Skip to main content
NCBI home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1977 Mar;4(3):673–683. doi: 10.1093/nar/4.3.673

On the binding of aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600.

J Flossdorf, R Marutzky, K Messer, M R Kula
PMCID: PMC342471  PMID: 325520

Abstract

The binding of nine aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600 was measured and compared with the binding of the cognate amino acids. It was found that they bind rather tightly to the enzyme, the Kd's ranging from 3.1.10(-4) M with glycinol-AMP ester to 3.7.10(-9) M with L-isoleucinol-AMP ester. The binding is not affected by magnesium. It is shown that the free energies of binding of the esters can be calculated adding a constant contribution of the AMP-moiety of about - 4.1 (- 17) kcal/mole (kJ/mole) to the free energies of binding of the cognate amino acids, which we have reported earlier (19, 25, 26).

Full text

PDF
673

Selected References

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

  1. Blanquet S., Fayat G., Waller J. P., Iwatsubo M. The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction. Eur J Biochem. 1972 Jan 21;24(3):461–469. doi: 10.1111/j.1432-1033.1972.tb19707.x. [DOI] [PubMed] [Google Scholar]
  2. Blanquet S., Iwatsubo M., Waller J. P. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH. Eur J Biochem. 1973 Jul 2;36(1):213–226. doi: 10.1111/j.1432-1033.1973.tb02903.x. [DOI] [PubMed] [Google Scholar]
  3. Cassio D. Etude de la méthionyl tRNA synthétase de Escherichia coli. 2. Inactivation sélective et réversible de la capacité de charger le tRNA. Eur J Biochem. 1968 Apr 3;4(2):222–224. doi: 10.1111/j.1432-1033.1968.tb00197.x. [DOI] [PubMed] [Google Scholar]
  4. Cassio D., Lemoine F., Waller J. P., Sandrin E., Boissonnas R. A. Selective inhibition of aminoacyl ribonucleic acid synthetases by aminoalkyl adenylates. Biochemistry. 1967 Mar;6(3):827–836. doi: 10.1021/bi00855a024. [DOI] [PubMed] [Google Scholar]
  5. DIXON M. The determination of enzyme inhibitor constants. Biochem J. 1953 Aug;55(1):170–171. doi: 10.1042/bj0550170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dahlquist F. W., Jao L., Raftery M. On the binding of chitin oligosaccharides to lysozyme. Proc Natl Acad Sci U S A. 1966 Jul;56(1):26–30. doi: 10.1073/pnas.56.1.26. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dureković A., Flossdorf J., Kula M. R. Isolation and properties of isoleucyl-tRNA synthetase from Escherichia coli MRE 600. Eur J Biochem. 1973 Jul 16;36(2):528–533. doi: 10.1111/j.1432-1033.1973.tb02939.x. [DOI] [PubMed] [Google Scholar]
  8. Flossdorf J., Kula M. R. Ultracentrifuge studies on binding of aliphatic amino acids to isoleucyl-tRNA synthetase from Escherichia coli MRE 600. Eur J Biochem. 1973 Jul 16;36(2):534–540. doi: 10.1111/j.1432-1033.1973.tb02940.x. [DOI] [PubMed] [Google Scholar]
  9. Flossdorf J., Prätorius H. J., Kula M. R. Influence of side-chain structure of aliphatic amino acids on binding to isoleucyl-tRNA synthetase from Escherichia coli MRE 600. Eur J Biochem. 1976 Jun 15;66(1):147–155. doi: 10.1111/j.1432-1033.1976.tb10435.x. [DOI] [PubMed] [Google Scholar]
  10. Holler E., Bennett E. L., Calvin M. 2-p-Toluidinylnaphthalene-6-sulfonate, a fluorescent reporter group for L-isoleucyl-tRNA synthetase. Biochem Biophys Res Commun. 1971 Oct 15;45(2):409–415. doi: 10.1016/0006-291x(71)90834-5. [DOI] [PubMed] [Google Scholar]
  11. Holler E., Calvin M. Isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B. A rapid kinetic investigation of the L-isoleucine-activating reaction. Biochemistry. 1972 Sep 26;11(20):3741–3752. doi: 10.1021/bi00770a012. [DOI] [PubMed] [Google Scholar]
  12. Holler E., Rainey P., Orme A., Bennett E. L., Calvin M. On the active site topography of isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B. Biochemistry. 1973 Mar 13;12(6):1150–1159. doi: 10.1021/bi00730a021. [DOI] [PubMed] [Google Scholar]
  13. MICHELSON A. M. SYNTHESIS OF NUCLEOTIDE ANHYDRIDES BY ANION EXCHANGE. Biochim Biophys Acta. 1964 Sep 11;91:1–13. doi: 10.1016/0926-6550(64)90164-1. [DOI] [PubMed] [Google Scholar]
  14. Mehler A. H., Chakraburtty K. Some questions about the structure and activity of aminoacyl-tRNA synthetases. Adv Enzymol Relat Areas Mol Biol. 1971;35:443–501. doi: 10.1002/9780470122808.ch8. [DOI] [PubMed] [Google Scholar]
  15. Santi D. V., Peńa V. A. Tyrosyl transfer ribonucleic acid synthetase from Escherichia coli B. Analysis of tyrosine and adenosine 5'-triphosphate binding sites. J Med Chem. 1973 Mar;16(3):273–280. doi: 10.1021/jm00261a025. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES