Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
- 1 May 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (9) , 2494-2501
- https://doi.org/10.1021/bi00357a032
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 15 references indexed in Scilit:
- Stereochemistry of sodium borohydride reduction of tryptophan synthase of Escherichia coli and its amino acid Schiff's bases.Journal of Biological Chemistry, 1982
- The Mechanism of Tryptophan Binding to Tryptophan Synthase from Escherichia coliEuropean Journal of Biochemistry, 1981
- Kinetics of pH-dependent interconversion of tryptophanase spectral forms studied by scanning stopped-flow spectrophotometryBiochemistry, 1981
- Equilibrium and kinetic study of interaction of amino acid inhibitors with tryptophanase: mechanism of quinonoid formationBiochemistry, 1981
- Dependency on Serine Concentration of the Activity of Tryptophan Synthase. Cooperative PropertiesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- Kinetics of cooperative ligand binding to the apo.beta.2 subunit of tryptophan synthase and its modulation by the .alpha. subunitBiochemistry, 1980
- Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analogsBiochemistry, 1980
- On the mechanism of action of Escherichia coli tryptophan synthase Steady-state investigationsBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- The Mechanism of the Synthesis of Indoleglycerol Phosphate Catalyzed by Tryptophan Synthase from Escherichia coli. Steady-State Kinetic StudiesEuropean Journal of Biochemistry, 1976
- Interactions between the Subunits of the Tryptophan Synthetase of Escherichia coli. Optical Properties of an Intermediate Bound to the α2β2 Complex*Biochemistry, 1967