Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.
Open Access
- 1 November 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (32), 21548-21557
- https://doi.org/10.1016/s0021-9258(18)54673-1
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Schiff bases and geminal diamines derived from pyridoxal 5'-phosphate and diaminesJournal of the American Chemical Society, 1989
- Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of .beta.-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanismBiochemistry, 1984
- The Accessibility of the Active Site and Conformation States of the β2 Subunit of Tryptophan Synthase Studied by Fluorescence QuenchingEuropean Journal of Biochemistry, 1983
- The Catalytic Mechanism of Tryptophan Synthase from Escherichia coliEuropean Journal of Biochemistry, 1983
- Small‐Angle X‐Ray Scattering Studies of Tryptophan Synthase from Escherichia coli and Its α and β2 SubunitsEuropean Journal of Biochemistry, 1982
- Equilibriums and absorption spectra of Schiff basesJournal of the American Chemical Society, 1980
- Subunit interaction in tryptophan synthase of Escherichia coli: calorimetric studies on association of .alpha. and .beta.2 subunitsBiochemistry, 1979
- A new type of pyridoxal-p enzyme catalyzed reaction: The conversion of β, γ-unsaturated amino acids to saturated α-keto acids by tryptophan synthaseBiochemical and Biophysical Research Communications, 1975
- Effects of modification of the β2 subunit and of the α2β2 complex of tryptophan synthase by α-cyanoglycine, a substrate analogBiochemical and Biophysical Research Communications, 1975
- The 8 protein of Escherichia coli tryptophan synthetase II. New β-elimination and β-replacement reactionsBiochemical and Biophysical Research Communications, 1971