Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.

Abstract excerpt

The trpB8 mutation of Escherichia coli tryptophan synthase is unique in that the cells bearing this lesion are not only capable of utilizing indole for growth, but they also accumulate indole, under conditions of tryptophan limitation. The lesion was shown by DNA sequencing to be a G to C transversion at nucleotide 5528 of the trp operon, resulting in a Gly to Arg switch at codon 281. Gly-281, within the...

Topics

• Amino Acid Sequence
• Amino Acids
• Ammonia
• Base Sequence
• Catalysis
• Cloning, Molecular
• Computer Simulation
• DNA, Bacterial
• Electrophoresis, Polyacrylamide Gel
• Escherichia coli