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.

H Kawasaki; R Bauerle; G Zon; S A Ahmed; E W Miles

doi:10.1016/s0021-9258(18)61017-8

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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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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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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Aliphatic alcohols stabilize an alternative conformation of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)34032-2 ◽

1994 ◽

Vol 269 (23) ◽

pp. 16486-16492

Author(s):

S.A. Ahmed ◽

E.W. Miles

Keyword(s):

Salmonella Typhimurium ◽

Aliphatic Alcohols ◽

Tryptophan Synthase ◽

Alternative Conformation ◽

Beta 2

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Origin of the mutual activation of the alpha and beta 2 subunits in the alpha 2 beta 2 complex of tryptophan synthase. Effect of alanine or glycine substitutions at proline residues in the alpha subunit.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)42755-x ◽

1992 ◽

Vol 267 (8) ◽

pp. 5222-5228

Author(s):

K Ogasahara ◽

K Hiraga ◽

W Ito ◽

E.W. Miles ◽

K Yutani

Keyword(s):

Alpha Subunit ◽

Tryptophan Synthase ◽

Beta 2

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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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Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb15535.x ◽

1990 ◽

Vol 189 (3) ◽

pp. 667-673 ◽

Cited By ~ 2

Author(s):

Shintaro SAWADA ◽

Hideo AKUTSU ◽

Kyoko OGASAHARA ◽

Katsuhide YUTANI

Keyword(s):

1H Nmr ◽

Conformational Changes ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Nmr Spectrum

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Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)77913-7 ◽

1988 ◽

Vol 263 (33) ◽

pp. 17857-17871

Author(s):

C C Hyde ◽

S A Ahmed ◽

E A Padlan ◽

E W Miles ◽

D R Davies

Keyword(s):

Salmonella Typhimurium ◽

Three Dimensional ◽

Dimensional Structure ◽

Tryptophan Synthase ◽

Multienzyme Complex ◽

Three Dimensional Structure ◽

Beta 2

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Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)83682-7 ◽

1985 ◽

Vol 260 (6) ◽

pp. 3716-3718

Author(s):

S A Ahmed ◽

E W Miles ◽

D R Davies

Keyword(s):

Salmonella Typhimurium ◽

Crystallographic Data ◽

Tryptophan Synthase ◽

X Ray ◽

Beta 2

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The tryptophan synthase alpha 2 beta 2 complex. Cleavage of a flexible loop in the alpha subunit alters allosteric properties

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)99073-3 ◽

1991 ◽

Vol 266 (17) ◽

pp. 10715-10718

Author(s):

E.W. Miles

Keyword(s):

Alpha Subunit ◽

Tryptophan Synthase ◽

Flexible Loop ◽

Beta 2 ◽

Allosteric Properties

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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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