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Modification of histidyl residues in proteins by diethylpyrocarbonate.
  • E. W. Miles
  • Chemistry, Medicine
    Methods in enzymology
  • 1977
Although diethylpyrocarbonate does not always react specifically with histidyl residues in proteins, it is more selective than other acylating agents and can give useful information about the role of histidol residues in many proteins.
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
The three-dimensional structure of the alpha 2 beta 2 complex of tryptophan synthase from Salmonella typhimurium has been determined by x-ray crystallography at 2.5 A resolution. The four polypeptide
The Molecular Basis of Substrate Channeling*
A comparison of the structural and kinetic results reveals that these enzymes frequently exhibit allosteric interactions that synchronize the reactions to prevent the build-up of excess intermediate (12–16).
Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.
Three-dimensional structures are reported for a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with either the substrate L-serine (betaK87T-Ser) or product L-tryptophan (betaK87T-Trp) at
Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.
Refined crystal structures of the tryptophan synthase alpha2beta2 complex from Salmonella typhimurium in the presence of K+ and Cs+ provide a structural basis for understanding the effects of cations on activity and intersubunit communication.
Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.
The combined results show that the switching of the enzyme between open and closed conformations couples the catalytic reactions at the alpha and beta active sites and prevents the escape of indole.
The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper
It is concluded that the restoration of alpha subunit activity in the doubly altered second-site revertant results from restoration of the proper geometry of the substrate binding site.
Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism.
The kinetics of substrate channeling by tryptophan synthase is examined directly by chemical quench-flow and stopped-flow methods and shows that the reaction of serine at the beta site modulates the alpha reaction such that the formation of the aminoacrylate leads to a change in protein conformation that is transmitted to the alpha site to enhance the rate of IGP cleavage 150-fold.