Preparation of pyridoxal 5'-phosphate-bound sepharose and its use for immobilization of tryptophanase.
Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes.
Phosphorus 31 nuclear magnetic resonance study of tryptophanase. Pyridoxal phosphate-binding site.
Phosphorus-31 nuclear magnetic resonance studies on four pyridoxal 5'-phosphate dependent enzymes.
Functional role of cysteinyl residues in tryptophanase.
Catalytic function of a tyrosyl residue in tryptophanase.
Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase.
Overproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli.
NMR spectra of exchangeable protons of pyridoxal phosphate-dependent enzymes.
Preliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
Indole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine.
Identification of indigo-related pigments produced by Escherichia coli containing a cloned Rhodococcus gene.
Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents.
Crystallization and preliminary X-ray investigation of holotryptophanases from Escherichia coli and Proteus vulgaris.
Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
Analysis of stability and catalytic properties of two tryptophanases from a thermophile.
Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry.
Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
Although this enzyme binds potassium ion, it is too distant from the active site to be involved in catalysis directly (see [17]). According to the literature [17], this enzyme catalyzes five reactions: (A) Formation of external aldimine (Schiff-base between PLP & substrate amino group), (B) Elimination of indole ring from the external aldimine complex, (C) Addition of water to double-bonded carbon atom (or Hydration), (D) Elimination of imine group from the product, (E) Formation of internal aldimine (Schiff-base between PLP & catalytic lysine).