▪ Abstract The three-dimensional structures of tryptophan synthase, carbamoyl phosphate
synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine …

As a result of recent advances in molecular cloning, protein expression, and X-ray
crystallography, it has now become feasible to examine complicated protein structures at …

Tryptophan synthase, an alpha 2 beta 2 complex, is a classic example of an enzyme that is
thought to “channel” a metabolic intermediate (indole) from the active site of the alpha …

Revised Manuscript Received April 18, 1995® abstract: Monovalent cations affect both
conformational and catalytic properties of the tryptophan synthase, complex from Salmonella …

Tryptophan synthase is a classic enzyme that channels a metabolic intermediate, indole.
The crystal structure of the tryptophan synthase α2β2 complex from Salmonella typhimurium …

The amidotransferase family of enzymes utilizes the ammonia derived from the hydrolysis of
glutamine for a subsequent chemical reaction catalyzed by the same enzyme. The ammonia …

Substrate channeling is the process of direct transfer of an intermediate between the active
sites of two enzymes that catalyze sequential reactions in a biosynthetic pathway (for …

The α 2 β 2 form of the tryptophan synthase bienzyme complex catalyses the last two steps
in the synthesis of l-tryptophan, consecutive processes that depend on the channeling of the …

Tryptophan synthase (EC 4.2. 1.20) from bacteria, yeasts, molds, and plants catalyzes the
final two reactions in the biosynthesis of L-tryptophan. This enzyme has been the subject of …

Two important questions in modern biochemistry are how different proteins interact and how
protein-protein interaction regulates enzymatic activity. The bacterial tryptophan synthase α …