Folding of homologous proteins: Conservation of the folding mechanism of the .alpha. subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrides

Thomas Stackhouse; James J. Onuffer; C. Robert Matthews; Syed A. Ahmed; Edith W. Miles

doi:10.1021/bi00402a050

Folding of homologous proteins: Conservation of the folding mechanism of the .alpha. subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrides

Biochemistry ◽

10.1021/bi00402a050 ◽

1988 ◽

Vol 27 (2) ◽

pp. 824-832 ◽

Cited By ~ 23

Author(s):

Thomas Stackhouse ◽

James J. Onuffer ◽

C. Robert Matthews ◽

Syed A. Ahmed ◽

Edith W. Miles

Keyword(s):

Escherichia Coli ◽

Salmonella Typhimurium ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Homologous Proteins ◽

Folding Mechanism

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Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)61017-8 ◽

1987 ◽

Vol 262 (22) ◽

pp. 10678-10683 ◽

Cited By ~ 8

Author(s):

H Kawasaki ◽

R Bauerle ◽

G Zon ◽

S A Ahmed ◽

E W Miles

Keyword(s):

Salmonella Typhimurium ◽

Conformational Changes ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Site Specific ◽

Beta 2

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Probing the Role of Position 49 in the Folding of the Alpha Subunit of Tryptophan Synthase from Escherichia Coli

Current Research in Protein Chemistry ◽

10.1016/b978-0-12-721955-4.50032-4 ◽

1990 ◽

pp. 295-300

Author(s):

Boris A. Chrunyk ◽

C. Robert Matthews

Keyword(s):

Escherichia Coli ◽

Alpha Subunit ◽

Tryptophan Synthase

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Steady-State Kinetic Studies of the Synthesis of Indoleglycerol Phosphate Catalyzed by the alpha Subunit of Tryptophan Synthase from Escherichia coli. Comparison with the alpha2beta2-Complex

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1976.tb10351.x ◽

1976 ◽

Vol 65 (2) ◽

pp. 375-385 ◽

Cited By ~ 35

Author(s):

Wolfgang O. WEISCHET ◽

Kasper KIRSCHNER

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Studies ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Steady State Kinetic ◽

State Kinetic

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On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase from Salmonella typhimurium and BX1 from Maize, Two Evolutionarily Related Enzymes

Journal of Molecular Biology ◽

10.1016/j.jmb.2005.07.014 ◽

2005 ◽

Vol 352 (3) ◽

pp. 608-620 ◽

Cited By ~ 27

Author(s):

Victor Kulik ◽

Elisabeth Hartmann ◽

Michael Weyand ◽

Monika Frey ◽

Alfons Gierl ◽

...

Keyword(s):

Salmonella Typhimurium ◽

Catalytic Mechanism ◽

Alpha Subunit ◽

Structural Basis ◽

Tryptophan Synthase

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The Binding of Indole to the alpha-Subunit and beta2-Subunit and to the alpha2beta2-Complex of Tryptophan Synthase from Escherichia coli. Identification of a Second Indole-Binding Site on the alpha-Subunit

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1976.tb10303.x ◽

1976 ◽

Vol 64 (1) ◽

pp. 313-320 ◽

Cited By ~ 25

Author(s):

Wolfgang O. WEISCHET ◽

Kasper KIRSCHNER

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Alpha Subunit ◽

Tryptophan Synthase

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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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Effects of the phenylalanine-22 .fwdarw. leucine, glutamic acid-49 .fwdarw. methionine, glycine-234 .fwdarw. aspartic acid and glycine-234 .fwdarw. lysine mutations on the folding and stability of the .alpha. subunit of tryptophan synthase from Escherichia coli

Biochemistry ◽

10.1021/bi00358a035 ◽

1986 ◽

Vol 25 (10) ◽

pp. 2965-2974 ◽

Cited By ~ 88

Author(s):

A. M. Beasty ◽

M. R. Hurle ◽

J. T. Manz ◽

T. Stackhouse ◽

J. J. Onuffer ◽

...

Keyword(s):

Escherichia Coli ◽

Glutamic Acid ◽

Aspartic Acid ◽

Alpha Subunit ◽

Tryptophan Synthase

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[49] Tryptophan synthase from Escherichia coli and Salmonella typhimurium

Methods in Enzymology - Metabolism of Aromatic Amino Acids and Amines ◽

10.1016/s0076-6879(87)42051-x ◽

1987 ◽

pp. 398-414 ◽

Cited By ~ 92

Author(s):

Edith Wilson Miles ◽

Ronald Bauerle ◽

Syed Ashrafuddin Ahmed

Keyword(s):

Escherichia Coli ◽

Salmonella Typhimurium ◽

Tryptophan Synthase

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A single amino acid switch within the “hinge” region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)82421-8 ◽

1993 ◽

Vol 268 (20) ◽

pp. 14921-14931 ◽

Cited By ~ 1

Author(s):

G.P. Zhao ◽

R.L. Somerville

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Hinge Region ◽

Beta Subunit ◽

Alpha Subunit ◽

Single Amino Acid ◽

Tryptophan Synthase

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Faculty Opinions recommendation of On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1028162.336035 ◽

2005 ◽

Author(s):

Reinhard Sterner

Keyword(s):

Salmonella Typhimurium ◽

Catalytic Mechanism ◽

Alpha Subunit ◽

Structural Basis ◽

Tryptophan Synthase

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