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. 1981 Feb;67(2):316–324. doi: 10.1104/pp.67.2.316

Selenium Metabolism in Neptunia amplexicaulis1

James N Burnell 1
PMCID: PMC425675  PMID: 16661667

Abstract

ATP sulfurylase (EC 2.7.7.4), cysteinyl-tRNA synthetase (EC 6.1.1.16), and methionyl-tRNA synthetase (EC 6.1.1.10) from Neptunia amplexicaulis have been purified approximately 162-, 140- and 185-fold, respectively. Purified ATP sulfurylase in the presence of purified inorganic pyrophosphatase catalyzed the incorporation of sulfate into adenosine 5′-phosphosulfate; evidence of an analogous reaction with selenate is presented. Crude extracts catalyzed both the sulfate- and the adenosine 5′-phosphosulfate-dependent NADH oxidation in the adenosine 5′-phosphosulfate kinase assay of Burnell and Whatley (1977 Biochim Biophys Acta 481: 266-278), but an analogous reaction with selenate could not be detected. Both purified cysteinyl-tRNA synthetase and methionyl-tRNA synthetase used selenium-containing analogs as substrates in both the ATP-pyrophosphate exchange and the aminoacylation assays.

It seems that selenium-containing amino acids are excluded from proteins by a mechanism(s) other than substrate discrimination at the amino acid activation stage of protein synthesis.

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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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