Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

P.S. Brzović; Y Sawa; C.C. Hyde; E.W. Miles; M.F. Dunn

doi:10.1016/s0021-9258(18)42377-0

Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)42377-0 ◽

1992 ◽

Vol 267 (18) ◽

pp. 13028-13038

Author(s):

P.S. Brzović ◽

Y Sawa ◽

C.C. Hyde ◽

E.W. Miles ◽

M.F. Dunn

Keyword(s):

Alpha Subunit ◽

Tryptophan Synthase ◽

Closed Conformation ◽

Loop Region

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Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)68348-6 ◽

1988 ◽

Vol 263 (18) ◽

pp. 8611-8614 ◽

Cited By ~ 4

Author(s):

E W Miles ◽

P McPhie ◽

K Yutani

Keyword(s):

Glutamic Acid ◽

Beta Subunit ◽

Alpha Subunit ◽

Catalytic Residue ◽

Tryptophan Synthase ◽

Mutant Proteins

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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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Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the .alpha. subunit of tryptophan synthase

Biochemistry ◽

10.1021/bi00123a002 ◽

1992 ◽

Vol 31 (8) ◽

pp. 2219-2223 ◽

Cited By ~ 10

Author(s):

Xiaowu Chen ◽

Robert Rambo ◽

C. Robert Matthews

Keyword(s):

Amino Acid ◽

Interaction Energy ◽

Alpha Subunit ◽

Tryptophan Synthase

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Long-Range Interactions in the Alpha Subunit of Tryptophan Synthase Help to Coordinate Ligand Binding, Catalysis, and Substrate Channeling

Journal of Molecular Biology ◽

10.1016/j.jmb.2013.01.030 ◽

2013 ◽

Vol 425 (9) ◽

pp. 1527-1545 ◽

Cited By ~ 28

Author(s):

Jennifer M. Axe ◽

David D. Boehr

Keyword(s):

Ligand Binding ◽

Long Range ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Substrate Channeling ◽

Long Range Interactions

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Effect of single amino acid substitutions on the thermal stability of the .alpha. subunit of tryptophan synthase

Biochemistry ◽

10.1021/bi00548a004 ◽

1980 ◽

Vol 19 (7) ◽

pp. 1290-1293 ◽

Cited By ~ 43

Author(s):

C. R. Matthews ◽

M. M. Crisanti ◽

G. L. Gepner ◽

G. Velicelebi ◽

J. M. Sturtevant

Keyword(s):

Thermal Stability ◽

Amino Acid ◽

Alpha Subunit ◽

Single Amino Acid ◽

Amino Acid Substitutions ◽

Tryptophan Synthase ◽

Thermal Stability Of

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Characterization of the functional role of a flexible loop in the .alpha.-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis

Biochemistry ◽

10.1021/bi00090a016 ◽

1993 ◽

Vol 32 (39) ◽

pp. 10404-10413 ◽

Cited By ~ 40

Author(s):

Peter S. Brzovic ◽

C. Craig Hyde ◽

Edith W. Miles ◽

Michael F. Dunn

Keyword(s):

Functional Role ◽

Site Directed Mutagenesis ◽

Alpha Subunit ◽

Directed Mutagenesis ◽

Stopped Flow ◽

Tryptophan Synthase ◽

Flexible Loop ◽

Rapid Scanning

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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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