Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis.
Strains of Escherichia coli that lack the branched-chain amino acid amino-transferase because of mutations in the ilvE gene had no growth requirement for leucine when the cells contained the aromatic amino acid aminotransferase that is the product of the tyrB gene. The presence of leucine increased the generation time of these cells and decreased the specific activity of the aromatic amino acid aminotransferase. It is concluded that this enzyme functions efficiently in leucine biosynthesis and can be repressed by leucine as well as by tyrosine.
D002208:Caproates / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D007930:Leucine / Q000096:biosynthesis*; D000637:Transaminases / Q000378:metabolism*; D014443:Tyrosine
D002208:Caproates; D014443:Tyrosine; D000637:Transaminases; D007930:Leucine