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. 1979 Jun;63(6):1095–1097. doi: 10.1104/pp.63.6.1095

Cysteinyl-tRNA Synthetase from Astragalus Species 1

James N Burnell a, Alex Shrift b
PMCID: PMC542976  PMID: 16660863

Abstract

l-Cysteinyl-tRNA synthetases (EC 6.1.1.16) from four Astragalus species were partially purified. The substrate specificities of the cysteinyl-tRNA synthetase from three selenium accumulator species (A. crotalariae, A bisulcatus, and A. racemosus) were compared with those from two nonaccumulator species (A. lentigenosus and Phaseolus aureus). All species had similar Km values for cysteine, selenocysteine, and α-aminobutyric acid except A. bisulcatus which failed to use selenocysteine as a substrate and which had a Km for cysteine four times greater than the Km values for other species.

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Selected References

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

  1. Baldwin A. N., Berg P. Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase. J Biol Chem. 1966 Feb 25;241(4):839–845. [PubMed] [Google Scholar]
  2. Burnell J. N. Cysteinyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties. Plant Physiol. 1977 Nov;60(5):670–674. doi: 10.1104/pp.60.5.670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Burnell J. N., Whatley F. R. Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of cysteinyl-and methionyl-tRNA synthetase. Biochim Biophys Acta. 1977 Mar 15;481(1):266–278. doi: 10.1016/0005-2744(77)90158-9. [DOI] [PubMed] [Google Scholar]
  4. Fowden L., Lewis D., Tristram H. Toxic amino acids: their action as antimetabolites. Adv Enzymol Relat Areas Mol Biol. 1967;29:89–163. doi: 10.1002/9780470122747.ch3. [DOI] [PubMed] [Google Scholar]
  5. Hoffman J. L., McConnell K. P., Carpenter D. R. Aminoacylation of Escherichia coli methionine tRNA by selenomethionine. Biochim Biophys Acta. 1970 Feb 18;199(2):531–534. doi: 10.1016/0005-2787(70)90098-5. [DOI] [PubMed] [Google Scholar]
  6. Jáuregui-Adell J. Selenium derivatives in proteins. Adv Protein Chem. 1966;21:387–415. doi: 10.1016/s0065-3233(08)60130-8. [DOI] [PubMed] [Google Scholar]
  7. Shaw W. H., Anderson J. W. Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue. Biochem J. 1972 Mar;127(1):237–247. doi: 10.1042/bj1270237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Shrift A., Bechard D., Harcup C. Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus. Plant Physiol. 1976 Sep;58(3):248–252. doi: 10.1104/pp.58.3.248. [DOI] [PMC free article] [PubMed] [Google Scholar]

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