Crucial role of pyrophosphate in the aminoacylation of E. coli tRNA super(Phe) by yeast phenylalanyl-tRNA synthetase

Rapid inactivation of the yeast phenylalanyl-tRNA synthetase in the course of aminoacylation of the heterologous E. coli tRNA super(Phe) is observed. This inactivation occurs due to the formation of the tight complex of the enzyme with the pyrophosphate formed during the aminoacylation reaction. Thi...

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Bibliographic Details
Published in:FEBS letters 1992-01, Vol.311 (2), p.139-142
Main Authors: Khvorova, A M, Motorin, YA, Wolfson, AD
Format: Article
Language:English
Subjects:
Escherichia coli
Saccharomyces cerevisiae
Online Access:Get full text
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Summary:Rapid inactivation of the yeast phenylalanyl-tRNA synthetase in the course of aminoacylation of the heterologous E. coli tRNA super(Phe) is observed. This inactivation occurs due to the formation of the tight complex of the enzyme with the pyrophosphate formed during the aminoacylation reaction. This complex is shown to be the normal intermediate of the reaction. Possible inactivation mechanism and correlation between structural differences of yeast and E. coli tRNAs super(Phe) with the changes in the enzymatic mechanism of aminoacylation are discussed.
ISSN:0014-5793