Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analogs

Juerg Tschopp; Kasper Kirschner

doi:10.1021/bi00560a020

Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analogs

Biochemistry ◽

10.1021/bi00560a020 ◽

1980 ◽

Vol 19 (19) ◽

pp. 4514-4521 ◽

Cited By ~ 50

Author(s):

Juerg Tschopp ◽

Kasper Kirschner

Keyword(s):

Escherichia Coli ◽

Pyridoxal Phosphate ◽

Tryptophan Synthase ◽

Binding Studies ◽

Subunit Interactions

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Affinity labeling of the pyridoxal phosphate binding site of the beta2 subunit of Escherichia coli tryptophan synthase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)30438-6 ◽

1978 ◽

Vol 253 (13) ◽

pp. 4648-4652

Author(s):

W. Higgins ◽

E.W. Miles

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Pyridoxal Phosphate ◽

Affinity Labeling ◽

Tryptophan Synthase ◽

Phosphate Binding

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The Tryptophan Synthase from Escherichia coli. An Improved Purification Procedure for the alpha-Subunit and Binding Studies with Substrate Analogues

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1975.tb21030.x ◽

1975 ◽

Vol 60 (2) ◽

pp. 513-523 ◽

Cited By ~ 107

Author(s):

Kasper KIRSCHNER ◽

Robert L. WISKOCIL ◽

Martha FOEHN ◽

Laurel REZEAU

Keyword(s):

Escherichia Coli ◽

Alpha Subunit ◽

Tryptophan Synthase ◽

Purification Procedure ◽

Binding Studies ◽

Substrate Analogues

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Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)41802-3 ◽

1994 ◽

Vol 269 (6) ◽

pp. 4467-4472

Author(s):

C. Tang ◽

S. Wilkens ◽

R.A. Capaldi

Keyword(s):

Escherichia Coli ◽

Trypsin Digestion ◽

Binding Studies ◽

Gamma Subunit ◽

F1 Atpase

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Receptor Binding Studies Disclose a Novel Class of High-Affinity Inhibitors of the Escherichia Coli FimH Adhesin

The Journal of Urology ◽

10.1016/s0022-5347(01)68545-8 ◽

2005 ◽

Vol 174 (3) ◽

pp. 1150-1150

Author(s):

Timothy L. Ratliff

Keyword(s):

Escherichia Coli ◽

Receptor Binding ◽

Binding Studies ◽

High Affinity

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Sequence similarities between tryptophan synthase β subunit and other pyridoxal-phosphate-dependent enzymes

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(90)90830-g ◽

1990 ◽

Vol 171 (3) ◽

pp. 1319-1325 ◽

Cited By ~ 14

Author(s):

Peer Bork ◽

Klaus Rohde

Keyword(s):

Pyridoxal Phosphate ◽

Tryptophan Synthase ◽

Β Subunit ◽

Sequence Similarities

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Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies

Biochemistry ◽

10.1021/bi00489a018 ◽

1990 ◽

Vol 29 (37) ◽

pp. 8620-8627 ◽

Cited By ~ 26

Author(s):

Donald W. Pettigrew ◽

Gui Ju Yu ◽

Youguo Liu

Keyword(s):

Escherichia Coli ◽

Initial Velocity ◽

Substrate Binding ◽

Glycerol Kinase ◽

Binding Studies ◽

Nucleotide Regulation

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Topology of Binding Sites for Carbamyl Phosphate in Aspartate Transcarbamylase from Escherichia coli. The Use of Pyridoxal Phosphate as Covalent Probe

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1975.tb04139.x ◽

1975 ◽

Vol 54 (1) ◽

pp. 293-299 ◽

Cited By ~ 13

Author(s):

Peter SUTER ◽

Jurg P. ROSENBUSCH

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Pyridoxal Phosphate ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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Crystallographic and kinetic studies of the tryptophan synthase α2β2 complex with a mutation in β subunit lysine-87 that binds pyridoxal phosphate

Biochemistry of Vitamin B6 and PQQ ◽

10.1007/978-3-0348-7393-2_18 ◽

1994 ◽

pp. 113-117 ◽

Cited By ~ 3

Author(s):

E. W. Miles ◽

U. Banik ◽

Z. Lu ◽

S. A. Ahmed ◽

K. D. Parris ◽

...

Keyword(s):

Pyridoxal Phosphate ◽

Kinetic Studies ◽

Tryptophan Synthase ◽

Β Subunit

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THE CONVERSION OF PYRIDOXINE PHOSPHATE INTO PYRIDOXAL PHOSPHATE IN ESCHERICHIA COLI

Biochemical Journal ◽

10.1042/bj0950775 ◽

1965 ◽

Vol 95 (3) ◽

pp. 775-779 ◽

Cited By ~ 9

Author(s):

HM HENDERSON

Keyword(s):

Escherichia Coli ◽

Pyridoxal Phosphate

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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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