Conformational effects of ligand binding on the .beta.2 subunit of Escherichia coli tryptophan-synthase analyzed with monoclonal antibodies

Lisa Djavadi-Ohaniance; Bertrand Friguet; Michel E. Goldberg

doi:10.1021/bi00357a033

Conformational effects of ligand binding on the .beta.2 subunit of Escherichia coli tryptophan-synthase analyzed with monoclonal antibodies

Biochemistry ◽

10.1021/bi00357a033 ◽

1986 ◽

Vol 25 (9) ◽

pp. 2502-2508 ◽

Cited By ~ 33

Author(s):

Lisa Djavadi-Ohaniance ◽

Bertrand Friguet ◽

Michel E. Goldberg

Keyword(s):

Escherichia Coli ◽

Monoclonal Antibodies ◽

Ligand Binding ◽

Tryptophan Synthase ◽

Conformational Effects ◽

Beta 2

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Mechanism of inactivation of the beta 2 subunit of Escherichia coli tryptophan synthase by monoclonal antibodies.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)39028-3 ◽

1990 ◽

Vol 265 (14) ◽

pp. 7987-7993

Author(s):

A Murry-Brelier ◽

M E Goldberg

Keyword(s):

Escherichia Coli ◽

Monoclonal Antibodies ◽

Tryptophan Synthase ◽

Beta 2

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Conformational change in the N-terminal domain of the Escherichia coli tryptophan synthase β2 subunit induced by its interactions with monoclonal antibodies

Research in Immunology ◽

10.1016/0923-2494(90)90187-4 ◽

1990 ◽

Vol 141 (9) ◽

pp. 879-892 ◽

Cited By ~ 1

Author(s):

S Blond-Elguindi ◽

M.E Goldberg

Keyword(s):

Escherichia Coli ◽

Monoclonal Antibodies ◽

Conformational Change ◽

Tryptophan Synthase ◽

Terminal Domain

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Conformational change in the N-terminal domain of the Escherichia coli tryptophan synthase β2 subunit induced by its interactions with monoclonal antibodies

Research in Immunology ◽

10.1016/0923-2494(90)90044-y ◽

1990 ◽

Vol 141 (8) ◽

pp. 879-892 ◽

Cited By ~ 6

Author(s):

S. Blond-Elguindi ◽

M.E. Goldberg

Keyword(s):

Escherichia Coli ◽

Monoclonal Antibodies ◽

Conformational Change ◽

Tryptophan Synthase ◽

Terminal Domain

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Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the .beta.2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimurium

Biochemistry ◽

10.1021/bi00359a008 ◽

1986 ◽

Vol 25 (11) ◽

pp. 3118-3124 ◽

Cited By ~ 22

Author(s):

Syed Ashrafuddin Ahmed ◽

Thomas Fairwell ◽

Susan Dunn ◽

Kasper Kirschner ◽

Edith Wilson Miles

Keyword(s):

Escherichia Coli ◽

Salmonella Typhimurium ◽

Proteolytic Cleavage ◽

Hinge Region ◽

Tryptophan Synthase ◽

Beta 2

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Structural and functional influence of enzyme-antibody interactions: effects of eight different monoclonal antibodies on the enzymatic activity of Escherichia coli tryptophan synthase

Biochemistry ◽

10.1021/bi00296a016 ◽

1984 ◽

Vol 23 (1) ◽

pp. 97-104 ◽

Cited By ~ 62

Author(s):

Lisa Djavadi-Ohaniance ◽

Bertrand Friguet ◽

Michel E. Goldberg

Keyword(s):

Escherichia Coli ◽

Monoclonal Antibodies ◽

Enzymatic Activity ◽

Tryptophan Synthase ◽

Antibody Interactions

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Immunochemical evidence for conformational flexibility and its modulation by specific ligands in the .beta.2 subunit of Escherichia coli tryptophan synthase

Biochemistry ◽

10.1021/bi00280a019 ◽

1983 ◽

Vol 22 (11) ◽

pp. 2708-2714 ◽

Cited By ~ 14

Author(s):

Alain F. Chaffotte ◽

Michel E. Goldberg

Keyword(s):

Escherichia Coli ◽

Conformational Flexibility ◽

Tryptophan Synthase ◽

Beta 2

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Conformational and ligand binding properties of the isolated domains from the beta 2 subunit of Escherichia coli tryptophan synthetase investigated by the reactivity of their cysteines.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)36011-3 ◽

1979 ◽

Vol 254 (16) ◽

pp. 7752-7757

Author(s):

M.E. Goldberg ◽

A. Högberg-Raibaud

Keyword(s):

Escherichia Coli ◽

Ligand Binding ◽

Binding Properties ◽

Beta 2 ◽

Tryptophan Synthetase

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L-Serine binds to arginine-148 of the .beta.2 subunit of Escherichia coli tryptophan synthase

Biochemistry ◽

10.1021/bi00284a009 ◽

1983 ◽

Vol 22 (15) ◽

pp. 3594-3603 ◽

Cited By ~ 20

Author(s):

Katsuyuki Tanizawa ◽

Edith Wilson Miles

Keyword(s):

Escherichia Coli ◽

Tryptophan Synthase ◽

Beta 2

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Influence of cofactor pyridoxal 5'-phosphate on reversible high-pressure denaturation of isolated .beta.2 dimer of tryptophan synthase bienzyme complex from Escherichia coli

Biochemistry ◽

10.1021/bi00323a016 ◽

1985 ◽

Vol 24 (2) ◽

pp. 339-345 ◽

Cited By ~ 24

Author(s):

Thomas Seifert ◽

Peter Bartholmes ◽

Rainer Jaenicke

Keyword(s):

Escherichia Coli ◽

High Pressure ◽

Tryptophan Synthase ◽

Beta 2

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The role of the hinge region of the beta 2-subunit in beta-replacement specificity of tryptophan synthase from Escherichia coli. Analysis of proteolytically modified beta species cleaved by endoproteinase Glu-C

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)36951-x ◽

1994 ◽

Vol 269 (13) ◽

pp. 9783-9789

Author(s):

H.J. Linkens ◽

P. Bartholmes ◽

M. Kaufmann

Keyword(s):

Escherichia Coli ◽

Hinge Region ◽

Tryptophan Synthase ◽

Beta Species ◽

Beta 2

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