The role of divalent cations in the reactions of valyl transfer ribonucleic acid synthetase of Escherichia coli. Effects of spermine and ethylenediaminetetraacetate.

نویسندگان

  • K Chakraburtty
  • C F Midelfort
  • A Steinschneider
  • A H Mehler
چکیده

We have analyzed the function of spermine in the aminoacylation of tRNA-Val by the valyl-tRNA synthetase of Escherichia coli. Our results indicate that Mg2+ is required for the aminoacylation reaction as well as for the ATP-PP-i exchange catalyzed by this enzyme. The apparent stimulation by spermine is a function of the tRNA used, which appears to contain bound cations even after dialysis against 10 minus 4 M EDTA. Higher concentrations of EDTA totally abolish spermine-stimulated esterification of tRNA-Val.

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The Role of Divalent Cations in the Reactions of Valyl Transfer Ribonucleic Acid Synthetase of Escherichia co1 i EFFECTS OF SPERMINE AND ETHYLENEDIAMINETETRAACETATE*

We have analyzed the function of spermine in the aminoacylation of tRNA Val by the valyl-tRNA synthetase of Escherichia coli. Our results indicate that Mg2+ is required for the aminoacylation reaction as well as for the ATP-PPi exchange catalyzed by this enzyme. The apparent stimulation by spermine is a function of the tRNA used, which appears to contain bound cations even after dialysis agains...

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 250 10  شماره 

صفحات  -

تاریخ انتشار 1975