Amino acid substrate specificity of asparaginyl-,aspartyl- and glutaminyl-tRNA synthetase isolated from higher plants |
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Authors: | Peter J Lea Leslie Fowden |
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Institution: | Department of Botany and Microbiology, University College Gower Street London WC1E, 6BT U.K. |
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Abstract: | AspNH2-, Asp- and GluNH2-tRNA synthetases were purified from Phaseolus aureus; their optimum assay conditions, substrate specificities and salt sensitivities were investigated. AspNH2-tRNA synthetase from β-cyanoalanine-producing (Vicia sativa), and non-producing (P. aureus and V. faba) species was able to utilize the analogue as a substrate irrespective of the source of the enzyme. Asp-tRNA synthetase from P. aureus was able to utilize α-aminomalonate and threo-β-hydroxy Asp as a substrate. The transfer of 14C-GluNH2 to tRNA, catalyzed by GluNH2-tRNA synthetase, was only inhibited by high concentrations of those analogues tested; albizziine was the most efficient, but no difference could be demonstrated between the substrate specificities of the enzyme isolated from an albizziine-producer (A. julibrissin and a non-producer (P. aureus) species. |
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Keywords: | Leguminosae amino acid-transfer RNA synthetases amino acid substrate specificity |
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