Substrate binding properties of mutant and wild-type A proteins of Escherichia coli tryptophan synthetase.
Most of the mutant A proteins studied appear to be similar to the normal enzyme both in their apparent conformation about the critical cysteine residues and their ability to bind substrate. Two mutant proteins, in which a glutamic acid or arginine residue is substituted for a glycine residue, do appear abnormal suggesting that these primary structural changes radically affect the conformation in regions at or near the site or sites of substrate binding.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003545:Cysteine; D004926:Escherichia coli; D005033:Ethylmaleimide; D005827:Genetics, Microbial; D005994:Glycerophosphates; D006836:Hydro-Lyases; D007461:Iodoacetates; D009154:Mutation; D009876:Operon; D011485:Protein Binding; D014364:Tryptophan
D001426:Bacterial Proteins; D005994:Glycerophosphates; D007461:Iodoacetates; D014364:Tryptophan; D006836:Hydro-Lyases; D003545:Cysteine; D005033:Ethylmaleimide