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. 1979 Apr;6(4):1631–1638. doi: 10.1093/nar/6.4.1631

The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli).

F Grosse, G Krauss, R Kownatzki, G Maass
PMCID: PMC327796  PMID: 377229

Abstract

The binding between tyrosyl-tRNA synthetase (E.coli) and the alkylanalogue of the aminoacyladenylate, tyrosinyl-5'-AMP, has been investigated by fluorescence titrations and rapid mixing experiments. Tyrosyl-tRNA synthetase has two equivalent and independent binding sites for tyrosinyl-5'-AMP. The intrinsic binding constant is 4 x 10(7)M-1. The binding sites for tRNATyr and tyrosinyl-5'-AMP are independent of each other, the anticooperative mode of tRNA binding being preserved in the presence of tyrosinyl-5-AMP.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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