Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions.

Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38630-1 ◽

1985 ◽

Vol 260 (27) ◽

pp. 14712-14716 ◽

Cited By ~ 7

Author(s):

S F Nowlan ◽

E R Kantrowitz

Keyword(s):

Escherichia Coli ◽

Catalytic Subunit ◽

Pyrimidine Pathway ◽

Rapid Purification

The Uptake of C4-Dicarboxylic Acids by Escherichia coli

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1971.tb01240.x ◽

1971 ◽

Vol 18 (2) ◽

pp. 274-281 ◽

Cited By ~ 74

Author(s):

William W. Kay ◽

Hans L. Kornberg

Keyword(s):

Escherichia Coli ◽

Dicarboxylic Acids

Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41435-x ◽

1975 ◽

Vol 250 (10) ◽

pp. 3571-3583 ◽

Cited By ~ 2

Author(s):

DR Evans ◽

SC Pastra-Landis ◽

WN Lipscomb

Keyword(s):

Escherichia Coli ◽

Partial Dissociation

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 ◽

Carbamyl Phosphate

Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.78.11.6759 ◽

1981 ◽

Vol 78 (11) ◽

pp. 6759-6763 ◽

Cited By ~ 14

Author(s):

M. Lennick ◽

N. M. Allewell

Keyword(s):

Escherichia Coli ◽

Hydrogen Exchange ◽

Exchange Kinetics ◽

Kinetics Of ◽

Effector Binding

Continuous synthesis of partially derepressed aspartate transcarbamylase during the division cycle of Escherichia coli B/r

Journal of Molecular Biology ◽

10.1016/0022-2836(73)90108-3 ◽

1973 ◽

Vol 74 (2) ◽

pp. 223-238 ◽

Cited By ~ 7

Author(s):

Francis L. Bellino

Keyword(s):

Escherichia Coli ◽

Continuous Synthesis ◽

Escherichia Coli B

Carbamoyl phosphate biosynthesis and partition in pyrimidine and arginine pathways of Escherichia coli. In situ properties of carbamoyl-phosphate synthase, ornithine transcarbamylase and aspartate transcarbamylase in permeabilized cells

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1989.tb21080.x ◽

1989 ◽

Vol 183 (3) ◽

pp. 519-528 ◽

Cited By ~ 18

Author(s):

Jean-Pierre ROBIN ◽

Bernadette PENVERNE ◽

Guy HERVE

Keyword(s):

Escherichia Coli ◽

Ornithine Transcarbamylase ◽

Carbamoyl Phosphate ◽

Permeabilized Cells ◽

Phosphate Synthase

Response to the adenylate energy charge by Escherichia coli aspartate transcarbamylase and its catalytic subunit

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(69)90575-0 ◽

1969 ◽

Vol 36 (3) ◽

pp. 381-386 ◽

Cited By ~ 12

Author(s):

William N. Bigler ◽

Daniel E. Atkinson

Keyword(s):

Escherichia Coli ◽

Energy Charge ◽

Catalytic Subunit ◽

Adenylate Energy Charge ◽

Heterotropic interactions in Escherichia coli aspartate transcarbamylase

Journal of Molecular Biology ◽

10.1016/0022-2836(91)90118-p ◽

1991 ◽

Vol 220 (3) ◽

pp. 789-799 ◽

Cited By ~ 20

Author(s):

Xu Guang Xi ◽

Françoise van Vliet ◽

Moncef M. Ladjimi ◽

Bénédicte de Wannemaeker ◽

Christine de Staercke ◽

...

Keyword(s):

Escherichia Coli ◽

Carbon-13 and nitrogen-15 isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase

Biochemistry ◽

10.1021/bi00143a030 ◽

1992 ◽

Vol 31 (28) ◽

pp. 6577-6584 ◽

Cited By ~ 14

Author(s):

Laura E. Parmentier ◽

Paul M. Weiss ◽

M. H. O'Leary ◽

H. K. Schachman ◽

W. W. Cleland

Keyword(s):

Escherichia Coli ◽

Isotope Effects ◽

Chemical Mechanism ◽