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. 1976 Aug;3(8):2067–2077. doi: 10.1093/nar/3.8.2067

ATP-analogues as substrates for the leucyl-tRNA synthetase from Escherichia coli MRE 600.

R Marutzky, J Flossdorf, M R Kula
PMCID: PMC343062  PMID: 787930

Abstract

No analogous nucleoside triphosphate was found which acts as well as ATP in binding to and supporting catalysis of leucyl-tRNA synthetase from Escherichia coli MRE 600. However, there are numerous nucleotides which are able to replace ATP, but with lower efficiency. The 6-amino group of the adenine ring and the 2'-hydroxyl group of the ribose ring are essential for binding and catalytic activity. Alterations in the triphosphate moiety of the molecule can cause drastic changes in Km and/or Vmax, whereas alterations of the imidazole ring and substitutions at the 8-position of the adenine ring cause only minor losses of catalytic activity.

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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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