(6):534-539.
Structure and Function of Biopolymers
Kinetic parameters of the tRNATyr transcript aminoacylation by the bovine liver tyrosyl-tRNA synthetase
1Naidenov V. G., 1Vudmaska M. I., 1Matsuka G. Kh.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680


The full-length tyrosyl-tRNA synthetase from bovine liver and its truncated form without the C-terminal noncatalytic domain were expressed in a bacterial system. Both enzymes have been compared in respect of the aminoacylation kinetic constants. It has been shown that the catalytic efficiency of the yeast tRNATyr and tRNATyr transcript tyrosylation upon deletion of the C-terminal domain decreases by factors of 4 and 18 respectively. The catalytic efficiency decrease in the tRNATyr transcript tyrosylation is mainly due to the increasing of K.w We suggest that the C-terminal domain improves the aminoacylation activity of tyrosyl-tRNA synthetase by strengthening tRNA binding.


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