The Activation of Arginyl Transfer Ribonucleic Acid Synthetase by Transfer Ribonucleic Acid
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چکیده
منابع مشابه
The activation of arginyl transfer ribonucleic acid synthetase by transfer ribonucleic acid.
The arginine-activating enzyme of Escherichk coli requires transfer ribonucleic acid (tRNA) for catalysis of the ATP-pyrophosphate exchange reaction. Only the specific arginiie-accepting tRNA is effective5 and the terminal adenylic acid residue is essential for the reaction. A previously described isotope-trapping experiment led to the suggestion that an arginyl-tRNA ester was not formed during...
متن کاملThe arginyl transfer ribonucleic acid synthetase of Escherichia coli.
The arginyl transfer ribonucleic acid (tRNA) synthetase of Escherichia coli has been purified over SO&fold. Its kinetic properties are similar to those of other amino acidactivating enzymes; it has a pH optimum near 8 and does not react with amino acids that occur in proteins other than arginine, but the analogues homoarginine and canavanine are competitive inhibitors, and canavanine can be est...
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The valyl-transfer ribonucleic acid (tRNA) synthetase of Escherichia coli strain NP2907, previously described as having an elevated Km for adenosine triphosphate and reduced stability in vitro compared to the wild type, was found to be conditionally thermolabile in vivo. The rate of inactivation of this enzyme at a particular temperature appears to be coordinated with the rate of growth; at 40 ...
متن کاملInhibition of arginyl-transfer ribonucleic acid synthetase activity of Escherichia coli by arginine biosynthetic precursors.
The arginine biosynthetic precursors, ornithine, citrulline, and argininosuccinate, inhibit arginyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.13, arginine: soluble RNA ligase, adenosine monophosphate) activity in the in vitro attachment assay system. Ornithine is the most potent, argininosuccinate is next, and citrulline is least effective. The implications of these results are disc...
متن کاملAn arginyl-transfer ribonucleic Acid protein transferase from cereal embryos.
Embryos from rice (Oryza sativa L. var. Bluebonnet) and wheat (Triticum aestivum L.) contain an aminoacyl-tRNA protein transferase which transfers arginine from arginyl-tRNA to the N terminus of a protein acceptor. The activity was measured in vitro in a reaction mixture containing embryo supernatant fraction, buffer, sulfhydryl reagent, and arginyl-tRNA. It was not dependent on the usual cofac...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1967
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)99386-5