Selenium Metabolism in Neptunia amplexicaulis |
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Authors: | Burnell J N |
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Institution: | School of Environmental and Life Sciences, Murdoch University, Murdoch, Western Australia 6155. |
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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. |
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