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

Syed Ashrafuddin Ahmed; Thomas Fairwell; Susan Dunn; Kasper Kirschner; Edith Wilson Miles

doi:10.1021/bi00359a008

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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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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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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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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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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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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[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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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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Scanning calorimetric study of tryptophan synthase α-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid

Thermochimica Acta ◽

10.1016/0040-6031(90)80386-d ◽

1990 ◽

Vol 163 ◽

pp. 117-122 ◽

Cited By ~ 8

Author(s):

Yoshiko Sugisaki ◽

Kyoko Ogasahara ◽

Edith W. Miles ◽

Katsuhide Yutani

Keyword(s):

Escherichia Coli ◽

Salmonella Typhimurium ◽

Calorimetric Study ◽

Tryptophan Synthase ◽

Α Subunits ◽

Interspecies Hybrid

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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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