Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity.
نویسندگان
چکیده
In this study, we have extended our earlier observations indicating in vitro inhibition of arginyl-transfer ribonucleic acid synthetase (EC 6.1.13, arginine: soluble ribonucleic acid ligase, adenosine monophosphate) activity by the arginine biosynthetic precursors ornithine, citrulline, and argininosuccinate. Furthermore, we report evidence which suggest that this enzyme activity is inhibited by these arginine precursors in vivo and that this inhibition of activity results in a derepression of arginine biosynthesis.
منابع مشابه
Evidence for the existence of two arginyl-transfer ribonucleic acid synthetase activities in Escherichia coli.
Two arginyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.13, arginine: ribonucleic acid ligase adenosine monophosphate) activities were found in extracts of Escherichia coli strains AB1132 and NP2. The two arginyl-tRNA synthetase activities in extracts of strain AB1132 were found to be separable by diethylaminoethyl-cellulose column chromatography, Sephadex column fractionation, and by...
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 کاملPurification and Substrate Specificity of Arginyl-ribonucleic Acid Synthetase from Rat Liver.
It is generally accepted that in the first phase of protein biosynthesis, amino acid-specific enzymes, the aminoacyl-ribonucleic acid synthetases, carry out the activation of the various amino acids, and that the exacting specificity of these enzymes extends to the transfer of the amino acid to a particular soluble ribonucleic acid. Several investigators (l-5) have achieved the purification of ...
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...
متن کاملRepression of enzymes of arginine biosynthesis by L-canavanine in arginyl-transfer ribonucleic acid synthetase mutants of Escherichia coli.
We show that the arginine analogue, l-canavanine, repressed the accumulation of translatable messenger ribonucleic acid (RNA) for three arginine biosynthetic enzymes in Escherichia coli. The method used to determine the level of translatable messenger RNA depended upon measurement of a burst of enzyme synthesis as described previously. E. coli strains with defective arginyltransfer ribonucleic ...
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عنوان ژورنال:
- Journal of bacteriology
دوره 115 1 شماره
صفحات -
تاریخ انتشار 1973