5-Azidoindole binding to the Escherichia coli tryptophan synthase α2β2 complex

[1]  E. W. Miles.  Tryptophan synthase: structure, function, and subunit interaction. , 2006 .

[2]  A. Lane,et al.  The catalytic mechanism of tryptophan synthase from Escherichia coli. Kinetics of the reaction of indole with the enzyme--L-serine complexes. , 2005, European journal of biochemistry.

[3]  A. Lane,et al.  The mechanism of binding of L-serine to tryptophan synthase from Escherichia coli. , 2005, European journal of biochemistry.

[4]  D. Baker,et al.  Photoaffinity labeling of the indole sites on the Escherichia coli tryptophan synthase α-subunit☆ , 1983 .

[5]  H. Heilmann.  On the mechanism of action of Escherichia coli tryptophan synthase. Steady-state investigations. , 1978, Biochimica et biophysica acta.

[6]  M. Moriguchi,et al.  Tryptophan synthase of Escherichia coli. Removal of pyridoxal 5'-phosphate and separation of the alpha and beta2 subunits. , 1977, The Journal of biological chemistry.

[7]  J. Murphy,et al.  Substrate interactions with the alpha-subunit of the Escherichia coli tryptophan synthase. A kinetic study of the wild-type alpha-subunit. , 1977, Archives of biochemistry and biophysics.

[8]  W. Weischet,et al.  The mechanism of the synthesis of indoleglycerol phosphate catalyzed by tryptophan synthase from Escherichia coli. Steady-state kinetic studies. , 1976, European journal of biochemistry.

[9]  W. Weischet,et al.  The Binding of Indole to the α‐Subunit and β2‐Subunit and to the α2β2‐Complex of Tryptophan Synthase from Escherichia coli , 1976 .

[10]  W. Weischet,et al.  Circular dichroism and fluorescence studies on the binding of ligands to the alpha subunit of tryptophan synthase. , 1975, Biochemistry.

[11]  O. Adachi,et al.  Crystalline α2β2 Complexes of Tryptophan Synthetase of Escherichia coli A COMPARISON BETWEEN THE NATIVE COMPLEX AND THE RECONSTITUTED COMPLEX , 1974 .

[12]  G. Hammes,et al.  Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme. , 1971, Biochemistry.

[13]  E. W. Miles.  The B protein of Escherichia coli tryptophan synthetase. I. Effects of sulfhydryl modification on enzymatic activities and subunit interaction. , 1970, The Journal of biological chemistry.

[14]  T. Creighton.  A steady-state kinetic investigation of the reaction mechanism of the tryptophan synthetase of Escherichia coli. , 1970, European journal of biochemistry.

[15]  C. Yanofsky,et al.  AN IMMUNOLOGICAL STUDY OF MUTANTS OF ESCHERICHIA COLI LACKING THE ENZYME TRYPTOPHAN SYNTHETASE , 1957, Journal of bacteriology.