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The differential rates of synthesis of the three branched-chain aminoacyl-transfer ribonucleic acid synthetases were measured inSalmonella typhimurium LT-2 and a mutant,ilvA504 . The mutant produced anl -threonine deaminase with a decreased affinity for its cofactor, pyridoxal-5′-monophosphate. The addition of pyridoxal-5′-monophosphate to cultures of strainilvA504 growing in excess isoleucine, valine, and leucine resulted in an increased rate of growth and repression of the synthesis of the isoleucine and valine biosynthetic enzymes. No differences in the rate of synthesis of the branched-chain aminoacyl-transfer ribonucleic acid synthetases were observed in cultures ofilvA504 growing with or without added pyridoxal-5′-monophosphate. The differential rates of synthesis of all three enzymes were similar to the rates measured in strain LT-2. These experiments suggest that different forms of theilvA gene product are involved in the regulation of the branched-chain amino acid biosynthetic enzymes and the branched-chain aminoacyl-transfer ribonucleic acid synthetases.

journal of bacteriology

Synthesis of Branched-Chain Aminoacyl-Transfer Ribonucleic Acid Synthetases in a <i>Salmonella typhimurium</i> Mutant with an Altered Biosynthetic <scp>l</scp> -Threonine Deaminase

Synthesis of Branched-Chain Aminoacyl-Transfer Ribonucleic Acid Synthetases in a Salmonella typhimurium Mutant with an Altered Biosynthetic l -Threonine Deaminase