Escherichia coli mutant trpA34 has an Asp----Asn change at active site residue 60 of the tryptophan synthetase alpha chain.

Article

Escherichia coli mutant trpA34 has an Asp----Asn change at active site residue 60 of the tryptophan synthetase alpha chain.

The Journal of biological chemistry - 25 Apr 1990

Shirvanee L, Horn V, Yanofsky C

Abstract excerpt

Asp-60 is believed to be a catalytically essential residue of the tryptophan synthetase alpha chain of Escherichia coli (Nagata, S., Hyde, C.C., and Miles, E.W. (1989) J. Biol. Chem. 264, 6288-6296). Surprisingly, mutations altering Asp-60 were not observed in the many trpA missense mutants chara...

Topics

Asparagine
Aspartic Acid
Base Sequence
Binding Sites
Codon
DNA, Bacterial
Escherichia coli
Molecular Sequence Data
Mutation
Oligonucleotide Probes
Plasmids
Tryptophan Synthase

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.